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Database: PDB
Entry: 3O78
LinkDB: 3O78
Original site: 3O78 
HEADER    FLUORESCENT PROTEIN                     30-JUL-10   3O78              
TITLE     THE STRUCTURE OF CA2+ SENSOR (CASE-12)                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MYOSIN LIGHT CHAIN KINASE, SMOOTH MUSCLE,GREEN FLUORESCENT 
COMPND   3 PROTEIN,GREEN FLUORESCENT PROTEIN,CALMODULIN-1;                      
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 SYNONYM: MLCK,TELOKIN;                                               
COMPND   6 EC: 2.7.11.18;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 OTHER_DETAILS: CHIMERA PROTEIN OF PEPTIDE OF M13 (RESIDUES 1730-1749,
COMPND  10 UNP P11799), C-TERMINAL DOMAIN OF GREEN FLUORESCENT PROTEIN (RESIDUES
COMPND  11 147-238, UNP P42212), LINKER, N-TERMINAL OF GREEN FLUORESCENT PROTEIN
COMPND  12 (RESIDUES 2-146, UNP P42212) AND RESIDUES 3-149 OF CALMODULIN (UNP   
COMPND  13 P0DP23)                                                              
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GALLUS GALLUS, AEQUOREA VICTORIA, HOMO SAPIENS; 
SOURCE   3 ORGANISM_COMMON: CHICKEN, JELLYFISH, HUMAN;                          
SOURCE   4 ORGANISM_TAXID: 9031, 6100, 9606;                                    
SOURCE   5 GENE: MYLK, GFP, CALM1, CALM, CAM, CAM1;                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) TUNER;                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET41                                     
KEYWDS    CIRCULAR PERMUTