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***  4O035EDM  ***

elNémo ID: 220317070618104167

Job options:

ID        	=	 220317070618104167
JOBID     	=	 4O035EDM
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 4O035EDM

HEADER    HYDROLASE                               13-DEC-13   4O03              
TITLE     CRYSTAL STRUCTURE OF CA2+ BOUND PROTHROMBIN DELETION MUTANT RESIDUES  
TITLE    2 146-167                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTHROMBIN;                                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.4.21.5;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: F2;                                                            
SOURCE   6 EXPRESSION_SYSTEM: CRICETINAE;                                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10026;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL: BABY HAMSTER KIDNEY (BHK)                    
KEYWDS    PROTHROMBIN, KRINGLE, SERINE PROTEASE, COAGULATION, HYDROLASE         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.POZZI,Z.CHEN,D.B.SHROPSHIRE,L.A.PELC,E.DI CERA                      
REVDAT   4   29-JUL-20 4O03    1       COMPND REMARK HETNAM LINK                
REVDAT   4 2                   1       SITE                                     
REVDAT   3   23-AUG-17 4O03    1       SOURCE REMARK                            
REVDAT   2   25-JUN-14 4O03    1       JRNL                                     
REVDAT   1   21-MAY-14 4O03    0                                                
JRNL        AUTH   N.POZZI,Z.CHEN,L.A.PELC,D.B.SHROPSHIRE,E.DI CERA             
JRNL        TITL   THE LINKER CONNECTING THE TWO KRINGLES PLAYS A KEY ROLE IN   
JRNL        TITL 2 PROTHROMBIN ACTIVATION.                                      
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 111  7630 2014              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   24821807                                                     
JRNL        DOI    10.1073/PNAS.1403779111                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.HUANG,A.C.RIGBY,X.MORELLI,M.A.GRANT,G.HUANG,B.FURIE        
REMARK   1  TITL   STRUCTURAL BASIS OF MEMBRANE BINDING BY GLA DOMAINS OF       
REMARK   1  TITL 2 VITAMIN K-DEPENDENT PROTEINS.                                
REMARK   1  REF    NAT.STRUCT.MOL.BIOL.          V.  10   751 2003              
REMARK   1  REFN                   ISSN 1545-9993                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.38 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.38                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.75                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : -0.700                         
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 15753                          
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) : 0.235                           
REMARK   3   R VALUE            (WORKING SET) : 0.233                           
REMARK   3   FREE R VALUE                     : 0.279                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 835                             
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) : 3.38                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 985                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 80.26                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3380                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 48                           
REMARK   3   BIN FREE R VALUE                    : 0.3780                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4321                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 47                                      
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) : 73.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.22000                                              
REMARK   3    B22 (A**2) : -0.05000                                             
REMARK   3    B33 (A**2) : -0.17000                                             
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): 0.515         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.430         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 26.650        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.874                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.813                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4483 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6093 ; 1.650 ; 1.959       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   537 ; 8.397 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   232 ;40.199 ;24.181       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   733 ;23.777 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    35 ;20.261 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   630 ; 0.113 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3505 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  2679 ; 0.639 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4312 ; 1.196 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1804 ; 1.148 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1781 ; 2.040 ; 4.500       
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   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   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4O03 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JAN-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000083872.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-JUN-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : MIRROR                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16635                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.380                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -0.700                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : 0.12800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 6.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.38                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.46                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP FROM CCP4                                      
REMARK 200 STARTING MODEL: PDB ENTRY 4NZQ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 75.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.92                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES, PH 7.5, 10% PEG 4000 AND   
REMARK 280  5% ISOPROPANOL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        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       88.72950            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.71550            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       88.72950            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       44.71550            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (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     THR A   256                                                      
REMARK 465     GLY A   257                                                      
REMARK 465     ASP A   258                                                      
REMARK 465     GLY A   259                                                      
REMARK 465     LEU A   260                                                      
REMARK 465     ASP A   261                                                      
REMARK 465     GLU A   262                                                      
REMARK 465     ASP A   263                                                      
REMARK 465     SER A   264                                                      
REMARK 465     ASP A   265                                                      
REMARK 465     ARG A   266                                                      
REMARK 465     ALA A   267                                                      
REMARK 465     ILE A   268                                                      
REMARK 465     GLU A   269                                                      
REMARK 465     GLY A   270                                                      
REMARK 465     ARG A   271                                                      
REMARK 465     THR A   272                                                      
REMARK 465     ALA A   273                                                      
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     ARG A  54    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LEU A   5   C     CGU A   6   N       0.161                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A   5   O   -  C   -  N   ANGL. DEV. =  10.0 DEGREES          
REMARK 500    CYS A  65   CA  -  CB  -  SG  ANGL. DEV. =   7.6 DEGREES          
REMARK 500    CYS A 170   CA  -  CB  -  SG  ANGL. DEV. =   8.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A   3       77.42    -55.42                                   
REMARK 500    PHE A   4     -108.59     58.51                                   
REMARK 500    LEU A   5      -86.79    -56.62                                   
REMARK 500    CGU A   6        7.09      7.56                                   
REMARK 500    SER A  33      150.75    137.48                                   
REMARK 500    SER A  34       34.82    -98.35                                   
REMARK 500    THR A  35       81.64    -62.02                                   
REMARK 500    ASP A  38      -85.92    150.42                                   
REMARK 500    TYR A  44      -72.46    -78.19                                   
REMARK 500    THR A  49        5.17    -56.47                                   
REMARK 500    ARG A  51       -0.91   -165.25                                   
REMARK 500    THR A  52     -152.47    -79.72                                   
REMARK 500    PRO A  53     -170.59    -68.29                                   
REMARK 500    ARG A  54      -37.44    -39.03                                   
REMARK 500    THR A  71       22.26    -77.29                                   
REMARK 500    ARG A  74       48.14   -141.72                                   
REMARK 500    SER A 101       46.05    -88.85                                   
REMARK 500    THR A 102      -41.34   -144.85                                   
REMARK 500    GLU A 111     -128.45     59.74                                   
REMARK 500    SER A 119       88.64     57.83                                   
REMARK 500    PRO A 131       -7.53    -55.86                                   
REMARK 500    CYS A 170       92.82     79.22                                   
REMARK 500    ARG A 174       21.53     45.82                                   
REMARK 500    HIS A 187        7.65    -62.99                                   
REMARK 500    ALA A 195      -57.72    -11.11                                   
REMARK 500    SER A 196      164.95    -49.82                                   
REMARK 500    LYS A 200      -66.69    -93.62                                   
REMARK 500    GLU A 216     -104.44     48.06                                   
REMARK 500    ASN A 217       42.48   -140.26                                   
REMARK 500    ASP A 223       31.54    -72.50                                   
REMARK 500    TRP A 230     -167.73   -162.42                                   
REMARK 500    CYS A 231      153.77    179.27                                   
REMARK 500    LYS A 236      149.60    -38.54                                   
REMARK 500    ASP A 239      163.63    -44.75                                   
REMARK 500    PHE A 240      176.24    178.75                                   
REMARK 500    GLU A 290      -70.59    -67.14                                   
REMARK 500    ALA A 291       -3.14    -49.43                                   
REMARK 500    ASP A 292       59.12   -142.24                                   
REMARK 500    PHE A 299      -80.21   -143.07                                   
REMARK 500    SER A 303       47.18     38.57                                   
REMARK 500    GLU A 311      -16.34    -47.58                                   
REMARK 500    ASP A 318       79.42    -63.77                                   
REMARK 500    ILE A 321       78.91    105.95                                   
REMARK 500    LYS A 341      -71.45    -68.31                                   
REMARK 500    GLU A 345      137.28   -173.73                                   
REMARK 500    SER A 354     -172.62   -175.51                                   
REMARK 500    THR A 360     -157.96   -148.89                                   
REMARK 500    HIS A 386      -51.08   -126.86                                   
REMARK 500    ARG A 390      151.88    -41.54                                   
REMARK 500    ILE A 395      -71.04   -122.02                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      72 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ALA A   36     THR A   37                 -144.37                    
REMARK 500 THR A   52     PRO A   53                 -146.19                    
REMARK 500 LEU A   69     GLY A   70                 -145.95                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 604  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA A   1   O                                                      
REMARK 620 2 CGU A   6  OE11 122.5                                              
REMARK 620 3 CGU A   7  OE22 134.4  58.6                                        
REMARK 620 4 CGU A  16  OE21  61.6  99.1 156.6                                  
REMARK 620 5 CGU A  16  OE22  92.2  56.0 113.3  43.5                            
REMARK 620 6 CGU A  26  OE11 108.9 128.6  86.4 105.1 126.1                      
REMARK 620 7 CGU A  26  OE22  66.6 151.2 137.9  59.3  98.8  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 A 605  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU A   6  OE12                                                    
REMARK 620 2 CGU A  16  OE22  71.0                                              
REMARK 620 3 CGU A  16  OE21 108.0  50.5                                        
REMARK 620 4 CGU A  20  OE12 127.2  92.4  96.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 602  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU A   7  OE12                                                    
REMARK 620 2 CGU A   7  OE21  68.0                                              
REMARK 620 3 CGU A  26  OE12  82.5  79.4                                        
REMARK 620 4 CGU A  29  OE22 158.2 133.5 102.7                                  
REMARK 620 5 CGU A  29  OE21 143.7  75.9  86.6  58.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 603  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU A   7  OE21                                                    
REMARK 620 2 CGU A  16  OE12 117.9                                              
REMARK 620 3 CGU A  26  OE11  78.8  65.8                                        
REMARK 620 4 CGU A  29  OE21  70.2 161.7 102.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 606  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU A  20  OE12                                                    
REMARK 620 2 CGU A  20  OE22  69.5                                              
REMARK 620 N                    1                                               
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1NL1   RELATED DB: PDB                                   
REMARK 900 BOVINE PROTHROMBIN FRAGMENT 1 IN COMPLEX WITH CALCIUM ION            
REMARK 900 RELATED ID: 4NZQ   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE COORDS CONTAIN DELETION OF RESIDUES 146-167, CORRESPONDING TO    
REMARK 999 UNP RESIDUES 189-210                                                 
DBREF  4O03 A    1   145  UNP    P00734   THRB_HUMAN      44    188             
DBREF  4O03 A  168   579  UNP    P00734   THRB_HUMAN     211    622             
SEQRES   1 A  557  ALA ASN THR PHE LEU CGU CGU VAL ARG LYS GLY ASN LEU          
SEQRES   2 A  557  CGU ARG CGU CYS VAL CGU CGU THR CYS SER TYR CGU CGU          
SEQRES   3 A  557  ALA PHE CGU ALA LEU CGU SER SER THR ALA THR ASP VAL          
SEQRES   4 A  557  PHE TRP ALA LYS TYR THR ALA CYS GLU THR ALA ARG THR          
SEQRES   5 A  557  PRO ARG ASP LYS LEU ALA ALA CYS LEU GLU GLY ASN CYS          
SEQRES   6 A  557  ALA GLU GLY LEU GLY THR ASN TYR ARG GLY HIS VAL ASN          
SEQRES   7 A  557  ILE THR ARG SER GLY ILE GLU CYS GLN LEU TRP ARG SER          
SEQRES   8 A  557  ARG TYR PRO HIS LYS PRO GLU ILE ASN SER THR THR HIS          
SEQRES   9 A  557  PRO GLY ALA ASP LEU GLN GLU ASN PHE CYS ARG ASN PRO          
SEQRES  10 A  557  ASP SER SER THR THR GLY PRO TRP CYS TYR THR THR ASP          
SEQRES  11 A  557  PRO THR VAL ARG ARG GLN GLU CYS SER ILE PRO VAL CYS          
SEQRES  12 A  557  GLY GLN GLU GLN CYS VAL PRO ASP ARG GLY GLN GLN TYR          
SEQRES  13 A  557  GLN GLY ARG LEU ALA VAL THR THR HIS GLY LEU PRO CYS          
SEQRES  14 A  557  LEU ALA TRP ALA SER ALA GLN ALA LYS ALA LEU SER LYS          
SEQRES  15 A  557  HIS GLN ASP PHE ASN SER ALA VAL GLN LEU VAL GLU ASN          
SEQRES  16 A  557  PHE CYS ARG ASN PRO ASP GLY ASP GLU GLU GLY VAL TRP          
SEQRES  17 A  557  CYS TYR VAL ALA GLY LYS PRO GLY ASP PHE GLY TYR CYS          
SEQRES  18 A  557  ASP LEU ASN TYR CYS GLU GLU ALA VAL GLU GLU GLU THR          
SEQRES  19 A  557  GLY ASP GLY LEU ASP GLU ASP SER ASP ARG ALA ILE GLU          
SEQRES  20 A  557  GLY ARG THR ALA THR SER GLU TYR GLN THR PHE PHE ASN          
SEQRES  21 A  557  PRO ARG THR PHE GLY SER GLY GLU ALA ASP CYS GLY LEU          
SEQRES  22 A  557  ARG PRO LEU PHE GLU LYS LYS SER LEU GLU ASP LYS THR          
SEQRES  23 A  557  GLU ARG GLU LEU LEU GLU SER TYR ILE ASP GLY ARG ILE          
SEQRES  24 A  557  VAL GLU GLY SER ASP ALA GLU ILE GLY MET SER PRO TRP          
SEQRES  25 A  557  GLN VAL MET LEU PHE ARG LYS SER PRO GLN GLU LEU LEU          
SEQRES  26 A  557  CYS GLY ALA SER LEU ILE SER ASP ARG TRP VAL LEU THR          
SEQRES  27 A  557  ALA ALA HIS CYS LEU LEU TYR PRO PRO TRP ASP LYS ASN          
SEQRES  28 A  557  PHE THR GLU ASN ASP LEU LEU VAL ARG ILE GLY LYS HIS          
SEQRES  29 A  557  SER ARG THR ARG TYR GLU ARG ASN ILE GLU LYS ILE SER          
SEQRES  30 A  557  MET LEU GLU LYS ILE TYR ILE HIS PRO ARG TYR ASN TRP          
SEQRES  31 A  557  ARG GLU ASN LEU ASP ARG ASP ILE ALA LEU MET LYS LEU          
SEQRES  32 A  557  LYS LYS PRO VAL ALA PHE SER ASP TYR ILE HIS PRO VAL          
SEQRES  33 A  557  CYS LEU PRO ASP ARG GLU THR ALA ALA SER LEU LEU GLN          
SEQRES  34 A  557  ALA GLY TYR LYS GLY ARG VAL THR GLY TRP GLY ASN LEU          
SEQRES  35 A  557  LYS GLU THR TRP THR ALA ASN VAL GLY LYS GLY GLN PRO          
SEQRES  36 A  557  SER VAL LEU GLN VAL VAL ASN LEU PRO ILE VAL GLU ARG          
SEQRES  37 A  557  PRO VAL CYS LYS ASP SER THR ARG ILE ARG ILE THR ASP          
SEQRES  38 A  557  ASN MET PHE CYS ALA GLY TYR LYS PRO ASP GLU GLY LYS          
SEQRES  39 A  557  ARG GLY ASP ALA CYS GLU GLY ASP SER GLY GLY PRO PHE          
SEQRES  40 A  557  VAL MET LYS SER PRO PHE ASN ASN ARG TRP TYR GLN MET          
SEQRES  41 A  557  GLY ILE VAL SER TRP GLY GLU GLY CYS ASP ARG ASP GLY          
SEQRES  42 A  557  LYS TYR GLY PHE TYR THR HIS VAL PHE ARG LEU LYS LYS          
SEQRES  43 A  557  TRP ILE GLN LYS VAL ILE ASP GLN PHE GLY GLU                  
MODRES 4O03 ASN A  100  ASN  GLYCOSYLATION SITE                                 
MODRES 4O03 ASN A   78  ASN  GLYCOSYLATION SITE                                 
MODRES 4O03 ASN A  373  ASN  GLYCOSYLATION SITE                                 
MODRES 4O03 CGU A    6  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 4O03 CGU A    7  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 4O03 CGU A   14  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 4O03 CGU A   16  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 4O03 CGU A   19  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 4O03 CGU A   20  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 4O03 CGU A   25  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 4O03 CGU A   26  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 4O03 CGU A   29  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 4O03 CGU A   32  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
HET    CGU  A   6      12                                                       
HET    CGU  A   7      12                                                       
HET    CGU  A  14      12                                                       
HET    CGU  A  16      12                                                       
HET    CGU  A  19      12                                                       
HET    CGU  A  20      12                                                       
HET    CGU  A  25      12                                                       
HET    CGU  A  26      12                                                       
HET    CGU  A  29      12                                                       
HET    CGU  A  32      12                                                       
HET     CA  A 602       1                                                       
HET     CA  A 603       1                                                       
HET     CA  A 604       1                                                       
HET     CA  A 605       1                                                       
HET     CA  A 606       1                                                       
HET    NAG  A 701      14                                                       
HET    NAG  A 702      14                                                       
HET    NAG  A 703      14                                                       
HETNAM     CGU GAMMA-CARBOXY-GLUTAMIC ACID                                      
HETNAM      CA CALCIUM ION                                                      
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
FORMUL   1  CGU    10(C6 H9 N O6)                                               
FORMUL   2   CA    5(CA 2+)                                                     
FORMUL   7  NAG    3(C8 H15 N O6)                                               
HELIX    1   1 ASN A   12  VAL A   18  1                                   7    
HELIX    2   2 SER A   23  LEU A   31  1                                   9    
HELIX    3   3 PHE A   40  ALA A   46  1                                   7    
HELIX    4   4 PRO A   53  GLU A   62  1                                  10    
HELIX    5   5 PRO A  172  GLN A  176  5                                   5    
HELIX    6   6 ALA A  251  GLU A  255  5                                   5    
HELIX    7   7 GLU A  309  GLU A  314  1                                   6    
HELIX    8   8 PRO A  368  ASP A  371  5                                   4    
HELIX    9   9 ASP A  442  GLY A  453  1                                  12    
HELIX   10  10 GLY A  462  THR A  469  1                                   8    
HELIX   11  11 GLU A  489  ASP A  495  1                                   7    
HELIX   12  12 LEU A  566  GLN A  576  1                                  11    
SHEET    1   A 3 CYS A  86  GLN A  87  0                                        
SHEET    2   A 3 TRP A 125  THR A 128 -1  O  TYR A 127   N  GLN A  87           
SHEET    3   A 3 ARG A 135  GLU A 137 -1  O  GLN A 136   N  CYS A 126           
SHEET    1   B 2 CYS A 231  TYR A 232  0                                        
SHEET    2   B 2 PHE A 240  GLY A 241 -1  O  GLY A 241   N  CYS A 231           
SHEET    1   C 7 SER A 325  ASP A 326  0                                        
SHEET    2   C 7 GLN A 481  PRO A 486 -1  O  VAL A 482   N  SER A 325           
SHEET    3   C 7 LYS A 455  GLY A 460 -1  N  VAL A 458   O  VAL A 483           
SHEET    4   C 7 PRO A 528  LYS A 532 -1  O  VAL A 530   N  ARG A 457           
SHEET    5   C 7 TRP A 539  VAL A 545 -1  O  MET A 542   N  PHE A 529           
SHEET    6   C 7 GLY A 558  HIS A 562 -1  O  THR A 561   N  ILE A 544           
SHEET    7   C 7 MET A 505  ALA A 508 -1  N  PHE A 506   O  TYR A 560           
SHEET    1   D 7 GLN A 335  ARG A 340  0                                        
SHEET    2   D 7 GLU A 345  LEU A 352 -1  O  GLU A 345   N  ARG A 340           
SHEET    3   D 7 TRP A 357  THR A 360 -1  O  LEU A 359   N  SER A 351           
SHEET    4   D 7 ALA A 421  LEU A 425 -1  O  MET A 423   N  VAL A 358           
SHEET    5   D 7 LYS A 397  ILE A 406 -1  N  TYR A 405   O  LEU A 422           
SHEET    6   D 7 LEU A 379  ILE A 383 -1  N  ILE A 383   O  LYS A 397           
SHEET    7   D 7 GLN A 335  ARG A 340 -1  N  PHE A 339   O  LEU A 380           
SHEET    1   E 2 LEU A 366  TYR A 367  0                                        
SHEET    2   E 2 LYS A 372  ASN A 373 -1  O  LYS A 372   N  TYR A 367           
SSBOND   1 CYS A   17    CYS A   22                          1555   1555  2.03  
SSBOND   2 CYS A   47    CYS A   60                          1555   1555  2.07  
SSBOND   3 CYS A   65    CYS A  143                          1555   1555  2.07  
SSBOND   4 CYS A   86    CYS A  126                          1555   1555  2.04  
SSBOND   5 CYS A  114    CYS A  138                          1555   1555  2.03  
SSBOND   6 CYS A  170    CYS A  248                          1555   1555  2.05  
SSBOND   7 CYS A  191    CYS A  231                          1555   1555  2.02  
SSBOND   8 CYS A  219    CYS A  243                          1555   1555  2.04  
SSBOND   9 CYS A  293    CYS A  439                          1555   1555  2.05  
SSBOND  10 CYS A  348    CYS A  364                          1555   1555  2.02  
SSBOND  11 CYS A  493    CYS A  507                          1555   1555  2.06  
SSBOND  12 CYS A  521    CYS A  551                          1555   1555  2.08  
LINK         C   LEU A   5                 N   CGU A   6     1555   1555  1.50  
LINK         C   CGU A   6                 N   CGU A   7     1555   1555  1.33  
LINK         C   CGU A   7                 N   VAL A   8     1555   1555  1.33  
LINK         C   LEU A  13                 N   CGU A  14     1555   1555  1.34  
LINK         C   CGU A  14                 N   ARG A  15     1555   1555  1.33  
LINK         C   ARG A  15                 N   CGU A  16     1555   1555  1.32  
LINK         C   CGU A  16                 N   CYS A  17     1555   1555  1.34  
LINK         C   VAL A  18                 N   CGU A  19     1555   1555  1.33  
LINK         C   CGU A  19                 N   CGU A  20     1555   1555  1.34  
LINK         C   CGU A  20                 N   THR A  21     1555   1555  1.24  
LINK         C   TYR A  24                 N   CGU A  25     1555   1555  1.34  
LINK         C   CGU A  25                 N   CGU A  26     1555   1555  1.34  
LINK         C   CGU A  26                 N   ALA A  27     1555   1555  1.34  
LINK         C   PHE A  28                 N   CGU A  29     1555   1555  1.34  
LINK         C   CGU A  29                 N   ALA A  30     1555   1555  1.33  
LINK         C   LEU A  31                 N   CGU A  32     1555   1555  1.34  
LINK         C   CGU A  32                 N   SER A  33     1555   1555  1.34  
LINK         ND2 ASN A  78                 C1  NAG A 702     1555   1555  1.46  
LINK         ND2 ASN A 100                 C1  NAG A 703     1555   1555  1.44  
LINK         ND2 ASN A 373                 C1  NAG A 701     1555   1555  1.47  
LINK         O   ALA A   1                CA    CA A 604     1555   1555  2.28  
LINK        OE11 CGU A   6                CA    CA A 604     1555   1555  2.29  
LINK        OE12 CGU A   6                CA    CA A 605     1555   1555  2.42  
LINK        OE12 CGU A   7                CA    CA A 602     1555   1555  2.41  
LINK        OE21 CGU A   7                CA    CA A 602     1555   1555  2.50  
LINK        OE21 CGU A   7                CA    CA A 603     1555   1555  2.81  
LINK        OE22 CGU A   7                CA    CA A 604     1555   1555  2.81  
LINK        OE12 CGU A  16                CA    CA A 603     1555   1555  2.73  
LINK        OE21 CGU A  16                CA    CA A 604     1555   1555  2.40  
LINK        OE22 CGU A  16                CA    CA A 604     1555   1555  3.15  
LINK        OE22 CGU A  16                CA    CA A 605     1555   1555  2.26  
LINK        OE21 CGU A  16                CA    CA A 605     1555   1555  2.73  
LINK        OE12 CGU A  20                CA    CA A 605     1555   1555  2.97  
LINK        OE12 CGU A  20                CA    CA A 606     1555   1555  2.22  
LINK        OE22 CGU A  20                CA    CA A 606     1555   1555  2.58  
LINK        OE12 CGU A  26                CA    CA A 602     1555   1555  2.35  
LINK        OE11 CGU A  26                CA    CA A 603     1555   1555  2.17  
LINK        OE11 CGU A  26                CA    CA A 604     1555   1555  3.08  
LINK        OE22 CGU A  26                CA    CA A 604     1555   1555  3.08  
LINK        OE22 CGU A  29                CA    CA A 602     1555   1555  2.11  
LINK        OE21 CGU A  29                CA    CA A 602     1555   1555  2.38  
LINK        OE21 CGU A  29                CA    CA A 603     1555   1555  2.37  
CISPEP   1 TYR A   93    PRO A   94          0        -2.32                     
CISPEP   2 SER A  342    PRO A  343          0        -7.90                     
CRYST1  177.459   89.431   87.982  90.00 116.36  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005635  0.000000  0.002792        0.00000                         
SCALE2      0.000000  0.011182  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012685        0.00000                         
ATOM      1  N   ALA A   1      -6.078 -13.248  45.321  1.00 96.03           N  
ATOM      2  CA  ALA A   1      -7.191 -13.182  46.301  1.00 96.29           C  
ATOM      3  C   ALA A   1      -6.677 -13.558  47.675  1.00 96.46           C  
ATOM      4  O   ALA A   1      -5.572 -14.093  47.792  1.00 96.40           O  
ATOM      5  CB  ALA A   1      -8.321 -14.120  45.890  1.00 96.35           C  
ATOM      6  N   ASN A   2      -7.479 -13.286  48.708  1.00 96.66           N  
ATOM      7  CA  ASN A   2      -7.130 -13.666  50.083  1.00 96.75           C  
ATOM      8  C   ASN A   2      -8.275 -14.229  50.937  1.00 96.83           C  
ATOM      9  O   ASN A   2      -8.508 -13.752  52.040  1.00 96.86           O  
ATOM     10  CB  ASN A   2      -6.484 -12.486  50.814  1.00 96.75           C  
ATOM     11  CG  ASN A   2      -5.314 -11.909  50.062  1.00 96.78           C  
ATOM     12  OD1 ASN A   2      -4.210 -12.470  50.059  1.00 96.48           O  
ATOM     13  ND2 ASN A   2      -5.550 -10.781  49.407  1.00 96.80           N  
ATOM     14  N   THR A   3      -8.963 -15.257  50.444  1.00 97.02           N  
ATOM     15  CA  THR A   3     -10.053 -15.905  51.200  1.00 97.21           C  
ATOM     16  C   THR A   3      -9.668 -16.427  52.618  1.00 96.99           C  
ATOM     17  O   THR A   3      -9.494 -17.633  52.844  1.00 97.07           O  
ATOM     18  CB  THR A   3     -10.751 -17.041  50.371  1.00 97.43           C  
ATOM     19  OG1 THR A   3      -9.789 -17.703  49.531  1.00 98.07           O  
ATOM     20  CG2 THR A   3     -11.891 -16.491  49.511  1.00 97.31           C  
ATOM     21  N   PHE A   4      -9.573 -15.515  53.576  1.00 96.60           N  
ATOM     22  CA  PHE A   4      -9.216 -15.881  54.933  1.00 96.46           C  
ATOM     23  C   PHE A   4      -7.851 -16.571  54.920  1.00 96.41           C  
ATOM     24  O   PHE A   4      -6.856 -15.926  54.607  1.00 96.31           O  
ATOM     25  CB  PHE A   4     -10.332 -16.727  55.591  1.00 96.46           C  
ATOM     26  CG  PHE A   4     -10.147 -16.984  57.085  1.00 96.76           C  
ATOM     27  CD1 PHE A   4      -9.063 -16.459  57.799  1.00 97.17           C  
ATOM     28  CD2 PHE A   4     -11.088 -17.742  57.782  1.00 96.60           C  
ATOM     29  CE1 PHE A   4      -8.914 -16.707  59.172  1.00 96.82           C  
ATOM     30  CE2 PHE A   4     -10.944 -17.992  59.155  1.00 96.43           C  
ATOM     31  CZ  PHE A   4      -9.858 -17.476  59.846  1.00 96.34           C  
ATOM     32  N   LEU A   5      -7.856 -17.955  55.170  1.00 96.41           N  
ATOM     33  CA  LEU A   5      -6.619 -18.558  55.687  1.00 96.54           C  
ATOM     34  C   LEU A   5      -5.333 -18.386  54.882  1.00 97.15           C  
ATOM     35  O   LEU A   5      -4.544 -17.506  55.192  1.00 97.26           O  
ATOM     36  CB  LEU A   5      -6.848 -20.022  56.030  1.00 96.14           C  
ATOM     37  CG  LEU A   5      -7.563 -20.161  57.367  1.00 95.59           C  
ATOM     38  CD1 LEU A   5      -7.883 -21.612  57.664  1.00 95.24           C  
ATOM     39  CD2 LEU A   5      -6.713 -19.564  58.463  1.00 95.24           C  
HETATM   40  N   CGU A   6      -5.277 -19.492  53.874  1.00 97.98           N  
HETATM   41  CA  CGU A   6      -4.199 -19.615  52.838  1.00 98.72           C  
HETATM   42  C   CGU A   6      -2.931 -18.708  52.802  1.00 99.16           C  
HETATM   43  O   CGU A   6      -2.160 -18.784  51.835  1.00 99.35           O  
HETATM   44  CB  CGU A   6      -4.823 -19.581  51.437  1.00 98.66           C  
HETATM   45  CG  CGU A   6      -4.999 -18.163  50.909  1.00 98.65           C  
HETATM   46  CD1 CGU A   6      -4.763 -18.066  49.416  1.00 96.88           C  
HETATM   47  CD2 CGU A   6      -6.306 -17.504  51.368  1.00100.41           C  
HETATM   48 OE11 CGU A   6      -3.758 -17.447  49.020  1.00 94.55           O  
HETATM   49 OE12 CGU A   6      -5.566 -18.619  48.635  1.00 96.63           O  
HETATM   50 OE21 CGU A   6      -7.385 -18.088  51.106  1.00102.05           O  
HETATM   51 OE22 CGU A   6      -6.270 -16.417  52.006  1.00100.23           O  
HETATM   52  N   CGU A   7      -2.704 -17.866  53.806  1.00 99.44           N  
HETATM   53  CA  CGU A   7      -1.500 -17.041  53.808  1.00 99.70           C  
HETATM   54  C   CGU A   7      -0.430 -17.633  54.697  1.00100.27           C  
HETATM   55  O   CGU A   7       0.604 -17.031  54.937  1.00100.23           O  
HETATM   56  CB  CGU A   7      -1.829 -15.577  54.093  1.00 99.37           C  
HETATM   57  CG  CGU A   7      -2.710 -15.031  52.985  1.00 99.10           C  
HETATM   58  CD1 CGU A   7      -3.208 -13.611  53.194  1.00 99.18           C  
HETATM   59  CD2 CGU A   7      -2.129 -15.243  51.598  1.00 99.40           C  
HETATM   60 OE11 CGU A   7      -4.181 -13.428  53.958  1.00 99.65           O  
HETATM   61 OE12 CGU A   7      -2.664 -12.677  52.565  1.00 99.06           O  
HETATM   62 OE21 CGU A   7      -1.157 -14.548  51.228  1.00100.45           O  
HETATM   63 OE22 CGU A   7      -2.649 -16.116  50.874  1.00 98.88           O  
ATOM     64  N   VAL A   8      -0.695 -18.846  55.160  1.00101.30           N  
ATOM     65  CA  VAL A   8       0.342 -19.726  55.664  1.00102.61           C  
ATOM     66  C   VAL A   8       1.178 -20.196  54.470  1.00103.30           C  
ATOM     67  O   VAL A   8       2.406 -20.374  54.582  1.00103.50           O  
ATOM     68  CB  VAL A   8      -0.267 -20.952  56.390  1.00102.78           C  
ATOM     69  CG1 VAL A   8       0.830 -21.994  56.756  1.00102.68           C  
ATOM     70  CG2 VAL A   8      -1.067 -20.495  57.640  1.00103.00           C  
ATOM     71  N   ARG A   9       0.499 -20.381  53.332  1.00103.98           N  
ATOM     72  CA  ARG A   9       1.126 -20.863  52.093  1.00104.64           C  
ATOM     73  C   ARG A   9       1.995 -19.782  51.412  1.00105.03           C  
ATOM     74  O   ARG A   9       1.646 -18.579  51.434  1.00104.95           O  
ATOM     75  CB  ARG A   9       0.061 -21.399  51.120  1.00104.51           C  
ATOM     76  CG  ARG A   9      -1.037 -22.228  51.779  1.00104.76           C  
ATOM     77  CD  ARG A   9      -2.090 -22.695  50.767  1.00106.29           C  
ATOM     78  NE  ARG A   9      -1.664 -23.873  49.995  1.00107.24           N  
ATOM     79  CZ  ARG A   9      -2.467 -24.661  49.269  1.00107.09           C  
ATOM     80  NH1 ARG A   9      -3.775 -24.427  49.190  1.00106.98           N  
ATOM     81  NH2 ARG A   9      -1.956 -25.701  48.617  1.00106.69           N  
ATOM     82  N   LYS A  10       3.124 -20.222  50.827  1.00105.31           N  
ATOM     83  CA  LYS A  10       4.016 -19.354  50.026  1.00105.40           C  
ATOM     84  C   LYS A  10       3.287 -18.812  48.785  1.00105.61           C  
ATOM     85  O   LYS A  10       2.436 -19.507  48.207  1.00105.80           O  
ATOM     86  CB  LYS A  10       5.312 -20.098  49.622  1.00105.25           C  
ATOM     87  CG  LYS A  10       5.199 -21.062  48.426  1.00104.85           C  
ATOM     88  CD  LYS A  10       6.570 -21.546  47.954  1.00104.03           C  
ATOM     89  CE  LYS A  10       6.445 -22.623  46.891  0.30103.54           C  
ATOM     90  NZ  LYS A  10       7.780 -23.169  46.529  0.30103.13           N  
ATOM     91  N   GLY A  11       3.613 -17.582  48.383  1.00105.63           N  
ATOM     92  CA  GLY A  11       2.992 -16.962  47.201  1.00105.69           C  
ATOM     93  C   GLY A  11       3.016 -17.818  45.932  1.00105.63           C  
ATOM     94  O   GLY A  11       3.980 -18.552  45.683  1.00105.68           O  
ATOM     95  N   ASN A  12       1.937 -17.745  45.148  1.00105.40           N  
ATOM     96  CA  ASN A  12       1.877 -18.369  43.814  1.00105.01           C  
ATOM     97  C   ASN A  12       1.272 -17.401  42.781  1.00105.16           C  
ATOM     98  O   ASN A  12       0.091 -17.022  42.867  1.00105.20           O  
ATOM     99  CB  ASN A  12       1.130 -19.717  43.848  1.00104.56           C  
ATOM    100  CG  ASN A  12       1.048 -20.394  42.475  1.00103.44           C  
ATOM    101  OD1 ASN A  12       1.625 -19.929  41.483  1.00101.74           O  
ATOM    102  ND2 ASN A  12       0.313 -21.501  42.418  1.00102.29           N  
ATOM    103  N   LEU A  13       2.102 -17.000  41.815  1.00105.12           N  
ATOM    104  CA  LEU A  13       1.700 -16.063  40.771  1.00104.94           C  
ATOM    105  C   LEU A  13       0.453 -16.589  40.059  1.00104.55           C  
ATOM    106  O   LEU A  13      -0.518 -15.840  39.889  1.00104.34           O  
ATOM    107  CB  LEU A  13       2.859 -15.812  39.786  1.00105.13           C  
ATOM    108  CG  LEU A  13       2.932 -14.483  39.006  1.00105.93           C  
ATOM    109  CD1 LEU A  13       3.354 -13.293  39.889  1.00106.39           C  
ATOM    110  CD2 LEU A  13       3.877 -14.598  37.798  1.00106.64           C  
HETATM  111  N   CGU A  14       0.475 -17.881  39.698  1.00104.01           N  
HETATM  112  CA  CGU A  14      -0.646 -18.526  38.996  1.00103.63           C  
HETATM  113  C   CGU A  14      -1.972 -18.576  39.780  1.00103.47           C  
HETATM  114  O   CGU A  14      -2.984 -18.033  39.325  1.00103.64           O  
HETATM  115  CB  CGU A  14      -0.284 -19.932  38.496  1.00103.55           C  
HETATM  116  CG  CGU A  14      -1.441 -20.602  37.736  1.00103.01           C  
HETATM  117  CD1 CGU A  14      -1.634 -20.080  36.309  1.00104.60           C  
HETATM  118  CD2 CGU A  14      -1.354 -22.105  37.709  1.00100.00           C  
HETATM  119 OE11 CGU A  14      -0.645 -19.584  35.716  1.00105.34           O  
HETATM  120 OE12 CGU A  14      -2.777 -20.164  35.774  1.00105.45           O  
HETATM  121 OE21 CGU A  14      -2.417 -22.763  37.717  1.00 97.43           O  
HETATM  122 OE22 CGU A  14      -0.222 -22.618  37.666  1.00 99.00           O  
ATOM    123  N   ARG A  15      -1.963 -19.256  40.928  1.00103.01           N  
ATOM    124  CA  ARG A  15      -3.137 -19.387  41.798  1.00102.47           C  
ATOM    125  C   ARG A  15      -3.722 -18.037  42.180  1.00101.70           C  
ATOM    126  O   ARG A  15      -4.935 -17.841  42.188  1.00101.32           O  
ATOM    127  CB  ARG A  15      -2.743 -20.121  43.082  1.00102.81           C  
ATOM    128  CG  ARG A  15      -3.911 -20.479  44.006  1.00104.09           C  
ATOM    129  CD  ARG A  15      -3.544 -20.356  45.485  1.00105.89           C  
ATOM    130  NE  ARG A  15      -2.127 -20.616  45.763  1.00107.33           N  
ATOM    131  CZ  ARG A  15      -1.560 -20.528  46.968  1.00107.86           C  
ATOM    132  NH1 ARG A  15      -2.281 -20.184  48.029  1.00108.01           N  
ATOM    133  NH2 ARG A  15      -0.264 -20.785  47.118  1.00107.97           N  
HETATM  134  N   CGU A  16      -2.835 -17.107  42.488  1.00101.15           N  
HETATM  135  CA  CGU A  16      -3.243 -15.873  43.096  1.00100.86           C  
HETATM  136  C   CGU A  16      -3.392 -14.697  42.137  1.00101.24           C  
HETATM  137  O   CGU A  16      -4.411 -14.009  42.191  1.00101.39           O  
HETATM  138  CB  CGU A  16      -2.327 -15.547  44.273  1.00100.58           C  
HETATM  139  CG  CGU A  16      -2.465 -16.549  45.411  1.00 98.90           C  
HETATM  140  CD1 CGU A  16      -1.389 -16.427  46.492  1.00 98.16           C  
HETATM  141  CD2 CGU A  16      -3.854 -16.534  46.035  1.00 97.24           C  
HETATM  142 OE11 CGU A  16      -1.249 -17.386  47.275  1.00 97.47           O  
HETATM  143 OE12 CGU A  16      -0.688 -15.388  46.583  1.00 97.18           O  
HETATM  144 OE21 CGU A  16      -4.471 -15.454  46.154  1.00 95.02           O  
HETATM  145 OE22 CGU A  16      -4.346 -17.605  46.425  1.00 96.63           O  
ATOM    146  N   CYS A  17      -2.411 -14.460  41.262  1.00101.46           N  
ATOM    147  CA  CYS A  17      -2.481 -13.284  40.369  1.00101.75           C  
ATOM    148  C   CYS A  17      -2.947 -13.567  38.945  1.00101.47           C  
ATOM    149  O   CYS A  17      -3.223 -12.625  38.191  1.00101.30           O  
ATOM    150  CB  CYS A  17      -1.167 -12.496  40.353  1.00101.92           C  
ATOM    151  SG  CYS A  17      -0.954 -11.368  41.774  1.00103.52           S  
ATOM    152  N   VAL A  18      -3.056 -14.856  38.606  1.00101.35           N  
ATOM    153  CA  VAL A  18      -3.468 -15.312  37.266  1.00101.34           C  
ATOM    154  C   VAL A  18      -4.826 -16.038  37.250  1.00101.35           C  
ATOM    155  O   VAL A  18      -5.651 -15.804  36.363  1.00101.23           O  
ATOM    156  CB  VAL A  18      -2.382 -16.199  36.600  1.00101.31           C  
ATOM    157  CG1 VAL A  18      -2.819 -16.638  35.205  1.00101.40           C  
ATOM    158  CG2 VAL A  18      -1.041 -15.459  36.535  1.00101.08           C  
HETATM  159  N   CGU A  19      -5.045 -16.925  38.217  1.00101.53           N  
HETATM  160  CA  CGU A  19      -6.345 -17.573  38.388  1.00101.88           C  
HETATM  161  C   CGU A  19      -7.369 -16.623  39.031  1.00102.18           C  
HETATM  162  O   CGU A  19      -8.563 -16.693  38.719  1.00102.22           O  
HETATM  163  CB  CGU A  19      -6.214 -18.892  39.165  1.00101.74           C  
HETATM  164  CG  CGU A  19      -5.707 -20.053  38.305  1.00102.37           C  
HETATM  165  CD1 CGU A  19      -5.063 -21.175  39.086  1.00102.51           C  
HETATM  166  CD2 CGU A  19      -6.776 -20.703  37.447  1.00103.32           C  
HETATM  167 OE11 CGU A  19      -4.343 -21.979  38.448  1.00102.48           O  
HETATM  168 OE12 CGU A  19      -5.305 -21.284  40.307  1.00102.21           O  
HETATM  169 OE21 CGU A  19      -6.405 -21.591  36.627  1.00103.82           O  
HETATM  170 OE22 CGU A  19      -7.974 -20.351  37.597  1.00103.61           O  
HETATM  171  N   CGU A  20      -6.863 -15.670  39.830  1.00102.55           N  
HETATM  172  CA  CGU A  20      -7.678 -14.637  40.507  1.00102.64           C  
HETATM  173  C   CGU A  20      -7.082 -13.263  40.145  1.00103.11           C  
HETATM  174  O   CGU A  20      -5.908 -13.182  39.797  1.00103.09           O  
HETATM  175  CB  CGU A  20      -7.672 -14.861  42.035  1.00102.15           C  
HETATM  176  CG  CGU A  20      -7.956 -16.303  42.479  1.00101.44           C  
HETATM  177  CD1 CGU A  20      -7.130 -16.761  43.656  1.00101.85           C  
HETATM  178  CD2 CGU A  20      -9.405 -16.581  42.802  1.00100.25           C  
HETATM  179 OE11 CGU A  20      -6.125 -16.098  43.967  1.00103.21           O  
HETATM  180 OE12 CGU A  20      -7.484 -17.794  44.279  1.00101.58           O  
HETATM  181 OE21 CGU A  20     -10.137 -15.621  43.081  1.00100.28           O  
HETATM  182 OE22 CGU A  20      -9.804 -17.767  42.804  1.00 99.27           O  
ATOM    183  N   THR A  21      -7.705 -12.196  40.078  1.00103.83           N  
ATOM    184  CA  THR A  21      -7.020 -10.891  39.967  1.00104.71           C  
ATOM    185  C   THR A  21      -6.396 -10.577  41.338  1.00105.37           C  
ATOM    186  O   THR A  21      -6.627 -11.328  42.287  1.00105.62           O  
ATOM    187  CB  THR A  21      -7.930  -9.738  39.428  1.00104.67           C  
ATOM    188  OG1 THR A  21      -9.145  -9.664  40.181  1.00105.04           O  
ATOM    189  CG2 THR A  21      -8.268  -9.952  37.945  1.00104.45           C  
ATOM    190  N   CYS A  22      -5.594  -9.516  41.461  1.00106.25           N  
ATOM    191  CA  CYS A  22      -4.787  -9.338  42.695  1.00107.13           C  
ATOM    192  C   CYS A  22      -4.365  -7.913  43.091  1.00108.33           C  
ATOM    193  O   CYS A  22      -4.780  -6.932  42.465  1.00108.76           O  
ATOM    194  CB  CYS A  22      -3.552 -10.256  42.667  1.00106.77           C  
ATOM    195  SG  CYS A  22      -2.267  -9.854  41.450  1.00104.59           S  
ATOM    196  N   SER A  23      -3.543  -7.824  44.145  1.00109.43           N  
ATOM    197  CA  SER A  23      -3.012  -6.553  44.672  1.00110.36           C  
ATOM    198  C   SER A  23      -1.464  -6.514  44.651  1.00111.02           C  
ATOM    199  O   SER A  23      -0.816  -7.517  44.303  1.00111.31           O  
ATOM    200  CB  SER A  23      -3.548  -6.307  46.094  1.00110.34           C  
ATOM    201  OG  SER A  23      -3.358  -7.448  46.923  1.00110.19           O  
ATOM    202  N   TYR A  24      -0.880  -5.367  45.027  1.00111.55           N  
ATOM    203  CA  TYR A  24       0.586  -5.201  45.034  1.00111.76           C  
ATOM    204  C   TYR A  24       1.337  -6.228  45.914  1.00111.13           C  
ATOM    205  O   TYR A  24       2.214  -6.932  45.405  1.00110.82           O  
ATOM    206  CB  TYR A  24       1.058  -3.773  45.419  1.00112.41           C  
ATOM    207  CG  TYR A  24       0.054  -2.618  45.587  1.00114.37           C  
ATOM    208  CD1 TYR A  24       0.093  -1.492  44.735  1.00115.66           C  
ATOM    209  CD2 TYR A  24      -0.861  -2.604  46.666  1.00116.11           C  
ATOM    210  CE1 TYR A  24      -0.796  -0.408  44.920  1.00116.97           C  
ATOM    211  CE2 TYR A  24      -1.755  -1.528  46.856  1.00117.08           C  
ATOM    212  CZ  TYR A  24      -1.714  -0.437  45.985  1.00117.55           C  
ATOM    213  OH  TYR A  24      -2.590   0.613  46.181  1.00117.86           O  
HETATM  214  N   CGU A  25       1.003  -6.292  47.214  1.00110.69           N  
HETATM  215  CA  CGU A  25       1.718  -7.158  48.193  1.00110.59           C  
HETATM  216  C   CGU A  25       1.589  -8.690  47.962  1.00110.60           C  
HETATM  217  O   CGU A  25       2.548  -9.445  48.216  1.00110.49           O  
HETATM  218  CB  CGU A  25       1.388  -6.785  49.663  1.00110.38           C  
HETATM  219  CG  CGU A  25       1.909  -7.792  50.710  1.00109.90           C  
HETATM  220  CD1 CGU A  25       3.412  -7.802  50.874  1.00109.81           C  
HETATM  221  CD2 CGU A  25       1.388  -7.576  52.106  1.00109.35           C  
HETATM  222 OE11 CGU A  25       4.048  -6.734  50.737  1.00109.82           O  
HETATM  223 OE12 CGU A  25       3.951  -8.880  51.196  1.00109.67           O  
HETATM  224 OE21 CGU A  25       1.423  -8.549  52.890  1.00108.94           O  
HETATM  225 OE22 CGU A  25       0.997  -6.437  52.433  1.00109.15           O  
HETATM  226  N   CGU A  26       0.416  -9.140  47.503  1.00110.42           N  
HETATM  227  CA  CGU A  26       0.223 -10.539  47.095  1.00110.05           C  
HETATM  228  C   CGU A  26       1.232 -10.887  46.006  1.00110.34           C  
HETATM  229  O   CGU A  26       1.888 -11.940  46.053  1.00110.15           O  
HETATM  230  CB  CGU A  26      -1.201 -10.768  46.576  1.00109.61           C  
HETATM  231  CG  CGU A  26      -2.204 -11.260  47.601  1.00107.61           C  
HETATM  232  CD1 CGU A  26      -1.607 -12.213  48.622  1.00105.62           C  
HETATM  233  CD2 CGU A  26      -3.360 -11.953  46.935  1.00107.23           C  
HETATM  234 OE11 CGU A  26      -1.272 -13.358  48.263  1.00103.62           O  
HETATM  235 OE12 CGU A  26      -1.475 -11.818  49.795  1.00104.92           O  
HETATM  236 OE21 CGU A  26      -4.480 -11.419  46.976  1.00107.49           O  
HETATM  237 OE22 CGU A  26      -3.144 -13.028  46.349  1.00107.28           O  
ATOM    238  N   ALA A  27       1.331  -9.977  45.033  1.00110.73           N  
ATOM    239  CA  ALA A  27       2.367  -9.986  44.012  1.00111.22           C  
ATOM    240  C   ALA A  27       3.754 -10.092  44.656  1.00111.71           C  
ATOM    241  O   ALA A  27       4.476 -11.064  44.397  1.00111.81           O  
ATOM    242  CB  ALA A  27       2.263  -8.733  43.136  1.00110.90           C  
ATOM    243  N   PHE A  28       4.107  -9.123  45.511  1.00112.17           N  
ATOM    244  CA  PHE A  28       5.406  -9.131  46.197  1.00112.62           C  
ATOM    245  C   PHE A  28       5.733 -10.449  46.915  1.00113.02           C  
ATOM    246  O   PHE A  28       6.788 -11.031  46.666  1.00113.13           O  
ATOM    247  CB  PHE A  28       5.577  -7.957  47.169  1.00112.45           C  
ATOM    248  CG  PHE A  28       6.774  -8.112  48.079  1.00113.00           C  
ATOM    249  CD1 PHE A  28       8.059  -7.798  47.625  1.00113.21           C  
ATOM    250  CD2 PHE A  28       6.624  -8.617  49.381  1.00113.64           C  
ATOM    251  CE1 PHE A  28       9.176  -7.965  48.459  1.00113.39           C  
ATOM    252  CE2 PHE A  28       7.733  -8.787  50.231  1.00113.46           C  
ATOM    253  CZ  PHE A  28       9.010  -8.462  49.767  1.00113.71           C  
HETATM  254  N   CGU A  29       4.849 -10.908  47.806  1.00113.54           N  
HETATM  255  CA  CGU A  29       5.063 -12.172  48.542  1.00113.93           C  
HETATM  256  C   CGU A  29       5.467 -13.287  47.599  1.00114.63           C  
HETATM  257  O   CGU A  29       6.408 -14.033  47.864  1.00114.42           O  
HETATM  258  CB  CGU A  29       3.798 -12.616  49.280  1.00113.69           C  
HETATM  259  CG  CGU A  29       3.410 -11.797  50.503  1.00112.08           C  
HETATM  260  CD1 CGU A  29       4.391 -11.912  51.677  1.00111.20           C  
HETATM  261  CD2 CGU A  29       1.978 -12.062  50.935  1.00110.38           C  
HETATM  262 OE11 CGU A  29       4.342 -11.058  52.587  1.00110.41           O  
HETATM  263 OE12 CGU A  29       5.228 -12.843  51.696  1.00110.79           O  
HETATM  264 OE21 CGU A  29       1.396 -13.112  50.561  1.00108.04           O  
HETATM  265 OE22 CGU A  29       1.413 -11.202  51.636  1.00110.21           O  
ATOM    266  N   ALA A  30       4.721 -13.386  46.502  1.00115.73           N  
ATOM    267  CA  ALA A  30       5.012 -14.315  45.433  1.00117.00           C  
ATOM    268  C   ALA A  30       6.376 -14.038  44.788  1.00117.88           C  
ATOM    269  O   ALA A  30       7.133 -14.976  44.531  1.00117.97           O  
ATOM    270  CB  ALA A  30       3.897 -14.280  44.393  1.00116.83           C  
ATOM    271  N   LEU A  31       6.688 -12.761  44.550  1.00118.99           N  
ATOM    272  CA  LEU A  31       7.936 -12.367  43.872  1.00120.21           C  
ATOM    273  C   LEU A  31       9.194 -12.414  44.745  1.00121.07           C  
ATOM    274  O   LEU A  31       9.137 -12.169  45.955  1.00121.30           O  
ATOM    275  CB  LEU A  31       7.817 -10.970  43.242  1.00120.21           C  
ATOM    276  CG  LEU A  31       7.274 -10.794  41.816  1.00120.54           C  
ATOM    277  CD1 LEU A  31       8.101  -9.725  41.048  1.00120.16           C  
ATOM    278  CD2 LEU A  31       7.214 -12.121  41.031  1.00120.42           C  
HETATM  279  N   CGU A  32      10.328 -12.718  44.105  1.00122.12           N  
HETATM  280  CA  CGU A  32      11.649 -12.713  44.753  1.00123.11           C  
HETATM  281  C   CGU A  32      12.519 -11.576  44.176  1.00123.84           C  
HETATM  282  O   CGU A  32      13.346 -11.786  43.270  1.00123.83           O  
HETATM  283  CB  CGU A  32      12.337 -14.087  44.643  1.00123.05           C  
HETATM  284  CG  CGU A  32      11.402 -15.304  44.762  1.00123.32           C  
HETATM  285  CD1 CGU A  32      12.060 -16.630  44.380  1.00123.79           C  
HETATM  286  CD2 CGU A  32      10.665 -15.429  46.103  1.00123.00           C  
HETATM  287 OE11 CGU A  32      11.314 -17.603  44.077  1.00123.49           O  
HETATM  288 OE12 CGU A  32      13.318 -16.705  44.376  1.00123.80           O  
HETATM  289 OE21 CGU A  32       9.535 -15.978  46.097  1.00122.55           O  
HETATM  290 OE22 CGU A  32      11.194 -14.990  47.159  1.00122.49           O  
ATOM    291  N   SER A  33      12.275 -10.380  44.735  1.00124.77           N  
ATOM    292  CA  SER A  33      12.827  -9.045  44.369  1.00125.46           C  
ATOM    293  C   SER A  33      11.651  -8.051  44.427  1.00125.92           C  
ATOM    294  O   SER A  33      10.487  -8.447  44.223  1.00126.03           O  
ATOM    295  CB  SER A  33      13.552  -8.998  42.999  1.00125.43           C  
ATOM    296  OG  SER A  33      12.685  -8.685  41.919  1.00125.39           O  
ATOM    297  N   SER A  34      11.932  -6.782  44.731  1.00126.30           N  
ATOM    298  CA  SER A  34      10.863  -5.769  44.745  1.00126.61           C  
ATOM    299  C   SER A  34      10.838  -4.967  43.439  1.00126.78           C  
ATOM    300  O   SER A  34      10.537  -3.761  43.424  1.00126.81           O  
ATOM    301  CB  SER A  34      10.924  -4.866  45.984  1.00126.54           C  
ATOM    302  OG  SER A  34      11.755  -3.740  45.771  1.00126.73           O  
ATOM    303  N   THR A  35      11.159  -5.667  42.348  1.00126.91           N  
ATOM    304  CA  THR A  35      10.977  -5.160  40.995  1.00126.93           C  
ATOM    305  C   THR A  35       9.488  -4.889  40.713  1.00127.14           C  
ATOM    306  O   THR A  35       8.774  -5.738  40.154  1.00127.21           O  
ATOM    307  CB  THR A  35      11.570  -6.128  39.939  1.00126.81           C  
ATOM    308  OG1 THR A  35      10.986  -7.429  40.092  1.00126.43           O  
ATOM    309  CG2 THR A  35      13.086  -6.222  40.089  1.00126.48           C  
ATOM    310  N   ALA A  36       9.024  -3.724  41.173  1.00127.22           N  
ATOM    311  CA  ALA A  36       7.793  -3.122  40.687  1.00127.40           C  
ATOM    312  C   ALA A  36       8.281  -2.455  39.411  1.00127.48           C  
ATOM    313  O   ALA A  36       8.868  -1.366  39.453  1.00127.53           O  
ATOM    314  CB  ALA A  36       7.248  -2.102  41.694  1.00127.37           C  
ATOM    315  N   THR A  37       8.064  -3.130  38.281  1.00127.55           N  
ATOM    316  CA  THR A  37       9.058  -3.077  37.192  1.00127.67           C  
ATOM    317  C   THR A  37       8.952  -2.015  36.062  1.00127.57           C  
ATOM    318  O   THR A  37       9.921  -1.256  35.852  1.00127.66           O  
ATOM    319  CB  THR A  37       9.441  -4.511  36.679  1.00127.76           C  
ATOM    320  OG1 THR A  37       9.380  -4.564  35.247  1.00127.78           O  
ATOM    321  CG2 THR A  37       8.513  -5.565  37.274  1.00127.71           C  
ATOM    322  N   ASP A  38       7.816  -1.986  35.348  1.00127.23           N  
ATOM    323  CA  ASP A  38       7.585  -1.083  34.182  1.00126.84           C  
ATOM    324  C   ASP A  38       6.623  -1.701  33.167  1.00126.53           C  
ATOM    325  O   ASP A  38       5.414  -1.442  33.219  1.00126.73           O  
ATOM    326  CB  ASP A  38       8.885  -0.641  33.475  1.00126.85           C  
ATOM    327  CG  ASP A  38       9.186   0.836  33.666  1.00126.56           C  
ATOM    328  OD1 ASP A  38       8.277   1.660  33.426  1.00126.02           O  
ATOM    329  OD2 ASP A  38      10.333   1.169  34.041  1.00126.45           O  
ATOM    330  N   VAL A  39       7.158  -2.512  32.248  1.00125.91           N  
ATOM    331  CA  VAL A  39       6.321  -3.308  31.343  1.00125.15           C  
ATOM    332  C   VAL A  39       5.886  -4.645  32.010  1.00124.63           C  
ATOM    333  O   VAL A  39       5.357  -5.537  31.336  1.00124.54           O  
ATOM    334  CB  VAL A  39       6.968  -3.464  29.911  1.00125.24           C  
ATOM    335  CG1 VAL A  39       7.802  -4.768  29.765  1.00124.86           C  
ATOM    336  CG2 VAL A  39       5.898  -3.337  28.821  1.00124.88           C  
ATOM    337  N   PHE A  40       6.085  -4.744  33.336  1.00123.81           N  
ATOM    338  CA  PHE A  40       5.704  -5.926  34.151  1.00122.94           C  
ATOM    339  C   PHE A  40       4.552  -5.698  35.168  1.00122.06           C  
ATOM    340  O   PHE A  40       3.757  -6.612  35.441  1.00121.79           O  
ATOM    341  CB  PHE A  40       6.932  -6.559  34.828  1.00123.13           C  
ATOM    342  CG  PHE A  40       6.614  -7.777  35.651  1.00123.28           C  
ATOM    343  CD1 PHE A  40       6.724  -9.047  35.099  1.00123.25           C  
ATOM    344  CD2 PHE A  40       6.198  -7.650  36.973  1.00123.15           C  
ATOM    345  CE1 PHE A  40       6.425 -10.167  35.839  1.00123.07           C  
ATOM    346  CE2 PHE A  40       5.900  -8.757  37.717  1.00123.42           C  
ATOM    347  CZ  PHE A  40       6.013 -10.025  37.151  1.00123.49           C  
ATOM    348  N   TRP A  41       4.474  -4.500  35.744  1.00120.89           N  
ATOM    349  CA  TRP A  41       3.185  -4.037  36.221  1.00119.80           C  
ATOM    350  C   TRP A  41       2.315  -3.804  34.984  1.00119.22           C  
ATOM    351  O   TRP A  41       1.095  -3.865  35.076  1.00119.30           O  
ATOM    352  CB  TRP A  41       3.279  -2.763  37.060  1.00119.81           C  
ATOM    353  CG  TRP A  41       2.842  -2.919  38.514  1.00119.34           C  
ATOM    354  CD1 TRP A  41       3.633  -2.775  39.622  1.00119.33           C  
ATOM    355  CD2 TRP A  41       1.517  -3.214  39.008  1.00118.47           C  
ATOM    356  NE1 TRP A  41       2.893  -2.970  40.766  1.00118.94           N  
ATOM    357  CE2 TRP A  41       1.595  -3.247  40.420  1.00118.48           C  
ATOM    358  CE3 TRP A  41       0.280  -3.460  38.398  1.00118.14           C  
ATOM    359  CZ2 TRP A  41       0.479  -3.523  41.234  1.00117.78           C  
ATOM    360  CZ3 TRP A  41      -0.833  -3.733  39.210  1.00117.66           C  
ATOM    361  CH2 TRP A  41      -0.719  -3.762  40.610  1.00117.39           C  
ATOM    362  N   ALA A  42       2.942  -3.541  33.831  1.00118.28           N  
ATOM    363  CA  ALA A  42       2.221  -3.478  32.542  1.00117.42           C  
ATOM    364  C   ALA A  42       1.955  -4.870  31.951  1.00116.80           C  
ATOM    365  O   ALA A  42       0.934  -5.080  31.277  1.00116.80           O  
ATOM    366  CB  ALA A  42       2.938  -2.579  31.531  1.00117.34           C  
ATOM    367  N   LYS A  43       2.862  -5.818  32.204  1.00115.86           N  
ATOM    368  CA  LYS A  43       2.567  -7.227  31.950  1.00114.87           C  
ATOM    369  C   LYS A  43       1.241  -7.508  32.623  1.00114.37           C  
ATOM    370  O   LYS A  43       0.401  -8.222  32.082  1.00114.57           O  
ATOM    371  CB  LYS A  43       3.663  -8.152  32.478  1.00114.74           C  
ATOM    372  CG  LYS A  43       4.583  -8.713  31.399  1.00114.15           C  
ATOM    373  CD  LYS A  43       5.946  -9.079  31.971  1.00113.28           C  
ATOM    374  CE  LYS A  43       6.665 -10.111  31.125  1.00112.91           C  
ATOM    375  NZ  LYS A  43       6.136 -11.490  31.347  1.00112.65           N  
ATOM    376  N   TYR A  44       1.036  -6.900  33.785  1.00113.48           N  
ATOM    377  CA  TYR A  44      -0.296  -6.849  34.341  1.00112.81           C  
ATOM    378  C   TYR A  44      -1.163  -5.765  33.653  1.00112.02           C  
ATOM    379  O   TYR A  44      -2.031  -6.113  32.857  1.00111.68           O  
ATOM    380  CB  TYR A  44      -0.270  -6.736  35.878  1.00113.12           C  
ATOM    381  CG  TYR A  44      -1.593  -7.100  36.535  1.00113.76           C  
ATOM    382  CD1 TYR A  44      -1.930  -8.439  36.789  1.00113.99           C  
ATOM    383  CD2 TYR A  44      -2.516  -6.104  36.886  1.00114.04           C  
ATOM    384  CE1 TYR A  44      -3.146  -8.771  37.373  1.00113.92           C  
ATOM    385  CE2 TYR A  44      -3.727  -6.426  37.467  1.00114.25           C  
ATOM    386  CZ  TYR A  44      -4.034  -7.758  37.705  1.00114.36           C  
ATOM    387  OH  TYR A  44      -5.237  -8.069  38.281  1.00115.54           O  
ATOM    388  N   THR A  45      -0.901  -4.478  33.917  1.00111.25           N  
ATOM    389  CA  THR A  45      -1.862  -3.381  33.605  1.00110.68           C  
ATOM    390  C   THR A  45      -2.201  -3.079  32.141  1.00110.23           C  
ATOM    391  O   THR A  45      -3.237  -2.466  31.885  1.00110.22           O  
ATOM    392  CB  THR A  45      -1.543  -2.025  34.318  1.00110.68           C  
ATOM    393  OG1 THR A  45      -0.201  -1.625  34.035  1.00110.58           O  
ATOM    394  CG2 THR A  45      -1.755  -2.110  35.827  1.00110.70           C  
ATOM    395  N   ALA A  46      -1.344  -3.472  31.196  1.00109.75           N  
ATOM    396  CA  ALA A  46      -1.713  -3.436  29.765  1.00109.21           C  
ATOM    397  C   ALA A  46      -2.546  -4.677  29.410  1.00108.84           C  
ATOM    398  O   ALA A  46      -3.257  -4.702  28.392  1.00108.76           O  
ATOM    399  CB  ALA A  46      -0.479  -3.317  28.855  1.00109.06           C  
ATOM    400  N   CYS A  47      -2.461  -5.692  30.273  1.00108.19           N  
ATOM    401  CA  CYS A  47      -3.268  -6.906  30.142  1.00107.56           C  
ATOM    402  C   CYS A  47      -4.666  -6.828  30.803  1.00107.09           C  
ATOM    403  O   CYS A  47      -5.436  -7.791  30.731  1.00106.90           O  
ATOM    404  CB  CYS A  47      -2.486  -8.131  30.653  1.00107.46           C  
ATOM    405  SG  CYS A  47      -1.296  -8.871  29.458  1.00107.45           S  
ATOM    406  N   GLU A  48      -4.997  -5.693  31.426  1.00106.48           N  
ATOM    407  CA  GLU A  48      -6.308  -5.519  32.075  1.00105.84           C  
ATOM    408  C   GLU A  48      -7.489  -5.490  31.099  1.00105.73           C  
ATOM    409  O   GLU A  48      -8.575  -5.975  31.425  1.00105.56           O  
ATOM    410  CB  GLU A  48      -6.310  -4.297  32.984  1.00105.54           C  
ATOM    411  CG  GLU A  48      -5.813  -4.617  34.372  1.00104.74           C  
ATOM    412  CD  GLU A  48      -5.112  -3.448  35.026  1.00104.30           C  
ATOM    413  OE1 GLU A  48      -4.705  -3.589  36.200  1.00103.71           O  
ATOM    414  OE2 GLU A  48      -4.962  -2.392  34.367  1.00103.59           O  
ATOM    415  N   THR A  49      -7.270  -4.947  29.901  1.00105.75           N  
ATOM    416  CA  THR A  49      -8.241  -5.055  28.798  1.00105.73           C  
ATOM    417  C   THR A  49      -8.557  -6.530  28.498  1.00105.66           C  
ATOM    418  O   THR A  49      -9.265  -6.838  27.535  1.00105.63           O  
ATOM    419  CB  THR A  49      -7.782  -4.303  27.488  1.00105.85           C  
ATOM    420  OG1 THR A  49      -6.380  -4.510  27.248  1.00106.08           O  
ATOM    421  CG2 THR A  49      -8.063  -2.792  27.576  1.00105.60           C  
ATOM    422  N   ALA A  50      -8.005  -7.421  29.329  1.00105.58           N  
ATOM    423  CA  ALA A  50      -8.349  -8.849  29.368  1.00105.55           C  
ATOM    424  C   ALA A  50      -8.525  -9.303  30.826  1.00105.58           C  
ATOM    425  O   ALA A  50      -7.812  -8.849  31.730  1.00105.68           O  
ATOM    426  CB  ALA A  50      -7.300  -9.686  28.663  1.00105.36           C  
ATOM    427  N   ARG A  51      -9.479 -10.202  31.047  1.00105.39           N  
ATOM    428  CA  ARG A  51      -9.971 -10.488  32.389  1.00105.04           C  
ATOM    429  C   ARG A  51     -10.786 -11.790  32.423  1.00104.56           C  
ATOM    430  O   ARG A  51     -11.274 -12.194  33.481  1.00104.56           O  
ATOM    431  CB  ARG A  51     -10.830  -9.311  32.881  1.00105.22           C  
ATOM    432  CG  ARG A  51     -10.778  -9.081  34.382  1.00106.18           C  
ATOM    433  CD  ARG A  51     -11.840  -8.079  34.877  1.00107.84           C  
ATOM    434  NE  ARG A  51     -11.722  -7.861  36.324  1.00109.23           N  
ATOM    435  CZ  ARG A  51     -12.518  -8.391  37.256  1.00109.96           C  
ATOM    436  NH1 ARG A  51     -13.544  -9.172  36.922  1.00110.03           N  
ATOM    437  NH2 ARG A  51     -12.288  -8.129  38.539  1.00110.33           N  
ATOM    438  N   THR A  52     -10.947 -12.447  31.277  1.00103.76           N  
ATOM    439  CA  THR A  52     -11.604 -13.755  31.271  1.00103.04           C  
ATOM    440  C   THR A  52     -10.608 -14.881  31.717  1.00102.58           C  
ATOM    441  O   THR A  52      -9.658 -14.567  32.437  1.00102.55           O  
ATOM    442  CB  THR A  52     -12.515 -13.970  30.012  1.00103.01           C  
ATOM    443  OG1 THR A  52     -13.171 -15.241  30.089  1.00103.56           O  
ATOM    444  CG2 THR A  52     -11.756 -13.871  28.715  1.00102.87           C  
TER     445      THR A  52                                                      
HETATM 4323 CA    CA A 602      -0.409 -12.239  51.841  1.00100.53          CA  
HETATM 4324 CA    CA A 603       0.434 -14.522  48.911  1.00 86.87          CA  
HETATM 4325 CA    CA A 604      -3.700 -15.245  48.413  1.00 97.95          CA  
HETATM 4326 CA    CA A 605      -6.479 -17.105  46.987  1.00101.28          CA  
HETATM 4327 CA    CA A 606      -8.782 -19.592  44.310  1.00 68.15          CA  
CONECT    4 4325                                                                
CONECT   34   40                                                                
CONECT   40   34   41                                                           
CONECT   41   40   42   44                                                      
CONECT   42   41   43   52                                                      
CONECT   43   42                                                                
CONECT   44   41   45                                                           
CONECT   45   44   46   47                                                      
CONECT   46   45   48   49                                                      
CONECT   47   45   50   51                                                      
CONECT   48   46 4325                                                           
CONECT   49   46 4326                                                           
CONECT   50   47                                                                
CONECT   51   47                                                                
CONECT   52   42   53                                                           
CONECT   53   52   54   56                                                      
CONECT   54   53   55   64                                                      
CONECT   55   54                                                                
CONECT   56   53   57                                                           
CONECT   57   56   58   59                                                      
CONECT   58   57   60   61                                                      
CONECT   59   57   62   63                                                      
CONECT   60   58                                                                
CONECT   61   58 4323                                                           
CONECT   62   59 4323 4324                                                      
CONECT   63   59 4325                                                           
CONECT   64   54                                                                
CONECT  105  111                                                                
CONECT  111  105  112                                                           
CONECT  112  111  113  115                                                      
CONECT  113  112  114  123                                                      
CONECT  114  113                                                                
CONECT  115  112  116                                                           
CONECT  116  115  117  118                                                      
CONECT  117  116  119  120                                                      
CONECT  118  116  121  122                                                      
CONECT  119  117                                                                
CONECT  120  117                                                                
CONECT  121  118                                                                
CONECT  122  118                                                                
CONECT  123  113                                                                
CONECT  125  134                                                                
CONECT  134  125  135                                                           
CONECT  135  134  136  138                                                      
CONECT  136  135  137  146                                                      
CONECT  137  136                                                                
CONECT  138  135  139                                                           
CONECT  139  138  140  141                                                      
CONECT  140  139  142  143                                                      
CONECT  141  139  144  145                                                      
CONECT  142  140                                                                
CONECT  143  140 4324                                                           
CONECT  144  141 4325 4326                                                      
CONECT  145  141 4325 4326                                                      
CONECT  146  136                                                                
CONECT  151  195                                                                
CONECT  154  159                                                                
CONECT  159  154  160                                                           
CONECT  160  159  161  163                                                      
CONECT  161  160  162  171                                                      
CONECT  162  161                                                                
CONECT  163  160  164                                                           
CONECT  164  163  165  166                                                      
CONECT  165  164  167  168                                                      
CONECT  166  164  169  170                                                      
CONECT  167  165                                                                
CONECT  168  165                                                                
CONECT  169  166                                                                
CONECT  170  166                                                                
CONECT  171  161  172                                                           
CONECT  172  171  173  175                                                      
CONECT  173  172  174  183                                                      
CONECT  174  173                                                                
CONECT  175  172  176                                                           
CONECT  176  175  177  178                                                      
CONECT  177  176  179  180                                                      
CONECT  178  176  181  182                                                      
CONECT  179  177                                                                
CONECT  180  177 4326 4327                                                      
CONECT  181  178                                                                
CONECT  182  178 4327                                                           
CONECT  183  173                                                                
CONECT  195  151                                                                
CONECT  204  214                                                                
CONECT  214  204  215                                                           
CONECT  215  214  216  218                                                      
CONECT  216  215  217  226                                                      
CONECT  217  216                                                                
CONECT  218  215  219                                                           
CONECT  219  218  220  221                                                      
CONECT  220  219  222  223                                                      
CONECT  221  219  224  225                                                      
CONECT  222  220                                                                
CONECT  223  220                                                                
CONECT  224  221                                                                
CONECT  225  221                                                                
CONECT  226  216  227                                                           
CONECT  227  226  228  230                                                      
CONECT  228  227  229  238                                                      
CONECT  229  228                                                                
CONECT  230  227  231                                                           
CONECT  231  230  232  233                                                      
CONECT  232  231  234  235                                                      
CONECT  233  231  236  237                                                      
CONECT  234  232 4324 4325                                                      
CONECT  235  232 4323                                                           
CONECT  236  233                                                                
CONECT  237  233 4325                                                           
CONECT  238  228                                                                
CONECT  245  254                                                                
CONECT  254  245  255                                                           
CONECT  255  254  256  258                                                      
CONECT  256  255  257  266                                                      
CONECT  257  256                                                                
CONECT  258  255  259                                                           
CONECT  259  258  260  261                                                      
CONECT  260  259  262  263                                                      
CONECT  261  259  264  265                                                      
CONECT  262  260                                                                
CONECT  263  260                                                                
CONECT  264  261 4323 4324                                                      
CONECT  265  261 4323                                                           
CONECT  266  256                                                                
CONECT  273  279                                                                
CONECT  279  273  280                                                           
CONECT  280  279  281  283                                                      
CONECT  281  280  282  291                                                      
CONECT  282  281                                                                
CONECT  283  280  284                                                           
CONECT  284  283  285  286                                                      
CONECT  285  284  287  288                                                      
CONECT  286  284  289  290                                                      
CONECT  287  285                                                                
CONECT  288  285                                                                
CONECT  289  286                                                                
CONECT  290  286                                                                
CONECT  291  281                                                                
CONECT  405  497                                                                
CONECT  497  405                                                                
CONECT  532 1148                                                                
CONECT  629 4342                                                                
CONECT  688 1013                                                                
CONECT  817 4356                                                                
CONECT  922 1114                                                                
CONECT 1013  688                                                                
CONECT 1114  922                                                                
CONECT 1148  532                                                                
CONECT 1185 1787                                                                
CONECT 1345 1656                                                                
CONECT 1561 1745                                                                
CONECT 1656 1345                                                                
CONECT 1745 1561                                                                
CONECT 1787 1185                                                                
CONECT 2002 3214                                                                
CONECT 2447 2565                                                                
CONECT 2565 2447                                                                
CONECT 2646 4328                                                                
CONECT 3214 2002                                                                
CONECT 3623 3739                                                                
CONECT 3739 3623                                                                
CONECT 3840 4073                                                                
CONECT 4073 3840                                                                
CONECT 4323   61   62  235  264                                                 
CONECT 4323  265                                                                
CONECT 4324   62  143  234  264                                                 
CONECT 4325    4   48   63  144                                                 
CONECT 4325  145  234  237                                                      
CONECT 4326   49  144  145  180                                                 
CONECT 4327  180  182                                                           
CONECT 4328 2646 4329 4339                                                      
CONECT 4329 4328 4330 4336                                                      
CONECT 4330 4329 4331 4337                                                      
CONECT 4331 4330 4332 4338                                                      
CONECT 4332 4331 4333 4339                                                      
CONECT 4333 4332 4340                                                           
CONECT 4334 4335 4336 4341                                                      
CONECT 4335 4334                                                                
CONECT 4336 4329 4334                                                           
CONECT 4337 4330                                                                
CONECT 4338 4331                                                                
CONECT 4339 4328 4332                                                           
CONECT 4340 4333                                                                
CONECT 4341 4334                                                                
CONECT 4342  629 4343 4353                                                      
CONECT 4343 4342 4344 4350                                                      
CONECT 4344 4343 4345 4351                                                      
CONECT 4345 4344 4346 4352                                                      
CONECT 4346 4345 4347 4353                                                      
CONECT 4347 4346 4354                                                           
CONECT 4348 4349 4350 4355                                                      
CONECT 4349 4348                                                                
CONECT 4350 4343 4348                                                           
CONECT 4351 4344                                                                
CONECT 4352 4345                                                                
CONECT 4353 4342 4346                                                           
CONECT 4354 4347                                                                
CONECT 4355 4348                                                                
CONECT 4356  817 4357 4367                                                      
CONECT 4357 4356 4358 4364                                                      
CONECT 4358 4357 4359 4365                                                      
CONECT 4359 4358 4360 4366                                                      
CONECT 4360 4359 4361 4367                                                      
CONECT 4361 4360 4368                                                           
CONECT 4362 4363 4364 4369                                                      
CONECT 4363 4362                                                                
CONECT 4364 4357 4362                                                           
CONECT 4365 4358                                                                
CONECT 4366 4359                                                                
CONECT 4367 4356 4360                                                           
CONECT 4368 4361                                                                
CONECT 4369 4362                                                                
MASTER      458    0   18   12   21    0    0    6 4368    1  211   43          
END                                                                             


A second structure was input as follows:


HEADER    HYDROLASE                               21-OCT-15   5EDM              
TITLE     CRYSTAL STRUCTURE OF PROTHROMBIN DELETION MUTANT RESIDUES 154-167 (   
TITLE    2 FORM I )                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTHROMBIN;                                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: COAGULATION FACTOR II;                                      
COMPND   5 EC: 3.4.21.5;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: F2;                                                            
SOURCE   6 EXPRESSION_SYSTEM: MESOCRICETUS AURATUS;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10036;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: BABY HAMSTER KIDNEY (BHK)               
KEYWDS    PROTHROMBIN, KRINGLE, PROTEASE, COAGULATION FACTOR, ENZYME MECHANISM, 
KEYWDS   2 KINETICS, STRUCTURE-FUNCTION, HYDROLASE                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.POZZI,Z.CHEN,E.DI CERA                                              
REVDAT   7   29-JUL-20 5EDM    1       COMPND REMARK HETNAM LINK                
REVDAT   7 2                   1       SITE   ATOM                              
REVDAT   6   04-DEC-19 5EDM    1       REMARK                                   
REVDAT   5   06-SEP-17 5EDM    1       REMARK                                   
REVDAT   4   09-AUG-17 5EDM    1       JRNL   REMARK                            
REVDAT   3   30-MAR-16 5EDM    1       JRNL                                     
REVDAT   2   27-JAN-16 5EDM    1       JRNL                                     
REVDAT   1   20-JAN-16 5EDM    0                                                
JRNL        AUTH   N.POZZI,Z.CHEN,E.DI CERA                                     
JRNL        TITL   HOW THE LINKER CONNECTING THE TWO KRINGLES INFLUENCES        
JRNL        TITL 2 ACTIVATION AND CONFORMATIONAL PLASTICITY OF PROTHROMBIN.     
JRNL        REF    J.BIOL.CHEM.                  V. 291  6071 2016              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   26763231                                                     
JRNL        DOI    10.1074/JBC.M115.700401                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 92.07                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 63362                          
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) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3409                            
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4609                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.67                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3960                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 222                          
REMARK   3   BIN FREE R VALUE                    : 0.3860                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4414                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 127                                     
REMARK   3   SOLVENT ATOMS            : 464                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 59.17                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.78000                                             
REMARK   3    B22 (A**2) : -1.20000                                             
REMARK   3    B33 (A**2) : 1.98000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.151         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.150         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.150         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.149        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4708 ; 0.012 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4172 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6356 ; 1.681 ; 1.996       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9609 ; 0.812 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   548 ; 6.623 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   217 ;36.131 ;23.641       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   732 ;16.169 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    36 ;16.922 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   683 ; 0.116 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5217 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1069 ; 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):  2198 ; 1.706 ; 3.020       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2197 ; 1.706 ; 3.019       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2744 ; 2.824 ; 4.522       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2745 ; 2.824 ; 4.523       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2510 ; 3.603 ; 3.720       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2506 ; 3.497 ; 3.713       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3607 ; 4.728 ; 5.414       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  5818 ; 9.711 ;27.680       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  5613 ; 9.627 ;26.645       
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  : 10                                         
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     1        A    12                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.6067  45.3648  15.4617              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9070 T22:   0.6172                                     
REMARK   3      T33:   0.2624 T12:  -0.0044                                     
REMARK   3      T13:  -0.0023 T23:  -0.1405                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9409 L22:   1.3028                                     
REMARK   3      L33:  10.9528 L12:   1.5693                                     
REMARK   3      L13:  -1.4774 L23:   2.3537                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2886 S12:   0.7663 S13:  -0.6041                       
REMARK   3      S21:  -0.2413 S22:   0.1242 S23:  -0.1841                       
REMARK   3      S31:   0.2551 S32:  -0.4842 S33:   0.1645                       
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 :   A    13        A   154                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.5578  30.6996  17.3732              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3692 T22:   0.0854                                     
REMARK   3      T33:   0.0421 T12:  -0.0452                                     
REMARK   3      T13:  -0.0580 T23:  -0.0353                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7815 L22:   4.6379                                     
REMARK   3      L33:   2.7065 L12:   3.3584                                     
REMARK   3      L13:   1.7103 L23:   3.0241                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1521 S12:  -0.1950 S13:  -0.0291                       
REMARK   3      S21:   0.1603 S22:  -0.0561 S23:  -0.1140                       
REMARK   3      S31:  -0.0605 S32:   0.1536 S33:  -0.0960                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   155        A   193                          
REMARK   3    ORIGIN FOR THE GROUP (A): -43.6934   6.8702  14.5124              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3620 T22:   0.1132                                     
REMARK   3      T33:   0.1761 T12:   0.0032                                     
REMARK   3      T13:   0.0423 T23:   0.0245                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.0123 L22:   4.6045                                     
REMARK   3      L33:   7.5378 L12:   0.1431                                     
REMARK   3      L13:  -1.0120 L23:  -1.2227                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1778 S12:  -0.4412 S13:   0.4957                       
REMARK   3      S21:   0.2803 S22:   0.1771 S23:   0.6789                       
REMARK   3      S31:  -0.0587 S32:  -0.7997 S33:  -0.3548                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   194        A   235                          
REMARK   3    ORIGIN FOR THE GROUP (A): -42.4932   4.8457  15.5237              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3004 T22:   0.0383                                     
REMARK   3      T33:   0.0848 T12:  -0.0201                                     
REMARK   3      T13:   0.0713 T23:   0.0198                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0147 L22:   6.3070                                     
REMARK   3      L33:   4.6774 L12:  -0.7963                                     
REMARK   3      L13:   1.5553 L23:  -1.0952                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0377 S12:   0.0642 S13:   0.1623                       
REMARK   3      S21:   0.1480 S22:   0.1389 S23:   0.2843                       
REMARK   3      S31:  -0.1464 S32:  -0.3604 S33:  -0.1766                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   236        A   274                          
REMARK   3    ORIGIN FOR THE GROUP (A): -39.5416  -8.5558  29.7766              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3398 T22:   0.2597                                     
REMARK   3      T33:   0.2839 T12:   0.0178                                     
REMARK   3      T13:   0.0269 T23:  -0.0158                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4338 L22:   1.0055                                     
REMARK   3      L33:   0.9580 L12:   0.4115                                     
REMARK   3      L13:   0.2122 L23:  -0.0931                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0558 S12:  -0.2406 S13:   0.1482                       
REMARK   3      S21:   0.1234 S22:  -0.0210 S23:  -0.0504                       
REMARK   3      S31:  -0.0870 S32:   0.0856 S33:  -0.0349                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   275        A   398                          
REMARK   3    ORIGIN FOR THE GROUP (A): -41.4927 -25.9311  20.1558              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3255 T22:   0.0114                                     
REMARK   3      T33:   0.1441 T12:  -0.0087                                     
REMARK   3      T13:   0.1023 T23:   0.0149                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7429 L22:   3.0166                                     
REMARK   3      L33:   3.9499 L12:  -0.2014                                     
REMARK   3      L13:  -0.5699 L23:  -0.6002                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0557 S12:   0.0008 S13:  -0.2551                       
REMARK   3      S21:   0.3075 S22:  -0.0318 S23:   0.2496                       
REMARK   3      S31:   0.4287 S32:  -0.0885 S33:   0.0875                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   399        A   460                          
REMARK   3    ORIGIN FOR THE GROUP (A): -37.3680 -21.0405  19.8351              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2450 T22:   0.0369                                     
REMARK   3      T33:   0.0245 T12:   0.0232                                     
REMARK   3      T13:   0.0320 T23:   0.0085                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0285 L22:   4.0088                                     
REMARK   3      L33:   4.2306 L12:  -0.8631                                     
REMARK   3      L13:  -0.4932 L23:   0.0946                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0479 S12:   0.0905 S13:  -0.0983                       
REMARK   3      S21:   0.2606 S22:   0.0251 S23:   0.0185                       
REMARK   3      S31:   0.3076 S32:   0.3115 S33:   0.0228                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   461        A   485                          
REMARK   3    ORIGIN FOR THE GROUP (A): -24.5488 -22.8076  16.6426              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2987 T22:   0.1452                                     
REMARK   3      T33:   0.1011 T12:   0.0842                                     
REMARK   3      T13:  -0.0265 T23:   0.0133                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.2793 L22:   5.9940                                     
REMARK   3      L33:   4.7235 L12:   3.1072                                     
REMARK   3      L13:  -2.4526 L23:  -2.3753                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0287 S12:   0.1717 S13:   0.3888                       
REMARK   3      S21:   0.0783 S22:   0.0788 S23:  -0.2735                       
REMARK   3      S31:  -0.3155 S32:   0.4390 S33:  -0.0500                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   486        A   505                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.1491 -20.9378  13.5968              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5188 T22:   0.3063                                     
REMARK   3      T33:   0.5833 T12:  -0.0673                                     
REMARK   3      T13:   0.2169 T23:   0.0163                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5256 L22:   5.3371                                     
REMARK   3      L33:   6.9945 L12:  -3.5201                                     
REMARK   3      L13:   1.2596 L23:   1.9399                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6094 S12:   0.4873 S13:   0.2207                       
REMARK   3      S21:  -0.8092 S22:  -0.0140 S23:  -0.8332                       
REMARK   3      S31:   0.3997 S32:   0.9811 S33:  -0.5954                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   506        A   568                          
REMARK   3    ORIGIN FOR THE GROUP (A): -36.3913 -15.8540  20.0166              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2989 T22:   0.0364                                     
REMARK   3      T33:   0.0263 T12:  -0.0580                                     
REMARK   3      T13:   0.0022 T23:   0.0140                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8433 L22:   3.9782                                     
REMARK   3      L33:   4.8722 L12:  -0.6768                                     
REMARK   3      L13:  -0.6596 L23:   0.7344                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0064 S12:   0.0888 S13:   0.0099                       
REMARK   3      S21:   0.2856 S22:   0.0168 S23:   0.2366                       
REMARK   3      S31:  -0.0255 S32:   0.2010 S33:  -0.0104                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3   POSITIONS                                                          
REMARK   4                                                                      
REMARK   4 5EDM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-OCT-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000214396.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-AUG-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 67055                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 92.070                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -0.300                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.08700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 17.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.24                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.000                              
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: PDB CODE 4O03                                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES, PH 6.5 AND 1.6 M MGSO4,       
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       72.15750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       72.15750            
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        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       54.94200            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       84.34500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       54.94200            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       84.34500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       72.15750            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       54.94200            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       84.34500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       72.15750            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       54.94200            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       84.34500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3270 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -133.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A1087  LIES ON A SPECIAL POSITION.                          
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   243                                                      
REMARK 465     ASP A   244                                                      
REMARK 465     GLY A   245                                                      
REMARK 465     LEU A   246                                                      
REMARK 465     ASP A   247                                                      
REMARK 465     GLU A   248                                                      
REMARK 465     ASP A   249                                                      
REMARK 465     SER A   250                                                      
REMARK 465     ASP A   251                                                      
REMARK 465     ARG A   252                                                      
REMARK 465     ALA A   253                                                      
REMARK 465     ILE A   254                                                      
REMARK 465     GLU A   255                                                      
REMARK 465     GLY A   256                                                      
REMARK 465     ARG A   257                                                      
REMARK 465     THR A   258                                                      
REMARK 465     ALA A   259                                                      
REMARK 465     THR A   260                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500  OE12  CGU A    20     O    HOH A   701              1.73            
REMARK 500   O    HOH A  1032     O    HOH A  1054              2.11            
REMARK 500   O    HOH A   951     O    HOH A  1037              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LYS A  96   C     LYS A  96   O      -0.188                       
REMARK 500    PRO A  97   CA    PRO A  97   CB     -0.163                       
REMARK 500    PRO A  97   CG    PRO A  97   CD     -0.201                       
REMARK 500    PRO A  97   CA    PRO A  97   C      -0.156                       
REMARK 500    PRO A  97   C     PRO A  97   O      -0.194                       
REMARK 500    GLU A  98   CA    GLU A  98   CB     -0.237                       
REMARK 500    GLU A  98   CB    GLU A  98   CG     -0.203                       
REMARK 500    GLU A  98   CG    GLU A  98   CD     -0.128                       
REMARK 500    GLU A  98   CD    GLU A  98   OE1    -0.091                       
REMARK 500    GLU A  98   CD    GLU A  98   OE2    -0.096                       
REMARK 500    GLU A  98   C     GLU A  98   O      -0.220                       
REMARK 500    ILE A  99   C     ILE A  99   O      -0.227                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASN A  78   CB  -  CA  -  C   ANGL. DEV. = -15.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A   2      -99.52     48.58                                   
REMARK 500    GLU A 111     -126.35     40.38                                   
REMARK 500    LYS A 190      -55.78    -18.07                                   
REMARK 500    HIS A 191       22.26   -142.57                                   
REMARK 500    GLU A 202     -117.98     50.41                                   
REMARK 500    GLU A 239      -32.39    -36.31                                   
REMARK 500    PHE A 285      -73.84   -130.41                                   
REMARK 500    ILE A 303       49.54     33.97                                   
REMARK 500    SER A 318       64.02   -151.25                                   
REMARK 500    GLU A 331      128.37   -172.30                                   
REMARK 500    TYR A 353       86.16   -151.48                                   
REMARK 500    HIS A 372      -55.90   -126.92                                   
REMARK 500    GLU A 378       79.11   -106.50                                   
REMARK 500    GLU A 400      -85.56    -95.35                                   
REMARK 500    ASN A 401       48.17   -154.79                                   
REMARK 500    LYS A 460      105.25    -20.48                                   
REMARK 500    ASP A 489        3.21    -69.70                                   
REMARK 500    CYS A 507       44.45   -145.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                              MG A 606  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU A  14  OE12                                                    
REMARK 620 2 CGU A  14  OE22  78.9                                              
REMARK 620 3 CGU A  19  OE11  94.1  77.8                                        
REMARK 620 4 CGU A  19  OE21  97.4 156.9  79.8                                  
REMARK 620 5 HOH A 770   O   148.0  74.0  96.6 114.2                            
REMARK 620 6 HOH A 982   O    87.7  91.0 168.0 111.7  76.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 604  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU A  16  OE12                                                    
REMARK 620 2 CGU A  16  OE22  98.6                                              
REMARK 620 3 CGU A  26  OE12 101.1 156.5                                        
REMARK 620 4 CGU A  26  OE21  98.9  89.5  74.9                                  
REMARK 620 5 HOH A 710   O   167.1  94.0  66.0  78.2                            
REMARK 620 6 HOH A 744   O   100.1 116.4  72.5 144.9  76.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 605  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU A  20  OE12                                                    
REMARK 620 2 CGU A  20  OE22  79.8                                              
REMARK 620 3 HOH A 701   O    47.0 112.3                                        
REMARK 620 4 HOH A 754   O    72.6 124.5  81.7                                  
REMARK 620 5 HOH A 914   O   123.8  81.7  94.9 153.0                            
REMARK 620 6 HOH A1086   O   107.8 153.2  63.4  82.0  72.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 602  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU A  25  OE12                                                    
REMARK 620 2 CGU A  25  OE21  83.6                                              
REMARK 620 3 CGU A  29  OE12  73.8 154.9                                        
REMARK 620 4 CGU A  29  OE21  83.3  91.3  75.7                                  
REMARK 620 5 HOH A 719   O    68.9  76.7 104.3 150.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 603  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU A  26  OE11                                                    
REMARK 620 2 CGU A  26  OE12  47.3                                              
REMARK 620 3 CGU A  29  OE22 102.2 124.9                                        
REMARK 620 4 HOH A 746   O   109.4  78.3  71.8                                  
REMARK 620 5 HOH A 958   O   117.4 146.3  84.9 131.1                            
REMARK 620 6 HOH A1104   O   138.8  96.0 116.4  72.3  81.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU A  29   O                                                      
REMARK 620 2 CGU A  32  OE12  85.9                                              
REMARK 620 3 CGU A  32  OE22  83.5  79.9                                        
REMARK 620 4 HOH A 712   O   149.0  82.2  66.2                                  
REMARK 620 5 HOH A 775   O    82.6 159.8  82.4  99.3                            
REMARK 620 6 HOH A 804   O    80.3  76.5 152.1 123.9 117.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4O03   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF CA2+ BOUND PROTHROMBIN DELETION MUTANT          
REMARK 900 RESIDUES 146-167                                                     
DBREF  5EDM A    1   565  UNP    P00734   THRB_HUMAN      44    622             
SEQADV 5EDM MET A  122  UNP  P00734    THR   165 CONFLICT                       
SEQADV 5EDM     A       UNP  P00734    PRO   197 DELETION                       
SEQADV 5EDM     A       UNP  P00734    ARG   198 DELETION                       
SEQADV 5EDM     A       UNP  P00734    SER   199 DELETION                       
SEQADV 5EDM     A       UNP  P00734    GLU   200 DELETION                       
SEQADV 5EDM     A       UNP  P00734    GLY   201 DELETION                       
SEQADV 5EDM     A       UNP  P00734    SER   202 DELETION                       
SEQADV 5EDM     A       UNP  P00734    SER   203 DELETION                       
SEQADV 5EDM     A       UNP  P00734    VAL   204 DELETION                       
SEQADV 5EDM     A       UNP  P00734    ASN   205 DELETION                       
SEQADV 5EDM     A       UNP  P00734    LEU   206 DELETION                       
SEQADV 5EDM     A       UNP  P00734    SER   207 DELETION                       
SEQADV 5EDM     A       UNP  P00734    PRO   208 DELETION                       
SEQADV 5EDM     A       UNP  P00734    PRO   209 DELETION                       
SEQADV 5EDM     A       UNP  P00734    LEU   210 DELETION                       
SEQADV 5EDM TYR A  566  UNP  P00734              EXPRESSION TAG                 
SEQADV 5EDM LEU A  567  UNP  P00734              EXPRESSION TAG                 
SEQADV 5EDM GLU A  568  UNP  P00734              EXPRESSION TAG                 
SEQRES   1 A  568  ALA ASN THR PHE LEU CGU CGU VAL ARG LYS GLY ASN LEU          
SEQRES   2 A  568  CGU ARG CGU CYS VAL CGU CGU THR CYS SER TYR CGU CGU          
SEQRES   3 A  568  ALA PHE CGU ALA LEU CGU SER SER THR ALA THR ASP VAL          
SEQRES   4 A  568  PHE TRP ALA LYS TYR THR ALA CYS GLU THR ALA ARG THR          
SEQRES   5 A  568  PRO ARG ASP LYS LEU ALA ALA CYS LEU GLU GLY ASN CYS          
SEQRES   6 A  568  ALA GLU GLY LEU GLY THR ASN TYR ARG GLY HIS VAL ASN          
SEQRES   7 A  568  ILE THR ARG SER GLY ILE GLU CYS GLN LEU TRP ARG SER          
SEQRES   8 A  568  ARG TYR PRO HIS LYS PRO GLU ILE ASN SER THR THR HIS          
SEQRES   9 A  568  PRO GLY ALA ASP LEU GLN GLU ASN PHE CYS ARG ASN PRO          
SEQRES  10 A  568  ASP SER SER THR MET GLY PRO TRP CYS TYR THR THR ASP          
SEQRES  11 A  568  PRO THR VAL ARG ARG GLN GLU CYS SER ILE PRO VAL CYS          
SEQRES  12 A  568  GLY GLN ASP GLN VAL THR VAL ALA MET THR GLU GLN CYS          
SEQRES  13 A  568  VAL PRO ASP ARG GLY GLN GLN TYR GLN GLY ARG LEU ALA          
SEQRES  14 A  568  VAL THR THR HIS GLY LEU PRO CYS LEU ALA TRP ALA SER          
SEQRES  15 A  568  ALA GLN ALA LYS ALA LEU SER LYS HIS GLN ASP PHE ASN          
SEQRES  16 A  568  SER ALA VAL GLN LEU VAL GLU ASN PHE CYS ARG ASN PRO          
SEQRES  17 A  568  ASP GLY ASP GLU GLU GLY VAL TRP CYS TYR VAL ALA GLY          
SEQRES  18 A  568  LYS PRO GLY ASP PHE GLY TYR CYS ASP LEU ASN TYR CYS          
SEQRES  19 A  568  GLU GLU ALA VAL GLU GLU GLU THR GLY ASP GLY LEU ASP          
SEQRES  20 A  568  GLU ASP SER ASP ARG ALA ILE GLU GLY ARG THR ALA THR          
SEQRES  21 A  568  SER GLU TYR GLN THR PHE PHE ASN PRO ARG THR PHE GLY          
SEQRES  22 A  568  SER GLY GLU ALA ASP CYS GLY LEU ARG PRO LEU PHE GLU          
SEQRES  23 A  568  LYS LYS SER LEU GLU ASP LYS THR GLU ARG GLU LEU LEU          
SEQRES  24 A  568  GLU SER TYR ILE ASP GLY ARG ILE VAL GLU GLY SER ASP          
SEQRES  25 A  568  ALA GLU ILE GLY MET SER PRO TRP GLN VAL MET LEU PHE          
SEQRES  26 A  568  ARG LYS SER PRO GLN GLU LEU LEU CYS GLY ALA SER LEU          
SEQRES  27 A  568  ILE SER ASP ARG TRP VAL LEU THR ALA ALA HIS CYS LEU          
SEQRES  28 A  568  LEU TYR PRO PRO TRP ASP LYS ASN PHE THR GLU ASN ASP          
SEQRES  29 A  568  LEU LEU VAL ARG ILE GLY LYS HIS SER ARG THR ARG TYR          
SEQRES  30 A  568  GLU ARG ASN ILE GLU LYS ILE SER MET LEU GLU LYS ILE          
SEQRES  31 A  568  TYR ILE HIS PRO ARG TYR ASN TRP ARG GLU ASN LEU ASP          
SEQRES  32 A  568  ARG ASP ILE ALA LEU MET LYS LEU LYS LYS PRO VAL ALA          
SEQRES  33 A  568  PHE SER ASP TYR ILE HIS PRO VAL CYS LEU PRO ASP ARG          
SEQRES  34 A  568  GLU THR ALA ALA SER LEU LEU GLN ALA GLY TYR LYS GLY          
SEQRES  35 A  568  ARG VAL THR GLY TRP GLY ASN LEU LYS GLU THR TRP THR          
SEQRES  36 A  568  ALA ASN VAL GLY LYS GLY GLN PRO SER VAL LEU GLN VAL          
SEQRES  37 A  568  VAL ASN LEU PRO ILE VAL GLU ARG PRO VAL CYS LYS ASP          
SEQRES  38 A  568  SER THR ARG ILE ARG ILE THR ASP ASN MET PHE CYS ALA          
SEQRES  39 A  568  GLY TYR LYS PRO ASP GLU GLY LYS ARG GLY ASP ALA CYS          
SEQRES  40 A  568  GLU GLY ASP SER GLY GLY PRO PHE VAL MET LYS SER PRO          
SEQRES  41 A  568  PHE ASN ASN ARG TRP TYR GLN MET GLY ILE VAL SER TRP          
SEQRES  42 A  568  GLY GLU GLY CYS ASP ARG ASP GLY LYS TYR GLY PHE TYR          
SEQRES  43 A  568  THR HIS VAL PHE ARG LEU LYS LYS TRP ILE GLN LYS VAL          
SEQRES  44 A  568  ILE ASP GLN PHE GLY GLU TYR LEU GLU                          
MODRES 5EDM CGU A    6  GLU  MODIFIED RESIDUE                                   
MODRES 5EDM CGU A    7  GLU  MODIFIED RESIDUE                                   
MODRES 5EDM CGU A   14  GLU  MODIFIED RESIDUE                                   
MODRES 5EDM CGU A   16  GLU  MODIFIED RESIDUE                                   
MODRES 5EDM CGU A   19  GLU  MODIFIED RESIDUE                                   
MODRES 5EDM CGU A   20  GLU  MODIFIED RESIDUE                                   
MODRES 5EDM CGU A   25  GLU  MODIFIED RESIDUE                                   
MODRES 5EDM CGU A   26  GLU  MODIFIED RESIDUE                                   
MODRES 5EDM CGU A   29  GLU  MODIFIED RESIDUE                                   
MODRES 5EDM CGU A   32  GLU  MODIFIED RESIDUE                                   
HET    CGU  A   6      12                                                       
HET    CGU  A   7      12                                                       
HET    CGU  A  14      12                                                       
HET    CGU  A  16      12                                                       
HET    CGU  A  19      12                                                       
HET    CGU  A  20      12                                                       
HET    CGU  A  25      12                                                       
HET    CGU  A  26      12                                                       
HET    CGU  A  29      12                                                       
HET    CGU  A  32      12                                                       
HET    NAG  B   1      14                                                       
HET    NAG  B   2      14                                                       
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET     MG  A 601       1                                                       
HET     MG  A 602       1                                                       
HET     MG  A 603       1                                                       
HET     MG  A 604       1                                                       
HET     MG  A 605       1                                                       
HET     MG  A 606       1                                                       
HET    NAG  A 607      14                                                       
HET    SO4  A 612       5                                                       
HET    SO4  A 613       5                                                       
HET    SO4  A 614       5                                                       
HET    SO4  A 615       5                                                       
HET    SO4  A 616       5                                                       
HET    SO4  A 617       5                                                       
HET    SO4  A 618       5                                                       
HET    SO4  A 619       5                                                       
HET    GOL  A 620       6                                                       
HET    SO4  A 621       5                                                       
HETNAM     CGU GAMMA-CARBOXY-GLUTAMIC ACID                                      
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  CGU    10(C6 H9 N O6)                                               
FORMUL   2  NAG    5(C8 H15 N O6)                                               
FORMUL   4   MG    6(MG 2+)                                                     
FORMUL  11  SO4    9(O4 S 2-)                                                   
FORMUL  19  GOL    C3 H8 O3                                                     
FORMUL  21  HOH   *464(H2 O)                                                    
HELIX    1 AA1 THR A    3  VAL A   18  1                                  16    
HELIX    2 AA2 SER A   23  CGU A   32  1                                  10    
HELIX    3 AA3 SER A   33  CYS A   47  1                                  15    
HELIX    4 AA4 PRO A   53  GLY A   63  1                                  11    
HELIX    5 AA5 PRO A  158  GLN A  162  5                                   5    
HELIX    6 AA6 SER A  182  LYS A  190  1                                   9    
HELIX    7 AA7 ALA A  237  GLU A  241  5                                   5    
HELIX    8 AA8 ASN A  268  GLY A  273  1                                   6    
HELIX    9 AA9 PHE A  285  SER A  289  5                                   5    
HELIX   10 AB1 THR A  294  LEU A  298  5                                   5    
HELIX   11 AB2 SER A  301  ARG A  306  5                                   6    
HELIX   12 AB3 ALA A  347  CYS A  350  5                                   4    
HELIX   13 AB4 PRO A  354  ASP A  357  5                                   4    
HELIX   14 AB5 THR A  361  ASN A  363  5                                   3    
HELIX   15 AB6 ASP A  428  ALA A  438  1                                  11    
HELIX   16 AB7 GLY A  448  THR A  455  1                                   8    
HELIX   17 AB8 GLU A  475  SER A  482  1                                   8    
HELIX   18 AB9 GLY A  534  ASP A  538  5                                   5    
HELIX   19 AC1 LEU A  552  LEU A  567  1                                  16    
SHEET    1 AA1 2 TRP A 125  TYR A 127  0                                        
SHEET    2 AA1 2 ARG A 135  GLU A 137 -1  O  GLN A 136   N  CYS A 126           
SHEET    1 AA2 2 TRP A 216  TYR A 218  0                                        
SHEET    2 AA2 2 PHE A 226  TYR A 228 -1  O  GLY A 227   N  CYS A 217           
SHEET    1 AA3 7 SER A 311  ASP A 312  0                                        
SHEET    2 AA3 7 GLN A 467  LEU A 471 -1  O  VAL A 468   N  SER A 311           
SHEET    3 AA3 7 GLY A 442  GLY A 446 -1  N  GLY A 442   O  LEU A 471           
SHEET    4 AA3 7 PRO A 514  LYS A 518 -1  O  VAL A 516   N  ARG A 443           
SHEET    5 AA3 7 TRP A 525  VAL A 531 -1  O  TYR A 526   N  MET A 517           
SHEET    6 AA3 7 GLY A 544  HIS A 548 -1  O  THR A 547   N  ILE A 530           
SHEET    7 AA3 7 MET A 491  ALA A 494 -1  N  PHE A 492   O  TYR A 546           
SHEET    1 AA4 7 LYS A 383  SER A 385  0                                        
SHEET    2 AA4 7 LEU A 365  ILE A 369 -1  N  ILE A 369   O  LYS A 383           
SHEET    3 AA4 7 GLN A 321  ARG A 326 -1  N  PHE A 325   O  LEU A 366           
SHEET    4 AA4 7 GLU A 331  LEU A 338 -1  O  CYS A 334   N  LEU A 324           
SHEET    5 AA4 7 TRP A 343  THR A 346 -1  O  LEU A 345   N  SER A 337           
SHEET    6 AA4 7 ALA A 407  LEU A 411 -1  O  MET A 409   N  VAL A 344           
SHEET    7 AA4 7 LEU A 387  ILE A 392 -1  N  GLU A 388   O  LYS A 410           
SHEET    1 AA5 2 LEU A 352  TYR A 353  0                                        
SHEET    2 AA5 2 LYS A 358  ASN A 359 -1  O  LYS A 358   N  TYR A 353           
SSBOND   1 CYS A   17    CYS A   22                          1555   1555  2.11  
SSBOND   2 CYS A   47    CYS A   60                          1555   1555  2.11  
SSBOND   3 CYS A   65    CYS A  143                          1555   1555  2.07  
SSBOND   4 CYS A   86    CYS A  126                          1555   1555  2.04  
SSBOND   5 CYS A  114    CYS A  138                          1555   1555  2.04  
SSBOND   6 CYS A  156    CYS A  234                          1555   1555  2.12  
SSBOND   7 CYS A  177    CYS A  217                          1555   1555  2.03  
SSBOND   8 CYS A  205    CYS A  229                          1555   1555  2.09  
SSBOND   9 CYS A  279    CYS A  425                          1555   1555  2.11  
SSBOND  10 CYS A  334    CYS A  350                          1555   1555  2.12  
SSBOND  11 CYS A  479    CYS A  493                          1555   1555  2.07  
SSBOND  12 CYS A  507    CYS A  537                          1555   1555  2.19  
LINK         C   LEU A   5                 N   CGU A   6     1555   1555  1.33  
LINK         C   CGU A   6                 N   CGU A   7     1555   1555  1.34  
LINK         C   CGU A   7                 N   VAL A   8     1555   1555  1.32  
LINK         C   LEU A  13                 N   CGU A  14     1555   1555  1.33  
LINK         C   CGU A  14                 N   ARG A  15     1555   1555  1.33  
LINK         C   ARG A  15                 N   CGU A  16     1555   1555  1.33  
LINK         C   CGU A  16                 N   CYS A  17     1555   1555  1.33  
LINK         C   VAL A  18                 N   CGU A  19     1555   1555  1.33  
LINK         C   CGU A  19                 N   CGU A  20     1555   1555  1.33  
LINK         C   CGU A  20                 N   THR A  21     1555   1555  1.32  
LINK         C   TYR A  24                 N   CGU A  25     1555   1555  1.34  
LINK         C   CGU A  25                 N   CGU A  26     1555   1555  1.33  
LINK         C   CGU A  26                 N   ALA A  27     1555   1555  1.33  
LINK         C   PHE A  28                 N   CGU A  29     1555   1555  1.33  
LINK         C   CGU A  29                 N   ALA A  30     1555   1555  1.33  
LINK         C   LEU A  31                 N   CGU A  32     1555   1555  1.33  
LINK         C   CGU A  32                 N   SER A  33     1555   1555  1.33  
LINK         ND2 ASN A  78                 C1  NAG A 607     1555   1555  1.40  
LINK         ND2 ASN A 100                 C1  NAG B   1     1555   1555  1.46  
LINK         ND2 ASN A 359                 C1  NAG C   1     1555   1555  1.45  
LINK         O4  NAG B   1                 C1  NAG B   2     1555   1555  1.39  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.45  
LINK        OE12 CGU A  14                MG    MG A 606     1555   1555  2.16  
LINK        OE22 CGU A  14                MG    MG A 606     1555   1555  2.18  
LINK        OE12 CGU A  16                MG    MG A 604     1555   1555  2.19  
LINK        OE22 CGU A  16                MG    MG A 604     1555   1555  2.15  
LINK        OE11 CGU A  19                MG    MG A 606     1555   1555  2.17  
LINK        OE21 CGU A  19                MG    MG A 606     1555   1555  2.16  
LINK        OE12 CGU A  20                MG    MG A 605     1555   1555  2.18  
LINK        OE22 CGU A  20                MG    MG A 605     1555   1555  2.18  
LINK        OE12 CGU A  25                MG    MG A 602     1555   1555  2.18  
LINK        OE21 CGU A  25                MG    MG A 602     1555   1555  2.18  
LINK        OE11 CGU A  26                MG    MG A 603     1555   1555  2.22  
LINK        OE12 CGU A  26                MG    MG A 603     1555   1555  2.94  
LINK        OE12 CGU A  26                MG    MG A 604     1555   1555  2.16  
LINK        OE21 CGU A  26                MG    MG A 604     1555   1555  2.18  
LINK         O   CGU A  29                MG    MG A 601     1555   1555  2.19  
LINK        OE12 CGU A  29                MG    MG A 602     1555   1555  2.18  
LINK        OE21 CGU A  29                MG    MG A 602     1555   1555  2.16  
LINK        OE22 CGU A  29                MG    MG A 603     1555   1555  2.19  
LINK        OE12 CGU A  32                MG    MG A 601     1555   1555  2.17  
LINK        OE22 CGU A  32                MG    MG A 601     1555   1555  2.19  
LINK        MG    MG A 601                 O   HOH A 712     1555   1555  2.15  
LINK        MG    MG A 601                 O   HOH A 775     1555   1555  2.14  
LINK        MG    MG A 601                 O   HOH A 804     1555   1555  2.14  
LINK        MG    MG A 602                 O   HOH A 719     1555   1555  2.15  
LINK        MG    MG A 603                 O   HOH A 746     1555   1555  2.17  
LINK        MG    MG A 603                 O   HOH A 958     1555   1555  2.15  
LINK        MG    MG A 603                 O   HOH A1104     1555   1555  2.15  
LINK        MG    MG A 604                 O   HOH A 710     1555   1555  2.16  
LINK        MG    MG A 604                 O   HOH A 744     1555   1555  2.16  
LINK        MG    MG A 605                 O   HOH A 701     1555   1555  2.16  
LINK        MG    MG A 605                 O   HOH A 754     1555   1555  2.18  
LINK        MG    MG A 605                 O   HOH A 914     1555   1555  2.16  
LINK        MG    MG A 605                 O   HOH A1086     1555   1555  2.14  
LINK        MG    MG A 606                 O   HOH A 770     1555   1555  2.15  
LINK        MG    MG A 606                 O   HOH A 982     1555   1555  2.14  
CISPEP   1 THR A   52    PRO A   53          0        -8.53                     
CISPEP   2 TYR A   93    PRO A   94          0         0.76                     
CISPEP   3 SER A  328    PRO A  329          0         1.09                     
CRYST1  109.884  168.690  144.315  90.00  90.00  90.00 C 2 2 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      0.009101  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005928  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006929        0.00000                         
ATOM      1  N   ALA A   1      -5.140  40.799  14.341  1.00107.03           N  
ANISOU    1  N   ALA A   1    16825  13470  10371   -828    471  -2262       N  
ATOM      2  CA  ALA A   1      -3.931  40.061  13.868  1.00109.66           C  
ANISOU    2  CA  ALA A   1    17282  13477  10907   -725    611  -2418       C  
ATOM      3  C   ALA A   1      -3.476  40.627  12.526  1.00109.55           C  
ANISOU    3  C   ALA A   1    17077  13816  10729   -735    616  -2556       C  
ATOM      4  O   ALA A   1      -3.970  41.670  12.088  1.00107.84           O  
ANISOU    4  O   ALA A   1    16695  14013  10263   -761    488  -2446       O  
ATOM      5  CB  ALA A   1      -4.212  38.559  13.761  1.00113.97           C  
ANISOU    5  CB  ALA A   1    18082  13666  11552   -964    833  -2689       C  
ATOM      6  N   ASN A   2      -2.543  39.933  11.874  1.00109.38           N  
ANISOU    6  N   ASN A   2    17097  13634  10827   -697    766  -2796       N  
ATOM      7  CA  ASN A   2      -1.941  40.418  10.637  1.00108.04           C  
ANISOU    7  CA  ASN A   2    16745  13812  10493   -736    790  -2944       C  
ATOM      8  C   ASN A   2      -1.478  41.885  10.767  1.00100.43           C  
ANISOU    8  C   ASN A   2    15666  13094   9399   -584    611  -2643       C  
ATOM      9  O   ASN A   2      -0.413  42.127  11.345  1.00 96.34           O  
ANISOU    9  O   ASN A   2    15148  12427   9027   -361    588  -2539       O  
ATOM     10  CB  ASN A   2      -2.888  40.204   9.439  1.00111.58           C  
ANISOU   10  CB  ASN A   2    17087  14648  10660  -1102    867  -3200       C  
ATOM     11  CG  ASN A   2      -2.950  38.752   8.984  1.00115.37           C  
ANISOU   11  CG  ASN A   2    17701  14886  11248  -1319   1123  -3616       C  
ATOM     12  OD1 ASN A   2      -2.467  37.848   9.669  1.00118.76           O  
ANISOU   12  OD1 ASN A   2    18376  14772  11974  -1163   1232  -3671       O  
ATOM     13  ND2 ASN A   2      -3.552  38.524   7.822  1.00116.09           N  
ANISOU   13  ND2 ASN A   2    17660  15375  11072  -1674   1225  -3912       N  
ATOM     14  N   THR A   3      -2.267  42.850  10.270  1.00 95.79           N  
ANISOU   14  N   THR A   3    15003  12878   8516   -695    493  -2506       N  
ATOM     15  CA  THR A   3      -1.785  44.251  10.199  1.00 92.69           C  
ANISOU   15  CA  THR A   3    14612  12645   7959   -595    368  -2244       C  
ATOM     16  C   THR A   3      -1.347  44.736  11.576  1.00 89.13           C  
ANISOU   16  C   THR A   3    14252  11909   7703   -374    284  -1992       C  
ATOM     17  O   THR A   3      -1.810  44.243  12.618  1.00 89.65           O  
ANISOU   17  O   THR A   3    14366  11741   7956   -285    259  -1929       O  
ATOM     18  CB  THR A   3      -2.732  45.280   9.466  1.00 92.36           C  
ANISOU   18  CB  THR A   3    14560  12989   7544   -653    235  -2080       C  
ATOM     19  OG1 THR A   3      -2.601  46.591  10.041  1.00 87.79           O  
ANISOU   19  OG1 THR A   3    14130  12330   6896   -476    101  -1744       O  
ATOM     20  CG2 THR A   3      -4.175  44.886   9.510  1.00 92.99           C  
ANISOU   20  CG2 THR A   3    14549  13262   7519   -705    185  -2131       C  
ATOM     21  N   PHE A   4      -0.393  45.658  11.561  1.00 86.14           N  
ANISOU   21  N   PHE A   4    13900  11580   7250   -345    265  -1875       N  
ATOM     22  CA  PHE A   4       0.184  46.193  12.793  1.00 81.50           C  
ANISOU   22  CA  PHE A   4    13368  10804   6794   -198    212  -1681       C  
ATOM     23  C   PHE A   4      -0.902  46.919  13.570  1.00 79.51           C  
ANISOU   23  C   PHE A   4    13232  10477   6500   -109     76  -1429       C  
ATOM     24  O   PHE A   4      -1.114  46.660  14.752  1.00 74.92           O  
ANISOU   24  O   PHE A   4    12656   9710   6101      7     35  -1343       O  
ATOM     25  CB  PHE A   4       1.329  47.144  12.453  1.00 80.00           C  
ANISOU   25  CB  PHE A   4    13192  10767   6436   -308    251  -1654       C  
ATOM     26  CG  PHE A   4       1.766  47.977  13.598  1.00 76.19           C  
ANISOU   26  CG  PHE A   4    12790  10172   5986   -252    204  -1459       C  
ATOM     27  CD1 PHE A   4       2.478  47.410  14.640  1.00 75.47           C  
ANISOU   27  CD1 PHE A   4    12561  10001   6112   -105    217  -1495       C  
ATOM     28  CD2 PHE A   4       1.449  49.328  13.650  1.00 74.68           C  
ANISOU   28  CD2 PHE A   4    12838   9950   5588   -331    151  -1239       C  
ATOM     29  CE1 PHE A   4       2.877  48.179  15.719  1.00 73.32           C  
ANISOU   29  CE1 PHE A   4    12325   9698   5832    -98    182  -1342       C  
ATOM     30  CE2 PHE A   4       1.840  50.103  14.726  1.00 73.50           C  
ANISOU   30  CE2 PHE A   4    12785   9684   5458   -330    140  -1106       C  
ATOM     31  CZ  PHE A   4       2.557  49.528  15.762  1.00 72.45           C  
ANISOU   31  CZ  PHE A   4    12450   9551   5524   -244    158  -1171       C  
ATOM     32  N   LEU A   5      -1.594  47.812  12.865  1.00 81.25           N  
ANISOU   32  N   LEU A   5    13545  10872   6453   -139      4  -1318       N  
ATOM     33  CA  LEU A   5      -2.758  48.508  13.396  1.00 82.83           C  
ANISOU   33  CA  LEU A   5    13827  11077   6566     18   -129  -1124       C  
ATOM     34  C   LEU A   5      -3.733  47.539  14.045  1.00 82.37           C  
ANISOU   34  C   LEU A   5    13624  11023   6650     47   -150  -1216       C  
ATOM     35  O   LEU A   5      -4.187  47.780  15.164  1.00 83.55           O  
ANISOU   35  O   LEU A   5    13790  11068   6885    163   -216  -1102       O  
ATOM     36  CB  LEU A   5      -3.460  49.347  12.307  1.00 86.73           C  
ANISOU   36  CB  LEU A   5    14416  11823   6713     58   -213  -1020       C  
ATOM     37  CG  LEU A   5      -3.384  50.900  12.360  1.00 89.85           C  
ANISOU   37  CG  LEU A   5    15135  12094   6911    195   -284   -741       C  
ATOM     38  CD1 LEU A   5      -2.371  51.468  13.367  1.00 87.46           C  
ANISOU   38  CD1 LEU A   5    14998  11468   6762    142   -215   -665       C  
ATOM     39  CD2 LEU A   5      -3.160  51.496  10.957  1.00 93.98           C  
ANISOU   39  CD2 LEU A   5    15827  12788   7093     91   -279   -664       C  
HETATM   40  N   CGU A   6      -4.035  46.438  13.373  1.00 82.05           N  
ANISOU   40  N   CGU A   6    13458  11103   6613   -111    -71  -1446       N  
HETATM   41  CA  CGU A   6      -4.942  45.448  13.951  1.00 82.19           C  
ANISOU   41  CA  CGU A   6    13395  11108   6723   -197    -46  -1563       C  
HETATM   42  C   CGU A   6      -4.354  44.810  15.200  1.00 78.91           C  
ANISOU   42  C   CGU A   6    13065  10305   6612   -156      2  -1519       C  
HETATM   43  O   CGU A   6      -5.094  44.561  16.142  1.00 78.65           O  
ANISOU   43  O   CGU A   6    13032  10229   6621   -175    -31  -1469       O  
HETATM   44  CB  CGU A   6      -5.379  44.403  12.907  1.00 86.35           C  
ANISOU   44  CB  CGU A   6    13823  11829   7154   -454     70  -1861       C  
HETATM   45  CG  CGU A   6      -6.448  44.932  11.919  1.00 89.86           C  
ANISOU   45  CG  CGU A   6    14107  12814   7222   -497    -17  -1894       C  
HETATM   46  CD1 CGU A   6      -6.714  43.990  10.756  1.00 92.04           C  
ANISOU   46  CD1 CGU A   6    14260  13357   7354   -809    117  -2222       C  
HETATM   47  CD2 CGU A   6      -7.757  45.222  12.626  1.00 91.69           C  
ANISOU   47  CD2 CGU A   6    14217  13302   7319   -420   -135  -1828       C  
HETATM   48 OE11 CGU A   6      -7.463  44.406   9.849  1.00 93.32           O  
ANISOU   48 OE11 CGU A   6    14255  14039   7164   -843     41  -2253       O  
HETATM   49 OE12 CGU A   6      -6.199  42.847  10.708  1.00 92.63           O  
ANISOU   49 OE12 CGU A   6    14412  13145   7636  -1005    303  -2460       O  
HETATM   50 OE21 CGU A   6      -8.074  46.417  12.862  1.00 92.85           O  
ANISOU   50 OE21 CGU A   6    14375  13571   7333   -120   -298  -1595       O  
HETATM   51 OE22 CGU A   6      -8.497  44.260  12.952  1.00 92.33           O  
ANISOU   51 OE22 CGU A   6    14205  13472   7403   -670    -52  -2030       O  
HETATM   52  N   CGU A   7      -3.042  44.548  15.233  1.00 76.75           N  
ANISOU   52  N   CGU A   7    12842   9808   6508    -90     73  -1538       N  
HETATM   53  CA  CGU A   7      -2.389  43.916  16.399  1.00 75.19           C  
ANISOU   53  CA  CGU A   7    12715   9290   6564     24     98  -1468       C  
HETATM   54  C   CGU A   7      -2.453  44.847  17.606  1.00 72.53           C  
ANISOU   54  C   CGU A   7    12384   8944   6228    139    -20  -1218       C  
HETATM   55  O   CGU A   7      -2.523  44.411  18.748  1.00 70.55           O  
ANISOU   55  O   CGU A   7    12177   8524   6104    183    -39  -1118       O  
HETATM   56  CB  CGU A   7      -0.942  43.524  16.036  1.00 76.98           C  
ANISOU   56  CB  CGU A   7    12915   9424   6910    138    185  -1577       C  
HETATM   57  CG  CGU A   7      -0.169  42.641  17.051  1.00 78.78           C  
ANISOU   57  CG  CGU A   7    13204   9353   7373    352    209  -1529       C  
HETATM   58  CD1 CGU A   7      -0.768  41.258  17.183  1.00 82.43           C  
ANISOU   58  CD1 CGU A   7    13864   9486   7967    301    305  -1628       C  
HETATM   59  CD2 CGU A   7       1.300  42.479  16.682  1.00 79.50           C  
ANISOU   59  CD2 CGU A   7    13174   9511   7520    542    268  -1655       C  
HETATM   60 OE11 CGU A   7      -1.534  40.838  16.279  1.00 84.75           O  
ANISOU   60 OE11 CGU A   7    14197   9824   8180     63    396  -1834       O  
HETATM   61 OE12 CGU A   7      -0.457  40.566  18.185  1.00 82.26           O  
ANISOU   61 OE12 CGU A   7    13987   9165   8103    476    300  -1503       O  
HETATM   62 OE21 CGU A   7       1.744  43.006  15.628  1.00 79.62           O  
ANISOU   62 OE21 CGU A   7    13065   9794   7391    436    312  -1803       O  
HETATM   63 OE22 CGU A   7       2.042  41.799  17.438  1.00 79.10           O  
ANISOU   63 OE22 CGU A   7    13139   9289   7626    813    268  -1612       O  
ATOM     64  N   VAL A   8      -2.455  46.146  17.358  1.00 70.78           N  
ANISOU   64  N   VAL A   8    12157   8891   5842    172    -89  -1118       N  
ATOM     65  CA  VAL A   8      -2.565  47.107  18.420  1.00 69.07           C  
ANISOU   65  CA  VAL A   8    11981   8653   5609    259   -172   -931       C  
ATOM     66  C   VAL A   8      -3.967  47.099  18.960  1.00 69.26           C  
ANISOU   66  C   VAL A   8    11973   8764   5577    264   -244   -902       C  
ATOM     67  O   VAL A   8      -4.169  47.183  20.167  1.00 67.57           O  
ANISOU   67  O   VAL A   8    11750   8491   5429    294   -282   -809       O  
ATOM     68  CB  VAL A   8      -2.260  48.522  17.920  1.00 69.56           C  
ANISOU   68  CB  VAL A   8    12151   8792   5486    278   -195   -847       C  
ATOM     69  CG1 VAL A   8      -2.650  49.565  18.965  1.00 69.31           C  
ANISOU   69  CG1 VAL A   8    12213   8704   5416    371   -262   -697       C  
ATOM     70  CG2 VAL A   8      -0.785  48.642  17.592  1.00 70.06           C  
ANISOU   70  CG2 VAL A   8    12213   8851   5557    193   -107   -897       C  
ATOM     71  N   ARG A   9      -4.937  47.039  18.060  1.00 70.32           N  
ANISOU   71  N   ARG A   9    12049   9121   5546    223   -263  -1001       N  
ATOM     72  CA  ARG A   9      -6.333  47.068  18.465  1.00 71.77           C  
ANISOU   72  CA  ARG A   9    12123   9538   5606    225   -332  -1028       C  
ATOM     73  C   ARG A   9      -6.696  45.794  19.238  1.00 71.14           C  
ANISOU   73  C   ARG A   9    12012   9370   5647     12   -263  -1114       C  
ATOM     74  O   ARG A   9      -7.548  45.812  20.142  1.00 69.99           O  
ANISOU   74  O   ARG A   9    11789   9357   5447    -31   -303  -1102       O  
ATOM     75  CB  ARG A   9      -7.231  47.272  17.249  1.00 75.23           C  
ANISOU   75  CB  ARG A   9    12451  10351   5778    238   -375  -1132       C  
ATOM     76  CG  ARG A   9      -7.030  48.624  16.552  1.00 76.98           C  
ANISOU   76  CG  ARG A   9    12792  10631   5826    481   -460   -983       C  
ATOM     77  CD  ARG A   9      -8.123  48.871  15.532  1.00 80.61           C  
ANISOU   77  CD  ARG A   9    13112  11548   5965    581   -548  -1040       C  
ATOM     78  NE  ARG A   9      -7.908  50.044  14.673  1.00 83.53           N  
ANISOU   78  NE  ARG A   9    13674  11936   6125    812   -625   -863       N  
ATOM     79  CZ  ARG A   9      -7.442  50.009  13.415  1.00 84.70           C  
ANISOU   79  CZ  ARG A   9    13880  12170   6130    704   -593   -871       C  
ATOM     80  NH1 ARG A   9      -7.087  48.866  12.825  1.00 85.44           N  
ANISOU   80  NH1 ARG A   9    13830  12338   6293    387   -474  -1088       N  
ATOM     81  NH2 ARG A   9      -7.312  51.139  12.731  1.00 86.23           N  
ANISOU   81  NH2 ARG A   9    14316  12353   6092    904   -666   -663       N  
ATOM     82  N   LYS A  10      -6.019  44.705  18.901  1.00 70.38           N  
ANISOU   82  N   LYS A  10    12008   9032   5698   -118   -147  -1202       N  
ATOM     83  CA  LYS A  10      -6.171  43.455  19.625  1.00 72.15           C  
ANISOU   83  CA  LYS A  10    12343   9025   6045   -306    -57  -1240       C  
ATOM     84  C   LYS A  10      -5.716  43.599  21.082  1.00 69.13           C  
ANISOU   84  C   LYS A  10    12028   8445   5793   -197   -112  -1019       C  
ATOM     85  O   LYS A  10      -6.392  43.125  21.983  1.00 68.86           O  
ANISOU   85  O   LYS A  10    12032   8400   5730   -362   -103   -987       O  
ATOM     86  CB  LYS A  10      -5.386  42.329  18.927  1.00 76.38           C  
ANISOU   86  CB  LYS A  10    13034   9256   6729   -364     85  -1376       C  
ATOM     87  CG  LYS A  10      -5.187  41.056  19.757  1.00 80.66           C  
ANISOU   87  CG  LYS A  10    13833   9373   7439   -449    183  -1342       C  
ATOM     88  CD  LYS A  10      -4.111  40.126  19.194  1.00 84.41           C  
ANISOU   88  CD  LYS A  10    14491   9477   8103   -320    306  -1444       C  
ATOM     89  CE  LYS A  10      -4.682  39.101  18.232  1.00 89.01           C  
ANISOU   89  CE  LYS A  10    15213   9970   8636   -626    491  -1750       C  
ATOM     90  NZ  LYS A  10      -3.624  38.314  17.519  1.00 92.50           N  
ANISOU   90  NZ  LYS A  10    15806  10085   9254   -451    623  -1914       N  
ATOM     91  N   GLY A  11      -4.566  44.228  21.303  1.00 66.16           N  
ANISOU   91  N   GLY A  11    11654   7966   5516     28   -157   -886       N  
ATOM     92  CA  GLY A  11      -4.057  44.437  22.657  1.00 64.89           C  
ANISOU   92  CA  GLY A  11    11508   7711   5432    121   -211   -692       C  
ATOM     93  C   GLY A  11      -4.930  45.354  23.502  1.00 63.02           C  
ANISOU   93  C   GLY A  11    11173   7701   5069     90   -294   -630       C  
ATOM     94  O   GLY A  11      -5.041  45.175  24.723  1.00 62.41           O  
ANISOU   94  O   GLY A  11    11102   7605   5006     37   -319   -517       O  
ATOM     95  N   ASN A  12      -5.533  46.337  22.844  1.00 62.04           N  
ANISOU   95  N   ASN A  12    10968   7800   4804    152   -336   -704       N  
ATOM     96  CA  ASN A  12      -6.437  47.267  23.483  1.00 62.76           C  
ANISOU   96  CA  ASN A  12    10964   8118   4761    209   -409   -696       C  
ATOM     97  C   ASN A  12      -7.719  46.627  23.908  1.00 65.25           C  
ANISOU   97  C   ASN A  12    11161   8664   4966     23   -408   -799       C  
ATOM     98  O   ASN A  12      -8.235  46.926  24.978  1.00 63.71           O  
ANISOU   98  O   ASN A  12    10880   8613   4712     -6   -442   -780       O  
ATOM     99  CB  ASN A  12      -6.766  48.425  22.549  1.00 63.08           C  
ANISOU   99  CB  ASN A  12    11008   8304   4655    409   -460   -732       C  
ATOM    100  CG  ASN A  12      -5.614  49.395  22.408  1.00 62.72           C  
ANISOU  100  CG  ASN A  12    11124   8054   4649    521   -445   -628       C  
ATOM    101  OD1 ASN A  12      -4.689  49.407  23.221  1.00 63.04           O  
ANISOU  101  OD1 ASN A  12    11196   7954   4800    465   -412   -555       O  
ATOM    102  ND2 ASN A  12      -5.657  50.203  21.374  1.00 63.32           N  
ANISOU  102  ND2 ASN A  12    11309   8152   4594    648   -462   -623       N  
ATOM    103  N   LEU A  13      -8.252  45.770  23.044  1.00 48.93           N  
ANISOU  103  N   LEU A  13     8244   6063   4284  -2044     59  -1468       N  
ATOM    104  CA  LEU A  13      -9.411  44.961  23.389  1.00 49.19           C  
ANISOU  104  CA  LEU A  13     8288   6027   4373  -1859    -40  -1328       C  
ATOM    105  C   LEU A  13      -9.132  44.114  24.621  1.00 49.74           C  
ANISOU  105  C   LEU A  13     8220   6198   4479  -1781   -170  -1315       C  
ATOM    106  O   LEU A  13      -9.957  44.041  25.519  1.00 50.56           O  
ANISOU  106  O   LEU A  13     8389   6274   4547  -1746   -213  -1234       O  
ATOM    107  CB  LEU A  13      -9.780  44.051  22.239  1.00 50.33           C  
ANISOU  107  CB  LEU A  13     8419   6130   4573  -1783    -53  -1287       C  
ATOM    108  CG  LEU A  13     -10.848  44.476  21.256  1.00 50.14           C  
ANISOU  108  CG  LEU A  13     8595   5935   4520  -1784    -30  -1192       C  
ATOM    109  CD1 LEU A  13     -11.222  43.239  20.458  1.00 49.47           C  
ANISOU  109  CD1 LEU A  13     8450   5850   4497  -1680    -67  -1146       C  
ATOM    110  CD2 LEU A  13     -12.080  44.984  21.963  1.00 50.35           C  
ANISOU  110  CD2 LEU A  13     8718   5835   4576  -1691    -77  -1114       C  
HETATM  111  N   CGU A  14      -7.954  43.502  24.660  1.00 51.42           N  
ANISOU  111  N   CGU A  14     8250   6519   4769  -1783   -246  -1420       N  
HETATM  112  CA  CGU A  14      -7.528  42.743  25.812  1.00 55.46           C  
ANISOU  112  CA  CGU A  14     8661   7086   5323  -1731   -451  -1400       C  
HETATM  113  C   CGU A  14      -7.554  43.605  27.050  1.00 57.93           C  
ANISOU  113  C   CGU A  14     9073   7434   5503  -1846   -445  -1377       C  
HETATM  114  O   CGU A  14      -8.163  43.216  28.043  1.00 58.58           O  
ANISOU  114  O   CGU A  14     9243   7504   5510  -1851   -549  -1267       O  
HETATM  115  CB  CGU A  14      -6.143  42.122  25.592  1.00 58.14           C  
ANISOU  115  CB  CGU A  14     8748   7506   5833  -1706   -567  -1578       C  
HETATM  116  CG  CGU A  14      -5.622  41.444  26.861  1.00 62.23           C  
ANISOU  116  CG  CGU A  14     9196   8036   6410  -1661   -866  -1546       C  
HETATM  117  CD1 CGU A  14      -6.363  40.195  27.207  1.00 61.76           C  
ANISOU  117  CD1 CGU A  14     9207   7879   6378  -1540  -1086  -1370       C  
HETATM  118  CD2 CGU A  14      -4.198  41.042  26.720  1.00 66.56           C  
ANISOU  118  CD2 CGU A  14     9458   8644   7186  -1628  -1010  -1778       C  
HETATM  119 OE11 CGU A  14      -7.293  39.805  26.485  1.00 58.49           O  
ANISOU  119 OE11 CGU A  14     8861   7405   5955  -1468   -989  -1287       O  
HETATM  120 OE12 CGU A  14      -6.013  39.563  28.220  1.00 66.30           O  
ANISOU  120 OE12 CGU A  14     9790   8423   6975  -1533  -1385  -1305       O  
HETATM  121 OE21 CGU A  14      -3.713  41.041  25.580  1.00 68.40           O  
ANISOU  121 OE21 CGU A  14     9523   8924   7539  -1635   -852  -1980       O  
HETATM  122 OE22 CGU A  14      -3.553  40.709  27.748  1.00 71.62           O  
ANISOU  122 OE22 CGU A  14    10035   9281   7895  -1612  -1295  -1782       O  
ATOM    123  N   ARG A  15      -6.909  44.772  27.008  1.00 60.79           N  
ANISOU  123  N   ARG A  15     9437   7843   5815  -1976   -311  -1493       N  
ATOM    124  CA  ARG A  15      -6.848  45.665  28.179  1.00 62.65           C  
ANISOU  124  CA  ARG A  15     9753   8119   5929  -2104   -288  -1500       C  
ATOM    125  C   ARG A  15      -8.209  46.163  28.663  1.00 59.76           C  
ANISOU  125  C   ARG A  15     9561   7672   5471  -2125   -196  -1418       C  
ATOM    126  O   ARG A  15      -8.506  46.104  29.864  1.00 62.15           O  
ANISOU  126  O   ARG A  15     9919   8019   5675  -2206   -245  -1389       O  
ATOM    127  CB  ARG A  15      -5.999  46.902  27.893  1.00 68.90           C  
ANISOU  127  CB  ARG A  15    10534   8956   6686  -2247   -137  -1645       C  
ATOM    128  CG  ARG A  15      -4.498  46.688  27.890  1.00 78.63           C  
ANISOU  128  CG  ARG A  15    11556  10317   8000  -2294   -207  -1812       C  
ATOM    129  CD  ARG A  15      -3.915  46.527  29.300  1.00 87.26           C  
ANISOU  129  CD  ARG A  15    12592  11492   9070  -2331   -399  -1813       C  
ATOM    130  NE  ARG A  15      -2.587  45.894  29.277  1.00 95.78           N  
ANISOU  130  NE  ARG A  15    13411  12655  10324  -2295   -577  -1977       N  
ATOM    131  CZ  ARG A  15      -2.352  44.610  28.970  1.00 95.36           C  
ANISOU  131  CZ  ARG A  15    13195  12570  10466  -2135   -789  -1995       C  
ATOM    132  NH1 ARG A  15      -3.334  43.769  28.648  1.00 90.42           N  
ANISOU  132  NH1 ARG A  15    12659  11844   9851  -2008   -839  -1832       N  
ATOM    133  NH2 ARG A  15      -1.111  44.169  28.973  1.00 97.94           N  
ANISOU  133  NH2 ARG A  15    13245  12957  11008  -2099   -960  -2209       N  
HETATM  134  N   CGU A  16      -9.018  46.658  27.730  1.00 55.00           N  
ANISOU  134  N   CGU A  16     9042   6947   4907  -2078    -73  -1408       N  
HETATM  135  CA  CGU A  16     -10.221  47.421  28.051  1.00 52.58           C  
ANISOU  135  CA  CGU A  16     8851   6534   4590  -2092     20  -1417       C  
HETATM  136  C   CGU A  16     -11.471  46.603  28.083  1.00 51.80           C  
ANISOU  136  C   CGU A  16     8767   6382   4532  -1987    -10  -1349       C  
HETATM  137  O   CGU A  16     -12.448  46.981  28.737  1.00 51.73           O  
ANISOU  137  O   CGU A  16     8794   6336   4523  -2024     59  -1413       O  
HETATM  138  CB  CGU A  16     -10.420  48.505  26.987  1.00 53.27           C  
ANISOU  138  CB  CGU A  16     9041   6465   4734  -2098    101  -1452       C  
HETATM  139  CG  CGU A  16      -9.176  49.405  26.773  1.00 56.03           C  
ANISOU  139  CG  CGU A  16     9409   6860   5017  -2251    161  -1533       C  
HETATM  140  CD1 CGU A  16      -9.324  50.484  25.719  1.00 56.94           C  
ANISOU  140  CD1 CGU A  16     9700   6792   5140  -2322    205  -1541       C  
HETATM  141  CD2 CGU A  16      -8.685  50.053  28.042  1.00 55.88           C  
ANISOU  141  CD2 CGU A  16     9362   6942   4926  -2372    201  -1620       C  
HETATM  142 OE11 CGU A  16      -8.329  50.678  24.994  1.00 62.09           O  
ANISOU  142 OE11 CGU A  16    10375   7495   5720  -2455    251  -1580       O  
HETATM  143 OE12 CGU A  16     -10.367  51.159  25.593  1.00 58.57           O  
ANISOU  143 OE12 CGU A  16    10028   6797   5427  -2272    178  -1530       O  
HETATM  144 OE21 CGU A  16      -7.504  49.811  28.343  1.00 56.84           O  
ANISOU  144 OE21 CGU A  16     9380   7217   4997  -2444    173  -1665       O  
HETATM  145 OE22 CGU A  16      -9.421  50.784  28.718  1.00 55.41           O  
ANISOU  145 OE22 CGU A  16     9362   6812   4876  -2401    253  -1672       O  
ATOM    146  N   CYS A  17     -11.477  45.484  27.357  1.00 50.72           N  
ANISOU  146  N   CYS A  17     8586   6240   4443  -1870    -98  -1256       N  
ATOM    147  CA  CYS A  17     -12.691  44.709  27.180  1.00 49.72           C  
ANISOU  147  CA  CYS A  17     8479   6051   4361  -1768   -117  -1193       C  
ATOM    148  C   CYS A  17     -12.642  43.322  27.761  1.00 48.61           C  
ANISOU  148  C   CYS A  17     8310   5992   4166  -1757   -250  -1101       C  
ATOM    149  O   CYS A  17     -13.668  42.780  28.137  1.00 47.99           O  
ANISOU  149  O   CYS A  17     8273   5899   4058  -1761   -243  -1074       O  
ATOM    150  CB  CYS A  17     -13.045  44.626  25.694  1.00 50.65           C  
ANISOU  150  CB  CYS A  17     8616   6045   4582  -1647   -114  -1151       C  
ATOM    151  SG  CYS A  17     -13.738  46.170  25.070  1.00 53.19           S  
ANISOU  151  SG  CYS A  17     9057   6167   4983  -1657    -46  -1221       S  
ATOM    152  N   VAL A  18     -11.460  42.742  27.855  1.00 49.87           N  
ANISOU  152  N   VAL A  18     8399   6221   4326  -1756   -389  -1072       N  
ATOM    153  CA  VAL A  18     -11.341  41.384  28.361  1.00 51.34           C  
ANISOU  153  CA  VAL A  18     8583   6430   4494  -1735   -596   -971       C  
ATOM    154  C   VAL A  18     -10.920  41.395  29.827  1.00 52.28           C  
ANISOU  154  C   VAL A  18     8779   6623   4460  -1914   -719   -951       C  
ATOM    155  O   VAL A  18     -11.612  40.838  30.672  1.00 53.71           O  
ANISOU  155  O   VAL A  18     9095   6811   4502  -2031   -779   -875       O  
ATOM    156  CB  VAL A  18     -10.367  40.574  27.479  1.00 52.65           C  
ANISOU  156  CB  VAL A  18     8597   6584   4824  -1596   -733   -982       C  
ATOM    157  CG1 VAL A  18     -10.311  39.118  27.906  1.00 54.06           C  
ANISOU  157  CG1 VAL A  18     8779   6725   5036  -1541  -1003   -876       C  
ATOM    158  CG2 VAL A  18     -10.800  40.667  26.016  1.00 51.27           C  
ANISOU  158  CG2 VAL A  18     8386   6350   4744  -1489   -583  -1009       C  
HETATM  159  N   CGU A  19      -9.804  42.049  30.126  1.00 53.13           N  
ANISOU  159  N   CGU A  19     8823   6792   4572  -1972   -750  -1027       N  
HETATM  160  CA  CGU A  19      -9.329  42.184  31.508  1.00 55.06           C  
ANISOU  160  CA  CGU A  19     9154   7106   4657  -2166   -880  -1010       C  
HETATM  161  C   CGU A  19     -10.212  43.118  32.303  1.00 55.05           C  
ANISOU  161  C   CGU A  19     9283   7153   4478  -2362   -658  -1068       C  
HETATM  162  O   CGU A  19     -10.131  43.174  33.539  1.00 57.26           O  
ANISOU  162  O   CGU A  19     9689   7502   4565  -2591   -725  -1054       O  
HETATM  163  CB  CGU A  19      -7.909  42.746  31.515  1.00 57.08           C  
ANISOU  163  CB  CGU A  19     9273   7420   4992  -2168   -947  -1114       C  
HETATM  164  CG  CGU A  19      -6.856  41.824  30.881  1.00 59.72           C  
ANISOU  164  CG  CGU A  19     9415   7723   5552  -1999  -1185  -1146       C  
HETATM  165  CD1 CGU A  19      -5.609  42.595  30.547  1.00 61.19           C  
ANISOU  165  CD1 CGU A  19     9414   7987   5849  -2005  -1128  -1335       C  
HETATM  166  CD2 CGU A  19      -6.462  40.688  31.786  1.00 62.63           C  
ANISOU  166  CD2 CGU A  19     9835   8037   5921  -2017  -1588  -1032       C  
HETATM  167 OE11 CGU A  19      -4.801  42.044  29.775  1.00 64.29           O  
ANISOU  167 OE11 CGU A  19     9590   8372   6463  -1877  -1220  -1455       O  
HETATM  168 OE12 CGU A  19      -5.401  43.729  31.068  1.00 60.93           O  
ANISOU  168 OE12 CGU A  19     9433   8026   5689  -2156   -986  -1395       O  
HETATM  169 OE21 CGU A  19      -5.560  39.930  31.410  1.00 68.96           O  
ANISOU  169 OE21 CGU A  19    10452   8787   6961  -1868  -1837  -1096       O  
HETATM  170 OE22 CGU A  19      -7.016  40.499  32.889  1.00 65.51           O  
ANISOU  170 OE22 CGU A  19    10433   8397   6061  -2199  -1690   -894       O  
HETATM  171  N   CGU A  20     -11.020  43.903  31.594  1.00 52.85           N  
ANISOU  171  N   CGU A  20     8974   6827   4278  -2291   -408  -1159       N  
HETATM  172  CA  CGU A  20     -11.934  44.856  32.202  1.00 52.77           C  
ANISOU  172  CA  CGU A  20     9024   6831   4192  -2436   -189  -1288       C  
HETATM  173  C   CGU A  20     -13.181  44.788  31.420  1.00 49.95           C  
ANISOU  173  C   CGU A  20     8643   6374   3960  -2305    -68  -1324       C  
HETATM  174  O   CGU A  20     -13.168  44.336  30.292  1.00 49.37           O  
ANISOU  174  O   CGU A  20     8520   6220   4017  -2110   -125  -1246       O  
HETATM  175  CB  CGU A  20     -11.401  46.284  32.086  1.00 54.32           C  
ANISOU  175  CB  CGU A  20     9176   7023   4439  -2460    -54  -1419       C  
HETATM  176  CG  CGU A  20     -10.128  46.456  32.922  1.00 59.68           C  
ANISOU  176  CG  CGU A  20     9861   7816   4998  -2604   -165  -1413       C  
HETATM  177  CD1 CGU A  20      -9.398  47.758  32.694  1.00 59.87           C  
ANISOU  177  CD1 CGU A  20     9836   7842   5069  -2628    -50  -1530       C  
HETATM  178  CD2 CGU A  20     -10.439  46.336  34.383  1.00 63.39           C  
ANISOU  178  CD2 CGU A  20    10455   8386   5244  -2872   -175  -1428       C  
HETATM  179 OE11 CGU A  20      -9.897  48.632  31.966  1.00 57.46           O  
ANISOU  179 OE11 CGU A  20     9529   7428   4874  -2557    103  -1610       O  
HETATM  180 OE12 CGU A  20      -8.301  47.926  33.260  1.00 66.27           O  
ANISOU  180 OE12 CGU A  20    10623   8747   5807  -2730   -139  -1544       O  
HETATM  181 OE21 CGU A  20     -11.641  46.357  34.776  1.00 63.54           O  
ANISOU  181 OE21 CGU A  20    10532   8405   5203  -2977    -23  -1506       O  
HETATM  182 OE22 CGU A  20      -9.457  46.214  35.140  1.00 72.26           O  
ANISOU  182 OE22 CGU A  20    11615   9589   6248  -3001   -342  -1382       O  
ATOM    183  N   THR A  21     -14.277  45.231  32.007  1.00 48.81           N  
ANISOU  183  N   THR A  21     8519   6235   3790  -2423     98  -1473       N  
ATOM    184  CA  THR A  21     -15.514  45.412  31.286  1.00 47.67           C  
ANISOU  184  CA  THR A  21     8312   5973   3827  -2288    208  -1572       C  
ATOM    185  C   THR A  21     -15.402  46.685  30.465  1.00 48.53           C  
ANISOU  185  C   THR A  21     8371   5937   4128  -2153    256  -1659       C  
ATOM    186  O   THR A  21     -14.674  47.587  30.852  1.00 46.30           O  
ANISOU  186  O   THR A  21     8103   5679   3807  -2243    293  -1717       O  
ATOM    187  CB  THR A  21     -16.666  45.558  32.262  1.00 49.39           C  
ANISOU  187  CB  THR A  21     8520   6251   3992  -2486    383  -1788       C  
ATOM    188  OG1 THR A  21     -16.668  44.418  33.114  1.00 50.82           O  
ANISOU  188  OG1 THR A  21     8820   6566   3920  -2697    323  -1687       O  
ATOM    189  CG2 THR A  21     -17.999  45.644  31.549  1.00 49.76           C  
ANISOU  189  CG2 THR A  21     8459   6172   4275  -2331    466  -1933       C  
ATOM    190  N   CYS A  22     -16.088  46.723  29.318  1.00 48.08           N  
ANISOU  190  N   CYS A  22     8286   5716   4262  -1956    227  -1648       N  
ATOM    191  CA  CYS A  22     -16.085  47.874  28.451  1.00 48.59           C  
ANISOU  191  CA  CYS A  22     8371   5592   4500  -1853    208  -1697       C  
ATOM    192  C   CYS A  22     -17.483  48.140  27.933  1.00 48.15           C  
ANISOU  192  C   CYS A  22     8263   5346   4686  -1717    196  -1824       C  
ATOM    193  O   CYS A  22     -18.336  47.255  27.974  1.00 48.26           O  
ANISOU  193  O   CYS A  22     8214   5396   4725  -1675    211  -1840       O  
ATOM    194  CB  CYS A  22     -15.136  47.652  27.283  1.00 48.72           C  
ANISOU  194  CB  CYS A  22     8455   5571   4484  -1775    102  -1509       C  
ATOM    195  SG  CYS A  22     -15.575  46.332  26.098  1.00 50.16           S  
ANISOU  195  SG  CYS A  22     8634   5712   4710  -1609      1  -1346       S  
ATOM    196  N   SER A  23     -17.712  49.363  27.452  1.00 47.61           N  
ANISOU  196  N   SER A  23     8223   5057   4808  -1653    142  -1923       N  
ATOM    197  CA  SER A  23     -18.974  49.721  26.802  1.00 49.14           C  
ANISOU  197  CA  SER A  23     8370   5002   5299  -1487     41  -2046       C  
ATOM    198  C   SER A  23     -18.816  49.511  25.305  1.00 48.60           C  
ANISOU  198  C   SER A  23     8449   4767   5247  -1364   -149  -1814       C  
ATOM    199  O   SER A  23     -17.694  49.350  24.810  1.00 45.19           O  
ANISOU  199  O   SER A  23     8144   4408   4618  -1435   -164  -1620       O  
ATOM    200  CB  SER A  23     -19.341  51.187  27.039  1.00 51.92           C  
ANISOU  200  CB  SER A  23     8695   5137   5895  -1476      7  -2284       C  
ATOM    201  OG  SER A  23     -18.338  52.050  26.525  1.00 52.89           O  
ANISOU  201  OG  SER A  23     9006   5147   5944  -1525    -86  -2147       O  
ATOM    202  N   TYR A  24     -19.938  49.531  24.595  1.00 50.71           N  
ANISOU  202  N   TYR A  24     8692   4817   5755  -1205   -294  -1866       N  
ATOM    203  CA  TYR A  24     -19.907  49.456  23.133  1.00 52.38           C  
ANISOU  203  CA  TYR A  24     9086   4836   5979  -1125   -505  -1655       C  
ATOM    204  C   TYR A  24     -19.024  50.551  22.589  1.00 53.67           C  
ANISOU  204  C   TYR A  24     9479   4841   6071  -1232   -612  -1559       C  
ATOM    205  O   TYR A  24     -18.161  50.285  21.766  1.00 51.93           O  
ANISOU  205  O   TYR A  24     9429   4665   5637  -1332   -631  -1357       O  
ATOM    206  CB  TYR A  24     -21.297  49.606  22.522  1.00 55.51           C  
ANISOU  206  CB  TYR A  24     9435   4957   6696   -941   -711  -1758       C  
ATOM    207  CG  TYR A  24     -21.273  49.476  21.011  1.00 56.94           C  
ANISOU  207  CG  TYR A  24     9849   4941   6843   -904   -951  -1516       C  
ATOM    208  CD1 TYR A  24     -20.945  50.564  20.198  1.00 58.70           C  
ANISOU  208  CD1 TYR A  24    10343   4873   7085   -967  -1187  -1417       C  
ATOM    209  CD2 TYR A  24     -21.551  48.267  20.401  1.00 54.97           C  
ANISOU  209  CD2 TYR A  24     9581   4793   6510   -850   -943  -1385       C  
ATOM    210  CE1 TYR A  24     -20.917  50.443  18.818  1.00 59.13           C  
ANISOU  210  CE1 TYR A  24    10663   4753   7051  -1008  -1407  -1192       C  
ATOM    211  CE2 TYR A  24     -21.525  48.139  19.021  1.00 55.96           C  
ANISOU  211  CE2 TYR A  24     9933   4755   6575   -861  -1144  -1178       C  
ATOM    212  CZ  TYR A  24     -21.206  49.230  18.237  1.00 57.93           C  
ANISOU  212  CZ  TYR A  24    10469   4726   6815   -959  -1374  -1081       C  
ATOM    213  OH  TYR A  24     -21.162  49.099  16.875  1.00 58.17           O  
ANISOU  213  OH  TYR A  24    10771   4602   6727  -1043  -1572   -872       O  
HETATM  214  N   CGU A  25     -19.227  51.774  23.085  1.00 57.45           N  
ANISOU  214  N   CGU A  25     9956   5144   6729  -1238   -664  -1735       N  
HETATM  215  CA  CGU A  25     -18.520  52.929  22.555  1.00 60.10           C  
ANISOU  215  CA  CGU A  25    10545   5272   7015  -1354   -802  -1652       C  
HETATM  216  C   CGU A  25     -17.047  52.809  22.814  1.00 56.22           C  
ANISOU  216  C   CGU A  25    10119   5053   6189  -1562   -601  -1545       C  
HETATM  217  O   CGU A  25     -16.247  53.099  21.930  1.00 53.84           O  
ANISOU  217  O   CGU A  25    10056   4692   5707  -1712   -665  -1386       O  
HETATM  218  CB  CGU A  25     -19.100  54.232  23.107  1.00 67.43           C  
ANISOU  218  CB  CGU A  25    11432   5935   8252  -1297   -915  -1895       C  
HETATM  219  CG  CGU A  25     -18.258  55.462  22.703  1.00 74.06           C  
ANISOU  219  CG  CGU A  25    12566   6568   9006  -1458  -1046  -1804       C  
HETATM  220  CD1 CGU A  25     -18.173  55.699  21.206  1.00 74.78           C  
ANISOU  220  CD1 CGU A  25    13021   6371   9019  -1526  -1348  -1552       C  
HETATM  221  CD2 CGU A  25     -18.757  56.684  23.410  1.00 77.94           C  
ANISOU  221  CD2 CGU A  25    12977   6819   9818  -1397  -1135  -2075       C  
HETATM  222 OE11 CGU A  25     -18.976  55.138  20.428  1.00 72.06           O  
ANISOU  222 OE11 CGU A  25    12702   5895   8782  -1399  -1533  -1472       O  
HETATM  223 OE12 CGU A  25     -17.269  56.468  20.807  1.00 81.41           O  
ANISOU  223 OE12 CGU A  25    14147   7123   9662  -1748  -1397  -1435       O  
HETATM  224 OE21 CGU A  25     -18.071  57.723  23.308  1.00 84.41           O  
ANISOU  224 OE21 CGU A  25    14015   7484  10573  -1539  -1214  -2035       O  
HETATM  225 OE22 CGU A  25     -19.815  56.593  24.069  1.00 80.40           O  
ANISOU  225 OE22 CGU A  25    12997   7103  10445  -1227  -1109  -2355       O  
HETATM  226  N   CGU A  26     -16.675  52.378  24.019  1.00 54.69           N  
ANISOU  226  N   CGU A  26     9720   5155   5903  -1601   -368  -1648       N  
HETATM  227  CA  CGU A  26     -15.258  52.208  24.369  1.00 53.26           C  
ANISOU  227  CA  CGU A  26     9554   5234   5445  -1777   -209  -1577       C  
HETATM  228  C   CGU A  26     -14.680  51.251  23.377  1.00 52.10           C  
ANISOU  228  C   CGU A  26     9473   5189   5134  -1804   -221  -1392       C  
HETATM  229  O   CGU A  26     -13.621  51.495  22.816  1.00 53.16           O  
ANISOU  229  O   CGU A  26     9730   5366   5099  -1967   -195  -1326       O  
HETATM  230  CB  CGU A  26     -15.110  51.687  25.796  1.00 52.59           C  
ANISOU  230  CB  CGU A  26     9260   5428   5292  -1809    -26  -1689       C  
HETATM  231  CG  CGU A  26     -13.698  51.859  26.368  1.00 54.44           C  
ANISOU  231  CG  CGU A  26     9498   5874   5311  -1985     84  -1674       C  
HETATM  232  CD1 CGU A  26     -13.333  53.290  26.612  1.00 55.96           C  
ANISOU  232  CD1 CGU A  26     9787   5945   5529  -2097     98  -1778       C  
HETATM  233  CD2 CGU A  26     -13.551  51.153  27.693  1.00 53.15           C  
ANISOU  233  CD2 CGU A  26     9180   5969   5045  -2038    197  -1733       C  
HETATM  234 OE11 CGU A  26     -14.094  54.236  26.301  1.00 68.20           O  
ANISOU  234 OE11 CGU A  26    11421   7213   7276  -2041     -7  -1857       O  
HETATM  235 OE12 CGU A  26     -12.230  53.492  27.128  1.00 56.54           O  
ANISOU  235 OE12 CGU A  26     9848   6192   5440  -2245    192  -1791       O  
HETATM  236 OE21 CGU A  26     -12.406  51.092  28.209  1.00 54.55           O  
ANISOU  236 OE21 CGU A  26     9339   6328   5060  -2164    243  -1712       O  
HETATM  237 OE22 CGU A  26     -14.583  50.670  28.229  1.00 51.69           O  
ANISOU  237 OE22 CGU A  26     8903   5801   4936  -1982    226  -1811       O  
ATOM    238  N   ALA A  27     -15.407  50.163  23.131  1.00 49.28           N  
ANISOU  238  N   ALA A  27     9022   4869   4833  -1664   -248  -1341       N  
ATOM    239  CA  ALA A  27     -15.005  49.187  22.154  1.00 48.35           C  
ANISOU  239  CA  ALA A  27     8941   4830   4596  -1674   -261  -1196       C  
ATOM    240  C   ALA A  27     -14.848  49.778  20.751  1.00 49.40           C  
ANISOU  240  C   ALA A  27     9338   4755   4675  -1784   -387  -1094       C  
ATOM    241  O   ALA A  27     -13.884  49.461  20.074  1.00 48.62           O  
ANISOU  241  O   ALA A  27     9302   4772   4396  -1940   -318  -1041       O  
ATOM    242  CB  ALA A  27     -15.998  48.035  22.126  1.00 47.33           C  
ANISOU  242  CB  ALA A  27     8687   4731   4562  -1501   -288  -1168       C  
ATOM    243  N   PHE A  28     -15.795  50.609  20.318  1.00 51.95           N  
ANISOU  243  N   PHE A  28     9817   4764   5158  -1726   -586  -1087       N  
ATOM    244  CA  PHE A  28     -15.723  51.241  18.989  1.00 55.75           C  
ANISOU  244  CA  PHE A  28    10631   4992   5559  -1878   -774   -958       C  
ATOM    245  C   PHE A  28     -14.506  52.154  18.838  1.00 57.58           C  
ANISOU  245  C   PHE A  28    11060   5239   5578  -2165   -706   -955       C  
ATOM    246  O   PHE A  28     -13.804  52.109  17.833  1.00 57.35           O  
ANISOU  246  O   PHE A  28    11240   5230   5318  -2411   -687   -869       O  
ATOM    247  CB  PHE A  28     -16.995  52.031  18.700  1.00 58.21           C  
ANISOU  247  CB  PHE A  28    11067   4908   6140  -1737  -1080   -966       C  
ATOM    248  CG  PHE A  28     -16.973  52.738  17.383  1.00 62.38           C  
ANISOU  248  CG  PHE A  28    12006   5121   6573  -1922  -1352   -803       C  
ATOM    249  CD1 PHE A  28     -17.475  52.134  16.252  1.00 62.97           C  
ANISOU  249  CD1 PHE A  28    12229   5091   6602  -1930  -1512   -657       C  
ATOM    250  CD2 PHE A  28     -16.445  54.026  17.275  1.00 68.95           C  
ANISOU  250  CD2 PHE A  28    13114   5748   7333  -2127  -1463   -788       C  
ATOM    251  CE1 PHE A  28     -17.467  52.781  15.033  1.00 65.54           C  
ANISOU  251  CE1 PHE A  28    12992   5113   6794  -2160  -1793   -488       C  
ATOM    252  CE2 PHE A  28     -16.423  54.687  16.049  1.00 70.56           C  
ANISOU  252  CE2 PHE A  28    13771   5635   7403  -2362  -1751   -613       C  
ATOM    253  CZ  PHE A  28     -16.936  54.055  14.929  1.00 70.64           C  
ANISOU  253  CZ  PHE A  28    13946   5544   7347  -2390  -1921   -459       C  
HETATM  254  N   CGU A  29     -14.259  52.974  19.849  1.00 60.34           N  
ANISOU  254  N   CGU A  29    11339   5593   5992  -2165   -647  -1075       N  
HETATM  255  CA  CGU A  29     -13.099  53.872  19.868  1.00 63.51           C  
ANISOU  255  CA  CGU A  29    11900   6029   6201  -2437   -561  -1100       C  
HETATM  256  C   CGU A  29     -11.831  53.046  19.678  1.00 61.87           C  
ANISOU  256  C   CGU A  29    11584   6172   5749  -2609   -319  -1116       C  
HETATM  257  O   CGU A  29     -10.839  53.536  19.167  1.00 69.29           O  
ANISOU  257  O   CGU A  29    12694   7153   6478  -2903   -241  -1129       O  
HETATM  258  CB  CGU A  29     -13.090  54.647  21.206  1.00 65.06           C  
ANISOU  258  CB  CGU A  29    11950   6239   6531  -2367   -495  -1257       C  
HETATM  259  CG  CGU A  29     -13.328  56.187  21.335  1.00 72.03           C  
ANISOU  259  CG  CGU A  29    13044   6791   7533  -2429   -665  -1311       C  
HETATM  260  CD1 CGU A  29     -13.947  56.999  20.197  1.00 73.99           C  
ANISOU  260  CD1 CGU A  29    13667   6590   7855  -2486  -1014  -1187       C  
HETATM  261  CD2 CGU A  29     -13.999  56.390  22.686  1.00 73.00           C  
ANISOU  261  CD2 CGU A  29    12883   6938   7913  -2222   -605  -1513       C  
HETATM  262 OE11 CGU A  29     -13.389  57.053  19.079  1.00 75.37           O  
ANISOU  262 OE11 CGU A  29    14155   6709   7773  -2748  -1073  -1029       O  
HETATM  263 OE12 CGU A  29     -14.978  57.661  20.387  1.00 78.75           O  
ANISOU  263 OE12 CGU A  29    14280   6865   8776  -2303  -1258  -1261       O  
HETATM  264 OE21 CGU A  29     -15.209  56.622  22.824  1.00 74.43           O  
ANISOU  264 OE21 CGU A  29    12995   6883   8401  -2017   -772  -1609       O  
HETATM  265 OE22 CGU A  29     -13.257  56.294  23.679  1.00 79.38           O  
ANISOU  265 OE22 CGU A  29    13518   8031   8611  -2290   -373  -1609       O  
ATOM    266  N   ALA A  30     -11.846  51.783  20.096  1.00 58.75           N  
ANISOU  266  N   ALA A  30    10899   6022   5400  -2440   -209  -1142       N  
ATOM    267  CA  ALA A  30     -10.678  50.907  19.956  1.00 57.27           C  
ANISOU  267  CA  ALA A  30    10550   6140   5070  -2552    -26  -1203       C  
ATOM    268  C   ALA A  30     -10.583  50.242  18.577  1.00 58.13           C  
ANISOU  268  C   ALA A  30    10766   6250   5067  -2674    -25  -1145       C  
ATOM    269  O   ALA A  30      -9.497  50.108  18.030  1.00 58.20           O  
ANISOU  269  O   ALA A  30    10772   6423   4918  -2918    122  -1241       O  
ATOM    270  CB  ALA A  30     -10.703  49.834  21.032  1.00 54.63           C  
ANISOU  270  CB  ALA A  30     9887   6024   4844  -2331     32  -1251       C  
ATOM    271  N   LEU A  31     -11.710  49.795  18.033  1.00 58.76           N  
ANISOU  271  N   LEU A  31    10919   6169   5237  -2521   -172  -1022       N  
ATOM    272  CA  LEU A  31     -11.710  49.119  16.725  1.00 61.45           C  
ANISOU  272  CA  LEU A  31    11372   6512   5463  -2646   -173   -964       C  
ATOM    273  C   LEU A  31     -11.916  50.050  15.520  1.00 63.81           C  
ANISOU  273  C   LEU A  31    12108   6542   5592  -2929   -321   -851       C  
ATOM    274  O   LEU A  31     -11.577  49.695  14.389  1.00 65.35           O  
ANISOU  274  O   LEU A  31    12455   6778   5595  -3181   -270   -838       O  
ATOM    275  CB  LEU A  31     -12.766  48.026  16.714  1.00 61.99           C  
ANISOU  275  CB  LEU A  31    11293   6563   5695  -2358   -258   -888       C  
ATOM    276  CG  LEU A  31     -12.595  46.943  17.794  1.00 61.54           C  
ANISOU  276  CG  LEU A  31    10869   6746   5763  -2129   -152   -967       C  
ATOM    277  CD1 LEU A  31     -13.710  45.906  17.691  1.00 59.58           C  
ANISOU  277  CD1 LEU A  31    10530   6460   5647  -1890   -238   -884       C  
ATOM    278  CD2 LEU A  31     -11.231  46.275  17.688  1.00 61.18           C  
ANISOU  278  CD2 LEU A  31    10641   6967   5636  -2261     20  -1106       C  
HETATM  279  N   CGU A  32     -12.513  51.214  15.764  1.00 65.62           N  
ANISOU  279  N   CGU A  32    12552   6480   5900  -2901   -528   -778       N  
HETATM  280  CA  CGU A  32     -12.648  52.265  14.758  1.00 68.60           C  
ANISOU  280  CA  CGU A  32    13403   6541   6119  -3191   -744   -653       C  
HETATM  281  C   CGU A  32     -13.300  51.698  13.519  1.00 69.43           C  
ANISOU  281  C   CGU A  32    13717   6514   6148  -3258   -903   -509       C  
HETATM  282  O   CGU A  32     -12.856  51.943  12.404  1.00 75.12           O  
ANISOU  282  O   CGU A  32    14789   7178   6575  -3657   -922   -444       O  
HETATM  283  CB  CGU A  32     -11.250  52.873  14.575  1.00 70.84           C  
ANISOU  283  CB  CGU A  32    13827   6975   6112  -3607   -536   -751       C  
HETATM  284  CG  CGU A  32     -10.770  53.508  15.908  1.00 73.28           C  
ANISOU  284  CG  CGU A  32    13928   7376   6538  -3494   -427   -880       C  
HETATM  285  CD1 CGU A  32      -9.262  53.493  16.077  1.00 74.41           C  
ANISOU  285  CD1 CGU A  32    13947   7847   6477  -3774   -113  -1066       C  
HETATM  286  CD2 CGU A  32     -11.366  54.887  16.099  1.00 74.43           C  
ANISOU  286  CD2 CGU A  32    14364   7137   6779  -3490   -701   -798       C  
HETATM  287 OE11 CGU A  32      -8.564  52.951  15.199  1.00 75.25           O  
ANISOU  287 OE11 CGU A  32    14082   8131   6378  -4051     51  -1140       O  
HETATM  288 OE12 CGU A  32      -8.746  53.978  17.108  1.00 72.79           O  
ANISOU  288 OE12 CGU A  32    13581   7742   6332  -3724    -16  -1176       O  
HETATM  289 OE21 CGU A  32     -12.204  55.282  15.258  1.00 75.87           O  
ANISOU  289 OE21 CGU A  32    14883   6963   6981  -3527  -1018   -635       O  
HETATM  290 OE22 CGU A  32     -11.043  55.577  17.098  1.00 73.95           O  
ANISOU  290 OE22 CGU A  32    14192   7102   6801  -3439   -635   -901       O  
ATOM    291  N   SER A  33     -14.358  50.914  13.726  1.00 66.03           N  
ANISOU  291  N   SER A  33    13074   6049   5963  -2899  -1005   -473       N  
ATOM    292  CA  SER A  33     -15.108  50.282  12.654  1.00 64.49           C  
ANISOU  292  CA  SER A  33    13028   5735   5739  -2904  -1168   -342       C  
ATOM    293  C   SER A  33     -16.408  49.681  13.179  1.00 63.60           C  
ANISOU  293  C   SER A  33    12651   5544   5967  -2462  -1305   -337       C  
ATOM    294  O   SER A  33     -16.381  48.802  14.039  1.00 64.44           O  
ANISOU  294  O   SER A  33    12373   5914   6196  -2230  -1092   -446       O  
ATOM    295  CB  SER A  33     -14.278  49.173  12.022  1.00 63.52           C  
ANISOU  295  CB  SER A  33    12801   5944   5390  -3105   -877   -408       C  
ATOM    296  OG  SER A  33     -15.119  48.195  11.442  1.00 59.95           O  
ANISOU  296  OG  SER A  33    12298   5469   5010  -2954   -964   -330       O  
ATOM    297  N   SER A  34     -17.541  50.123  12.643  1.00 65.19           N  
ANISOU  297  N   SER A  34    13067   5378   6322  -2369  -1675   -224       N  
ATOM    298  CA  SER A  34     -18.850  49.634  13.101  1.00 65.20           C  
ANISOU  298  CA  SER A  34    12804   5291   6676  -1970  -1810   -271       C  
ATOM    299  C   SER A  34     -19.070  48.148  12.907  1.00 63.70           C  
ANISOU  299  C   SER A  34    12379   5360   6463  -1853  -1632   -271       C  
ATOM    300  O   SER A  34     -19.701  47.506  13.747  1.00 62.78           O  
ANISOU  300  O   SER A  34    11924   5359   6570  -1561  -1545   -378       O  
ATOM    301  CB  SER A  34     -19.988  50.372  12.415  1.00 67.44           C  
ANISOU  301  CB  SER A  34    13359   5104   7159  -1901  -2293   -174       C  
ATOM    302  OG  SER A  34     -20.164  51.615  13.043  1.00 70.51           O  
ANISOU  302  OG  SER A  34    13793   5233   7763  -1829  -2479   -257       O  
ATOM    303  N   THR A  35     -18.580  47.618  11.794  1.00 62.35           N  
ANISOU  303  N   THR A  35    12403   5271   6014  -2112  -1578   -167       N  
ATOM    304  CA  THR A  35     -18.705  46.210  11.523  1.00 61.44           C  
ANISOU  304  CA  THR A  35    12080   5389   5874  -2026  -1410   -177       C  
ATOM    305  C   THR A  35     -17.914  45.403  12.517  1.00 58.48           C  
ANISOU  305  C   THR A  35    11330   5381   5508  -1926  -1062   -323       C  
ATOM    306  O   THR A  35     -18.452  44.507  13.168  1.00 58.38           O  
ANISOU  306  O   THR A  35    11027   5487   5666  -1659   -993   -373       O  
ATOM    307  CB  THR A  35     -18.174  45.861  10.125  1.00 63.80           C  
ANISOU  307  CB  THR A  35    12660   5728   5853  -2389  -1377    -87       C  
ATOM    308  OG1 THR A  35     -18.998  46.501   9.158  1.00 64.79           O  
ANISOU  308  OG1 THR A  35    13178   5485   5951  -2498  -1763     84       O  
ATOM    309  CG2 THR A  35     -18.194  44.351   9.905  1.00 61.22           C  
ANISOU  309  CG2 THR A  35    12074   5662   5524  -2293  -1170   -137       C  
ATOM    310  N   ALA A  36     -16.628  45.708  12.619  1.00 56.55           N  
ANISOU  310  N   ALA A  36    11106   5303   5075  -2162   -864   -396       N  
ATOM    311  CA  ALA A  36     -15.789  44.993  13.542  1.00 53.64           C  
ANISOU  311  CA  ALA A  36    10396   5248   4735  -2075   -599   -538       C  
ATOM    312  C   ALA A  36     -16.378  45.122  14.937  1.00 51.81           C  
ANISOU  312  C   ALA A  36     9945   5008   4733  -1780   -628   -582       C  
ATOM    313  O   ALA A  36     -16.443  44.153  15.699  1.00 51.04           O  
ANISOU  313  O   ALA A  36     9574   5088   4728  -1598   -526   -634       O  
ATOM    314  CB  ALA A  36     -14.390  45.536  13.506  1.00 54.49           C  
ANISOU  314  CB  ALA A  36    10554   5496   4652  -2368   -424   -644       C  
ATOM    315  N   THR A  37     -16.853  46.307  15.272  1.00 51.49           N  
ANISOU  315  N   THR A  37    10037   4744   4782  -1756   -782   -572       N  
ATOM    316  CA  THR A  37     -17.379  46.479  16.596  1.00 50.41           C  
ANISOU  316  CA  THR A  37     9683   4622   4848  -1534   -767   -670       C  
ATOM    317  C   THR A  37     -18.658  45.679  16.797  1.00 50.32           C  
ANISOU  317  C   THR A  37     9507   4577   5033  -1285   -834   -681       C  
ATOM    318  O   THR A  37     -18.855  45.144  17.871  1.00 48.85           O  
ANISOU  318  O   THR A  37     9086   4551   4924  -1160   -713   -772       O  
ATOM    319  CB  THR A  37     -17.553  47.955  16.949  1.00 51.59           C  
ANISOU  319  CB  THR A  37     9973   4540   5089  -1566   -902   -713       C  
ATOM    320  OG1 THR A  37     -16.286  48.611  16.788  1.00 52.80           O  
ANISOU  320  OG1 THR A  37    10277   4757   5024  -1831   -805   -709       O  
ATOM    321  CG2 THR A  37     -18.009  48.118  18.383  1.00 50.14           C  
ANISOU  321  CG2 THR A  37     9536   4416   5097  -1388   -827   -872       C  
ATOM    322  N   ASP A  38     -19.509  45.556  15.780  1.00 51.42           N  
ANISOU  322  N   ASP A  38     9782   4520   5233  -1244  -1028   -594       N  
ATOM    323  CA  ASP A  38     -20.712  44.746  15.929  1.00 51.01           C  
ANISOU  323  CA  ASP A  38     9556   4456   5369  -1021  -1075   -630       C  
ATOM    324  C   ASP A  38     -20.349  43.257  16.068  1.00 48.76           C  
ANISOU  324  C   ASP A  38     9094   4457   4972   -996   -871   -607       C  
ATOM    325  O   ASP A  38     -20.921  42.518  16.884  1.00 46.75           O  
ANISOU  325  O   ASP A  38     8629   4317   4815   -855   -789   -681       O  
ATOM    326  CB  ASP A  38     -21.648  44.963  14.746  1.00 54.59           C  
ANISOU  326  CB  ASP A  38    10204   4619   5916   -990  -1366   -538       C  
ATOM    327  CG  ASP A  38     -22.375  46.289  14.819  1.00 59.16           C  
ANISOU  327  CG  ASP A  38    10886   4854   6738   -918  -1652   -605       C  
ATOM    328  OD1 ASP A  38     -22.390  46.902  15.900  1.00 59.20           O  
ANISOU  328  OD1 ASP A  38    10737   4871   6885   -847  -1579   -768       O  
ATOM    329  OD2 ASP A  38     -22.939  46.716  13.797  1.00 62.84           O  
ANISOU  329  OD2 ASP A  38    11591   5019   7267   -938  -1973   -504       O  
ATOM    330  N   VAL A  39     -19.392  42.825  15.262  1.00 46.07           N  
ANISOU  330  N   VAL A  39     8849   4223   4432  -1160   -795   -528       N  
ATOM    331  CA  VAL A  39     -18.904  41.481  15.347  1.00 43.92           C  
ANISOU  331  CA  VAL A  39     8404   4187   4096  -1136   -637   -534       C  
ATOM    332  C   VAL A  39     -18.433  41.206  16.785  1.00 42.87           C  
ANISOU  332  C   VAL A  39     8061   4235   3992  -1068   -511   -621       C  
ATOM    333  O   VAL A  39     -18.877  40.243  17.417  1.00 40.34           O  
ANISOU  333  O   VAL A  39     7588   4008   3730   -945   -479   -631       O  
ATOM    334  CB  VAL A  39     -17.771  41.237  14.329  1.00 45.50           C  
ANISOU  334  CB  VAL A  39     8697   4483   4108  -1360   -545   -524       C  
ATOM    335  CG1 VAL A  39     -16.989  39.965  14.643  1.00 44.72           C  
ANISOU  335  CG1 VAL A  39     8359   4623   4009  -1321   -392   -599       C  
ATOM    336  CG2 VAL A  39     -18.352  41.145  12.929  1.00 47.49           C  
ANISOU  336  CG2 VAL A  39     9163   4589   4292  -1455   -663   -426       C  
ATOM    337  N   PHE A  40     -17.541  42.037  17.304  1.00 42.29           N  
ANISOU  337  N   PHE A  40     8007   4205   3856  -1178   -454   -675       N  
ATOM    338  CA  PHE A  40     -17.072  41.828  18.671  1.00 41.83           C  
ANISOU  338  CA  PHE A  40     7783   4307   3803  -1144   -369   -744       C  
ATOM    339  C   PHE A  40     -18.208  41.793  19.691  1.00 41.74           C  
ANISOU  339  C   PHE A  40     7691   4267   3901  -1024   -385   -790       C  
ATOM    340  O   PHE A  40     -18.244  40.938  20.584  1.00 40.48           O  
ANISOU  340  O   PHE A  40     7416   4241   3722   -994   -341   -802       O  
ATOM    341  CB  PHE A  40     -16.112  42.908  19.077  1.00 43.61           C  
ANISOU  341  CB  PHE A  40     8054   4557   3958  -1282   -320   -806       C  
ATOM    342  CG  PHE A  40     -15.732  42.838  20.510  1.00 43.74           C  
ANISOU  342  CG  PHE A  40     7936   4713   3971  -1269   -264   -870       C  
ATOM    343  CD1 PHE A  40     -14.825  41.880  20.943  1.00 44.15           C  
ANISOU  343  CD1 PHE A  40     7851   4938   3983  -1274   -244   -880       C  
ATOM    344  CD2 PHE A  40     -16.293  43.702  21.429  1.00 44.42           C  
ANISOU  344  CD2 PHE A  40     8031   4741   4105  -1264   -257   -938       C  
ATOM    345  CE1 PHE A  40     -14.468  41.785  22.288  1.00 45.71           C  
ANISOU  345  CE1 PHE A  40     7970   5243   4152  -1293   -247   -913       C  
ATOM    346  CE2 PHE A  40     -15.935  43.631  22.771  1.00 46.50           C  
ANISOU  346  CE2 PHE A  40     8202   5145   4320  -1308   -201   -998       C  
ATOM    347  CZ  PHE A  40     -15.033  42.656  23.206  1.00 46.41           C  
ANISOU  347  CZ  PHE A  40     8101   5299   4231  -1330   -211   -963       C  
ATOM    348  N   TRP A  41     -19.147  42.707  19.545  1.00 43.11           N  
ANISOU  348  N   TRP A  41     7931   4253   4196   -981   -462   -837       N  
ATOM    349  CA  TRP A  41     -20.170  42.895  20.568  1.00 44.23           C  
ANISOU  349  CA  TRP A  41     7957   4378   4469   -909   -437   -976       C  
ATOM    350  C   TRP A  41     -21.128  41.726  20.664  1.00 43.58           C  
ANISOU  350  C   TRP A  41     7769   4353   4436   -819   -418   -985       C  
ATOM    351  O   TRP A  41     -21.691  41.431  21.747  1.00 41.51           O  
ANISOU  351  O   TRP A  41     7393   4188   4188   -842   -323  -1106       O  
ATOM    352  CB  TRP A  41     -20.946  44.193  20.325  1.00 45.51           C  
ANISOU  352  CB  TRP A  41     8174   4288   4829   -860   -562  -1081       C  
ATOM    353  CG  TRP A  41     -21.642  44.672  21.546  1.00 45.86           C  
ANISOU  353  CG  TRP A  41     8063   4346   5015   -845   -482  -1310       C  
ATOM    354  CD1 TRP A  41     -22.975  44.669  21.767  1.00 46.96           C  
ANISOU  354  CD1 TRP A  41     8059   4397   5385   -743   -506  -1502       C  
ATOM    355  CD2 TRP A  41     -21.031  45.208  22.727  1.00 45.94           C  
ANISOU  355  CD2 TRP A  41     8027   4482   4946   -966   -344  -1415       C  
ATOM    356  NE1 TRP A  41     -23.246  45.179  23.017  1.00 49.54           N  
ANISOU  356  NE1 TRP A  41     8243   4797   5781   -813   -365  -1749       N  
ATOM    357  CE2 TRP A  41     -22.069  45.515  23.629  1.00 47.49           C  
ANISOU  357  CE2 TRP A  41     8057   4667   5317   -955   -268  -1682       C  
ATOM    358  CE3 TRP A  41     -19.707  45.470  23.106  1.00 45.33           C  
ANISOU  358  CE3 TRP A  41     8019   4531   4674  -1098   -274  -1337       C  
ATOM    359  CZ2 TRP A  41     -21.830  46.063  24.891  1.00 47.14           C  
ANISOU  359  CZ2 TRP A  41     7941   4739   5228  -1094   -114  -1858       C  
ATOM    360  CZ3 TRP A  41     -19.465  45.997  24.361  1.00 45.30           C  
ANISOU  360  CZ3 TRP A  41     7948   4632   4631  -1209   -152  -1482       C  
ATOM    361  CH2 TRP A  41     -20.524  46.295  25.240  1.00 46.32           C  
ANISOU  361  CH2 TRP A  41     7939   4752   4909  -1218    -68  -1733       C  
ATOM    362  N   ALA A  42     -21.324  41.064  19.534  1.00 41.65           N  
ANISOU  362  N   ALA A  42     7577   4055   4193   -757   -496   -869       N  
ATOM    363  CA  ALA A  42     -22.178  39.903  19.519  1.00 42.19           C  
ANISOU  363  CA  ALA A  42     7559   4176   4296   -679   -480   -865       C  
ATOM    364  C   ALA A  42     -21.510  38.779  20.318  1.00 41.55           C  
ANISOU  364  C   ALA A  42     7423   4302   4060   -742   -385   -811       C  
ATOM    365  O   ALA A  42     -22.158  38.059  21.078  1.00 41.26           O  
ANISOU  365  O   ALA A  42     7322   4346   4007   -760   -331   -861       O  
ATOM    366  CB  ALA A  42     -22.453  39.469  18.088  1.00 42.62           C  
ANISOU  366  CB  ALA A  42     7694   4124   4372   -617   -589   -750       C  
ATOM    367  N   LYS A  43     -20.207  38.628  20.161  1.00 40.67           N  
ANISOU  367  N   LYS A  43     7343   4265   3841   -798   -386   -728       N  
ATOM    368  CA  LYS A  43     -19.492  37.691  21.006  1.00 40.39           C  
ANISOU  368  CA  LYS A  43     7260   4377   3707   -845   -375   -689       C  
ATOM    369  C   LYS A  43     -19.564  38.110  22.469  1.00 41.72           C  
ANISOU  369  C   LYS A  43     7422   4619   3809   -954   -323   -769       C  
ATOM    370  O   LYS A  43     -19.850  37.293  23.343  1.00 41.65           O  
ANISOU  370  O   LYS A  43     7419   4688   3718  -1022   -325   -756       O  
ATOM    371  CB  LYS A  43     -18.060  37.602  20.563  1.00 41.92           C  
ANISOU  371  CB  LYS A  43     7440   4622   3865   -875   -400   -655       C  
ATOM    372  CG  LYS A  43     -17.960  36.985  19.188  1.00 43.85           C  
ANISOU  372  CG  LYS A  43     7682   4831   4149   -825   -417   -614       C  
ATOM    373  CD  LYS A  43     -16.849  37.564  18.370  1.00 47.26           C  
ANISOU  373  CD  LYS A  43     8129   5276   4550   -919   -378   -660       C  
ATOM    374  CE  LYS A  43     -15.518  36.901  18.621  1.00 49.47           C  
ANISOU  374  CE  LYS A  43     8267   5676   4851   -942   -388   -729       C  
ATOM    375  NZ  LYS A  43     -14.717  37.071  17.369  1.00 53.04           N  
ANISOU  375  NZ  LYS A  43     8708   6153   5288  -1054   -305   -821       N  
ATOM    376  N   TYR A  44     -19.335  39.388  22.727  1.00 41.97           N  
ANISOU  376  N   TYR A  44     7468   4620   3859  -1003   -280   -854       N  
ATOM    377  CA  TYR A  44     -19.306  39.885  24.097  1.00 44.07           C  
ANISOU  377  CA  TYR A  44     7727   4968   4050  -1138   -210   -954       C  
ATOM    378  C   TYR A  44     -20.637  39.646  24.770  1.00 45.13           C  
ANISOU  378  C   TYR A  44     7822   5120   4203  -1190   -126  -1082       C  
ATOM    379  O   TYR A  44     -20.683  39.333  25.950  1.00 44.34           O  
ANISOU  379  O   TYR A  44     7747   5140   3960  -1364    -68  -1128       O  
ATOM    380  CB  TYR A  44     -19.014  41.367  24.107  1.00 45.42           C  
ANISOU  380  CB  TYR A  44     7911   5069   4276  -1165   -173  -1051       C  
ATOM    381  CG  TYR A  44     -18.350  41.922  25.351  1.00 46.06           C  
ANISOU  381  CG  TYR A  44     7996   5259   4243  -1322   -112  -1121       C  
ATOM    382  CD1 TYR A  44     -17.141  41.417  25.795  1.00 45.93           C  
ANISOU  382  CD1 TYR A  44     7998   5361   4091  -1395   -171  -1023       C  
ATOM    383  CD2 TYR A  44     -18.882  43.008  26.016  1.00 47.75           C  
ANISOU  383  CD2 TYR A  44     8184   5440   4517  -1392    -18  -1306       C  
ATOM    384  CE1 TYR A  44     -16.496  41.947  26.890  1.00 47.70           C  
ANISOU  384  CE1 TYR A  44     8240   5678   4205  -1547   -144  -1076       C  
ATOM    385  CE2 TYR A  44     -18.240  43.558  27.135  1.00 49.17           C  
ANISOU  385  CE2 TYR A  44     8376   5727   4576  -1560     47  -1375       C  
ATOM    386  CZ  TYR A  44     -17.043  43.026  27.557  1.00 48.14           C  
ANISOU  386  CZ  TYR A  44     8292   5722   4277  -1642    -19  -1243       C  
ATOM    387  OH  TYR A  44     -16.396  43.535  28.643  1.00 51.25           O  
ANISOU  387  OH  TYR A  44     8710   6217   4542  -1816     16  -1299       O  
ATOM    388  N   THR A  45     -21.713  39.787  24.008  1.00 46.16           N  
ANISOU  388  N   THR A  45     7899   5134   4504  -1069   -126  -1156       N  
ATOM    389  CA  THR A  45     -23.050  39.533  24.514  1.00 49.75           C  
ANISOU  389  CA  THR A  45     8268   5610   5023  -1115    -30  -1340       C  
ATOM    390  C   THR A  45     -23.290  38.036  24.727  1.00 51.19           C  
ANISOU  390  C   THR A  45     8493   5899   5058  -1182    -26  -1235       C  
ATOM    391  O   THR A  45     -23.951  37.599  25.697  1.00 49.85           O  
ANISOU  391  O   THR A  45     8320   5838   4782  -1371     88  -1358       O  
ATOM    392  CB  THR A  45     -24.079  40.097  23.544  1.00 51.24           C  
ANISOU  392  CB  THR A  45     8370   5613   5485   -936    -90  -1457       C  
ATOM    393  OG1 THR A  45     -23.910  41.521  23.483  1.00 55.68           O  
ANISOU  393  OG1 THR A  45     8921   6039   6193   -899   -132  -1565       O  
ATOM    394  CG2 THR A  45     -25.489  39.768  23.974  1.00 52.53           C  
ANISOU  394  CG2 THR A  45     8390   5806   5764   -972     13  -1702       C  
ATOM    395  N   ALA A  46     -22.741  37.239  23.831  1.00 51.26           N  
ANISOU  395  N   ALA A  46     8554   5874   5048  -1062   -146  -1024       N  
ATOM    396  CA  ALA A  46     -22.846  35.790  23.992  1.00 52.90           C  
ANISOU  396  CA  ALA A  46     8819   6147   5133  -1112   -185   -906       C  
ATOM    397  C   ALA A  46     -22.037  35.316  25.196  1.00 53.89           C  
ANISOU  397  C   ALA A  46     9058   6376   5041  -1309   -231   -825       C  
ATOM    398  O   ALA A  46     -22.348  34.277  25.754  1.00 55.61           O  
ANISOU  398  O   ALA A  46     9371   6641   5118  -1444   -262   -769       O  
ATOM    399  CB  ALA A  46     -22.406  35.065  22.739  1.00 51.73           C  
ANISOU  399  CB  ALA A  46     8674   5929   5048   -939   -303   -739       C  
ATOM    400  N   CYS A  47     -21.027  36.078  25.605  1.00 53.06           N  
ANISOU  400  N   CYS A  47     8966   6293   4898  -1346   -259   -816       N  
ATOM    401  CA  CYS A  47     -20.194  35.695  26.731  1.00 55.33           C  
ANISOU  401  CA  CYS A  47     9371   6657   4992  -1531   -357   -732       C  
ATOM    402  C   CYS A  47     -20.589  36.395  28.041  1.00 57.84           C  
ANISOU  402  C   CYS A  47     9743   7075   5156  -1800   -215   -888       C  
ATOM    403  O   CYS A  47     -19.815  36.384  28.993  1.00 58.27           O  
ANISOU  403  O   CYS A  47     9911   7188   5039  -1977   -301   -828       O  
ATOM    404  CB  CYS A  47     -18.722  35.943  26.373  1.00 57.74           C  
ANISOU  404  CB  CYS A  47     9641   6938   5356  -1419   -495   -641       C  
ATOM    405  SG  CYS A  47     -18.088  34.944  24.962  1.00 60.63           S  
ANISOU  405  SG  CYS A  47     9925   7220   5888  -1178   -645   -521       S  
ATOM    406  N   GLU A  48     -21.794  36.981  28.085  1.00 61.66           N  
ANISOU  406  N   GLU A  48    10135   7574   5718  -1841     -9  -1115       N  
ATOM    407  CA  GLU A  48     -22.354  37.658  29.277  1.00 67.93           C  
ANISOU  407  CA  GLU A  48    10930   8476   6402  -2122    184  -1357       C  
ATOM    408  C   GLU A  48     -22.201  36.872  30.571  1.00 68.80           C  
ANISOU  408  C   GLU A  48    11260   8711   6168  -2493    160  -1293       C  
ATOM    409  O   GLU A  48     -21.954  37.455  31.620  1.00 72.28           O  
ANISOU  409  O   GLU A  48    11767   9248   6446  -2751    241  -1396       O  
ATOM    410  CB  GLU A  48     -23.857  37.914  29.110  1.00 74.93           C  
ANISOU  410  CB  GLU A  48    11655   9361   7451  -2127    386  -1652       C  
ATOM    411  CG  GLU A  48     -24.239  39.269  28.530  1.00 84.41           C  
ANISOU  411  CG  GLU A  48    12651  10447   8973  -1920    450  -1871       C  
ATOM    412  CD  GLU A  48     -25.711  39.340  28.088  1.00 94.04           C  
ANISOU  412  CD  GLU A  48    13673  11607  10447  -1835    553  -2149       C  
ATOM    413  OE1 GLU A  48     -26.231  38.355  27.499  1.00 93.74           O  
ANISOU  413  OE1 GLU A  48    13644  11555  10416  -1761    507  -2058       O  
ATOM    414  OE2 GLU A  48     -26.353  40.393  28.319  1.00102.11           O  
ANISOU  414  OE2 GLU A  48    14514  12586  11697  -1832    665  -2484       O  
ATOM    415  N   THR A  49     -22.385  35.555  30.496  1.00 67.08           N  
ANISOU  415  N   THR A  49    11180   8479   5829  -2546     37  -1124       N  
ATOM    416  CA  THR A  49     -22.400  34.696  31.677  1.00 68.13           C  
ANISOU  416  CA  THR A  49    11588   8690   5605  -2948    -27  -1042       C  
ATOM    417  C   THR A  49     -21.042  34.083  31.947  1.00 67.94           C  
ANISOU  417  C   THR A  49    11757   8589   5465  -2938   -383   -732       C  
ATOM    418  O   THR A  49     -20.917  33.232  32.831  1.00 71.32           O  
ANISOU  418  O   THR A  49    12473   9021   5604  -3250   -553   -591       O  
ATOM    419  CB  THR A  49     -23.387  33.531  31.519  1.00 67.63           C  
ANISOU  419  CB  THR A  49    11613   8626   5456  -3056     -1  -1027       C  
ATOM    420  OG1 THR A  49     -22.865  32.591  30.562  1.00 67.65           O  
ANISOU  420  OG1 THR A  49    11631   8483   5589  -2756   -266   -758       O  
ATOM    421  CG2 THR A  49     -24.759  34.043  31.086  1.00 66.83           C  
ANISOU  421  CG2 THR A  49    11263   8581   5548  -3006    313  -1363       C  
ATOM    422  N   ALA A  50     -20.032  34.511  31.199  1.00 65.12           N  
ANISOU  422  N   ALA A  50    11252   8153   5337  -2607   -513   -645       N  
ATOM    423  CA  ALA A  50     -18.694  33.977  31.349  1.00 66.05           C  
ANISOU  423  CA  ALA A  50    11469   8187   5439  -2546   -862   -419       C  
ATOM    424  C   ALA A  50     -17.633  35.079  31.342  1.00 66.41           C  
ANISOU  424  C   ALA A  50    11384   8255   5592  -2432   -868   -468       C  
ATOM    425  O   ALA A  50     -16.594  34.937  30.690  1.00 64.88           O  
ANISOU  425  O   ALA A  50    11080   7984   5586  -2186  -1056   -383       O  
ATOM    426  CB  ALA A  50     -18.436  33.001  30.223  1.00 64.80           C  
ANISOU  426  CB  ALA A  50    11228   7895   5495  -2238  -1049   -280       C  
ATOM    427  N   ARG A  51     -17.886  36.170  32.067  1.00 68.13           N  
ANISOU  427  N   ARG A  51    11601   8585   5700  -2629   -649   -639       N  
ATOM    428  CA  ARG A  51     -17.007  37.364  31.992  1.00 67.68           C  
ANISOU  428  CA  ARG A  51    11411   8551   5753  -2525   -604   -715       C  
ATOM    429  C   ARG A  51     -15.787  37.272  32.921  1.00 66.86           C  
ANISOU  429  C   ARG A  51    11442   8462   5497  -2681   -864   -595       C  
ATOM    430  O   ARG A  51     -14.781  37.959  32.703  1.00 66.20           O  
ANISOU  430  O   ARG A  51    11237   8378   5536  -2548   -910   -616       O  
ATOM    431  CB  ARG A  51     -17.789  38.661  32.276  1.00 68.97           C  
ANISOU  431  CB  ARG A  51    11481   8797   5927  -2630   -270   -980       C  
ATOM    432  CG  ARG A  51     -18.858  39.033  31.252  1.00 68.30           C  
ANISOU  432  CG  ARG A  51    11215   8653   6083  -2416    -71  -1131       C  
ATOM    433  CD  ARG A  51     -18.279  39.452  29.899  1.00 69.27           C  
ANISOU  433  CD  ARG A  51    11194   8661   6465  -2068   -135  -1068       C  
ATOM    434  NE  ARG A  51     -19.324  39.814  28.920  1.00 67.87           N  
ANISOU  434  NE  ARG A  51    10890   8392   6505  -1885    -10  -1188       N  
ATOM    435  CZ  ARG A  51     -19.968  40.986  28.880  1.00 68.06           C  
ANISOU  435  CZ  ARG A  51    10812   8371   6675  -1867    143  -1410       C  
ATOM    436  NH1 ARG A  51     -19.697  41.959  29.759  1.00 68.40           N  
ANISOU  436  NH1 ARG A  51    10852   8472   6662  -2026    242  -1555       N  
ATOM    437  NH2 ARG A  51     -20.902  41.189  27.956  1.00 68.50           N  
ANISOU  437  NH2 ARG A  51    10766   8306   6955  -1684    172  -1498       N  
ATOM    438  N   THR A  52     -15.878  36.439  33.957  1.00 66.18           N  
ANISOU  438  N   THR A  52    11624   8382   5137  -2987  -1048   -474       N  
ATOM    439  CA  THR A  52     -14.724  36.145  34.794  1.00 67.01           C  
ANISOU  439  CA  THR A  52    11894   8451   5116  -3123  -1405   -320       C  
ATOM    440  C   THR A  52     -14.652  34.644  35.057  1.00 66.61           C  
ANISOU  440  C   THR A  52    12085   8258   4964  -3208  -1796    -85       C  
ATOM    441  O   THR A  52     -15.663  33.948  34.894  1.00 66.45           O  
ANISOU  441  O   THR A  52    12164   8222   4859  -3288  -1708    -62       O  
ATOM    442  CB  THR A  52     -14.750  36.928  36.131  1.00 70.99           C  
ANISOU  442  CB  THR A  52    12573   9090   5307  -3536  -1294   -407       C  
ATOM    443  OG1 THR A  52     -15.958  36.642  36.851  1.00 71.93           O  
ANISOU  443  OG1 THR A  52    12906   9297   5126  -3926  -1101   -476       O  
ATOM    444  CG2 THR A  52     -14.625  38.439  35.875  1.00 70.76           C  
ANISOU  444  CG2 THR A  52    12299   9162   5424  -3421   -971   -635       C  
TER     445      THR A  52                                                      
HETATM 4472 MG    MG A 601      -9.563  55.240  18.675  1.00 54.50          MG  
HETATM 4473 MG    MG A 602     -16.439  58.151  21.923  1.00 59.51          MG  
HETATM 4474 MG    MG A 603     -12.886  56.040  25.826  1.00 75.97          MG  
HETATM 4475 MG    MG A 604     -10.610  52.128  27.541  1.00 44.95          MG  
HETATM 4476 MG    MG A 605      -7.403  46.320  34.422  1.00 61.48          MG  
HETATM 4477 MG    MG A 606      -4.390  39.919  29.595  1.00 50.11          MG  
CONECT   34   40                                                                
CONECT   40   34   41                                                           
CONECT   41   40   42   44                                                      
CONECT   42   41   43   52                                                      
CONECT   43   42                                                                
CONECT   44   41   45                                                           
CONECT   45   44   46   47                                                      
CONECT   46   45   48   49                                                      
CONECT   47   45   50   51                                                      
CONECT   48   46                                                                
CONECT   49   46                                                                
CONECT   50   47                                                                
CONECT   51   47                                                                
CONECT   52   42   53                                                           
CONECT   53   52   54   56                                                      
CONECT   54   53   55   64                                                      
CONECT   55   54                                                                
CONECT   56   53   57                                                           
CONECT   57   56   58   59                                                      
CONECT   58   57   60   61                                                      
CONECT   59   57   62   63                                                      
CONECT   60   58                                                                
CONECT   61   58                                                                
CONECT   62   59                                                                
CONECT   63   59                                                                
CONECT   64   54                                                                
CONECT  105  111                                                                
CONECT  111  105  112                                                           
CONECT  112  111  113  115                                                      
CONECT  113  112  114  123                                                      
CONECT  114  113                                                                
CONECT  115  112  116                                                           
CONECT  116  115  117  118                                                      
CONECT  117  116  119  120                                                      
CONECT  118  116  121  122                                                      
CONECT  119  117                                                                
CONECT  120  117 4477                                                           
CONECT  121  118                                                                
CONECT  122  118 4477                                                           
CONECT  123  113                                                                
CONECT  125  134                                                                
CONECT  134  125  135                                                           
CONECT  135  134  136  138                                                      
CONECT  136  135  137  146                                                      
CONECT  137  136                                                                
CONECT  138  135  139                                                           
CONECT  139  138  140  141                                                      
CONECT  140  139  142  143                                                      
CONECT  141  139  144  145                                                      
CONECT  142  140                                                                
CONECT  143  140 4475                                                           
CONECT  144  141                                                                
CONECT  145  141 4475                                                           
CONECT  146  136                                                                
CONECT  151  195                                                                
CONECT  154  159                                                                
CONECT  159  154  160                                                           
CONECT  160  159  161  163                                                      
CONECT  161  160  162  171                                                      
CONECT  162  161                                                                
CONECT  163  160  164                                                           
CONECT  164  163  165  166                                                      
CONECT  165  164  167  168                                                      
CONECT  166  164  169  170                                                      
CONECT  167  165 4477                                                           
CONECT  168  165                                                                
CONECT  169  166 4477                                                           
CONECT  170  166                                                                
CONECT  171  161  172                                                           
CONECT  172  171  173  175                                                      
CONECT  173  172  174  183                                                      
CONECT  174  173                                                                
CONECT  175  172  176                                                           
CONECT  176  175  177  178                                                      
CONECT  177  176  179  180                                                      
CONECT  178  176  181  182                                                      
CONECT  179  177                                                                
CONECT  180  177 4476                                                           
CONECT  181  178                                                                
CONECT  182  178 4476                                                           
CONECT  183  173                                                                
CONECT  195  151                                                                
CONECT  204  214                                                                
CONECT  214  204  215                                                           
CONECT  215  214  216  218                                                      
CONECT  216  215  217  226                                                      
CONECT  217  216                                                                
CONECT  218  215  219                                                           
CONECT  219  218  220  221                                                      
CONECT  220  219  222  223                                                      
CONECT  221  219  224  225                                                      
CONECT  222  220                                                                
CONECT  223  220 4473                                                           
CONECT  224  221 4473                                                           
CONECT  225  221                                                                
CONECT  226  216  227                                                           
CONECT  227  226  228  230                                                      
CONECT  228  227  229  238                                                      
CONECT  229  228                                                                
CONECT  230  227  231                                                           
CONECT  231  230  232  233                                                      
CONECT  232  231  234  235                                                      
CONECT  233  231  236  237                                                      
CONECT  234  232 4474                                                           
CONECT  235  232 4474 4475                                                      
CONECT  236  233 4475                                                           
CONECT  237  233                                                                
CONECT  238  228                                                                
CONECT  245  254                                                                
CONECT  254  245  255                                                           
CONECT  255  254  256  258                                                      
CONECT  256  255  257  266                                                      
CONECT  257  256 4472                                                           
CONECT  258  255  259                                                           
CONECT  259  258  260  261                                                      
CONECT  260  259  262  263                                                      
CONECT  261  259  264  265                                                      
CONECT  262  260                                                                
CONECT  263  260 4473                                                           
CONECT  264  261 4473                                                           
CONECT  265  261 4474                                                           
CONECT  266  256                                                                
CONECT  273  279                                                                
CONECT  279  273  280                                                           
CONECT  280  279  281  283                                                      
CONECT  281  280  282  291                                                      
CONECT  282  281                                                                
CONECT  283  280  284                                                           
CONECT  284  283  285  286                                                      
CONECT  285  284  287  288                                                      
CONECT  286  284  289  290                                                      
CONECT  287  285                                                                
CONECT  288  285 4472                                                           
CONECT  289  286                                                                
CONECT  290  286 4472                                                           
CONECT  291  281                                                                
CONECT  405  503                                                                
CONECT  503  405                                                                
CONECT  538 1155                                                                
CONECT  635 4478                                                                
CONECT  694 1020                                                                
CONECT  823 4416                                                                
CONECT  928 1121                                                                
CONECT 1020  694                                                                
CONECT 1121  928                                                                
CONECT 1155  538                                                                
CONECT 1250 1852                                                                
CONECT 1410 1721                                                                
CONECT 1626 1810                                                                
CONECT 1721 1410                                                                
CONECT 1810 1626                                                                
CONECT 1852 1250                                                                
CONECT 2067 3279                                                                
CONECT 2512 2630                                                                
CONECT 2630 2512                                                                
CONECT 2711 4444                                                                
CONECT 3279 2067                                                                
CONECT 3688 3804                                                                
CONECT 3804 3688                                                                
CONECT 3905 4138                                                                
CONECT 4138 3905                                                                
CONECT 4416  823 4417 4427                                                      
CONECT 4417 4416 4418 4424                                                      
CONECT 4418 4417 4419 4425                                                      
CONECT 4419 4418 4420 4426                                                      
CONECT 4420 4419 4421 4427                                                      
CONECT 4421 4420 4428                                                           
CONECT 4422 4423 4424 4429                                                      
CONECT 4423 4422                                                                
CONECT 4424 4417 4422                                                           
CONECT 4425 4418                                                                
CONECT 4426 4419 4430                                                           
CONECT 4427 4416 4420                                                           
CONECT 4428 4421                                                                
CONECT 4429 4422                                                                
CONECT 4430 4426 4431 4441                                                      
CONECT 4431 4430 4432 4438                                                      
CONECT 4432 4431 4433 4439                                                      
CONECT 4433 4432 4434 4440                                                      
CONECT 4434 4433 4435 4441                                                      
CONECT 4435 4434 4442                                                           
CONECT 4436 4437 4438 4443                                                      
CONECT 4437 4436                                                                
CONECT 4438 4431 4436                                                           
CONECT 4439 4432                                                                
CONECT 4440 4433                                                                
CONECT 4441 4430 4434                                                           
CONECT 4442 4435                                                                
CONECT 4443 4436                                                                
CONECT 4444 2711 4445 4455                                                      
CONECT 4445 4444 4446 4452                                                      
CONECT 4446 4445 4447 4453                                                      
CONECT 4447 4446 4448 4454                                                      
CONECT 4448 4447 4449 4455                                                      
CONECT 4449 4448 4456                                                           
CONECT 4450 4451 4452 4457                                                      
CONECT 4451 4450                                                                
CONECT 4452 4445 4450                                                           
CONECT 4453 4446                                                                
CONECT 4454 4447 4458                                                           
CONECT 4455 4444 4448                                                           
CONECT 4456 4449                                                                
CONECT 4457 4450                                                                
CONECT 4458 4454 4459 4469                                                      
CONECT 4459 4458 4460 4466                                                      
CONECT 4460 4459 4461 4467                                                      
CONECT 4461 4460 4462 4468                                                      
CONECT 4462 4461 4463 4469                                                      
CONECT 4463 4462 4470                                                           
CONECT 4464 4465 4466 4471                                                      
CONECT 4465 4464                                                                
CONECT 4466 4459 4464                                                           
CONECT 4467 4460                                                                
CONECT 4468 4461                                                                
CONECT 4469 4458 4462                                                           
CONECT 4470 4463                                                                
CONECT 4471 4464                                                                
CONECT 4472  257  288  290 4554                                                 
CONECT 4472 4617 4646                                                           
CONECT 4473  223  224  263  264                                                 
CONECT 4473 4561                                                                
CONECT 4474  234  235  265 4588                                                 
CONECT 4474 4800 4946                                                           
CONECT 4475  143  145  235  236                                                 
CONECT 4475 4552 4586                                                           
CONECT 4476  180  182 4543 4596                                                 
CONECT 4476 4756 4928                                                           
CONECT 4477  120  122  167  169                                                 
CONECT 4477 4612 4824                                                           
CONECT 4478  635 4479 4489                                                      
CONECT 4479 4478 4480 4486                                                      
CONECT 4480 4479 4481 4487                                                      
CONECT 4481 4480 4482 4488                                                      
CONECT 4482 4481 4483 4489                                                      
CONECT 4483 4482 4490                                                           
CONECT 4484 4485 4486 4491                                                      
CONECT 4485 4484                                                                
CONECT 4486 4479 4484                                                           
CONECT 4487 4480                                                                
CONECT 4488 4481                                                                
CONECT 4489 4478 4482                                                           
CONECT 4490 4483                                                                
CONECT 4491 4484                                                                
CONECT 4492 4493 4494 4495 4496                                                 
CONECT 4493 4492                                                                
CONECT 4494 4492                                                                
CONECT 4495 4492                                                                
CONECT 4496 4492                                                                
CONECT 4497 4498 4499 4500 4501                                                 
CONECT 4498 4497                                                                
CONECT 4499 4497                                                                
CONECT 4500 4497                                                                
CONECT 4501 4497                                                                
CONECT 4502 4503 4504 4505 4506                                                 
CONECT 4503 4502                                                                
CONECT 4504 4502                                                                
CONECT 4505 4502                                                                
CONECT 4506 4502                                                                
CONECT 4507 4508 4509 4510 4511                                                 
CONECT 4508 4507                                                                
CONECT 4509 4507                                                                
CONECT 4510 4507                                                                
CONECT 4511 4507                                                                
CONECT 4512 4513 4514 4515 4516                                                 
CONECT 4513 4512                                                                
CONECT 4514 4512                                                                
CONECT 4515 4512                                                                
CONECT 4516 4512                                                                
CONECT 4517 4518 4519 4520 4521                                                 
CONECT 4518 4517                                                                
CONECT 4519 4517                                                                
CONECT 4520 4517                                                                
CONECT 4521 4517                                                                
CONECT 4522 4523 4524 4525 4526                                                 
CONECT 4523 4522                                                                
CONECT 4524 4522                                                                
CONECT 4525 4522                                                                
CONECT 4526 4522                                                                
CONECT 4527 4528 4529 4530 4531                                                 
CONECT 4528 4527                                                                
CONECT 4529 4527                                                                
CONECT 4530 4527                                                                
CONECT 4531 4527                                                                
CONECT 4532 4533 4534                                                           
CONECT 4533 4532                                                                
CONECT 4534 4532 4535 4536                                                      
CONECT 4535 4534                                                                
CONECT 4536 4534 4537                                                           
CONECT 4537 4536                                                                
CONECT 4538 4539 4540 4541 4542                                                 
CONECT 4539 4538                                                                
CONECT 4540 4538                                                                
CONECT 4541 4538                                                                
CONECT 4542 4538                                                                
CONECT 4543 4476                                                                
CONECT 4552 4475                                                                
CONECT 4554 4472                                                                
CONECT 4561 4473                                                                
CONECT 4586 4475                                                                
CONECT 4588 4474                                                                
CONECT 4596 4476                                                                
CONECT 4612 4477                                                                
CONECT 4617 4472                                                                
CONECT 4646 4472                                                                
CONECT 4756 4476                                                                
CONECT 4800 4474                                                                
CONECT 4824 4477                                                                
CONECT 4928 4476                                                                
CONECT 4946 4474                                                                
MASTER      638    0   31   19   20    0    0    6 5005    1  309   44          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.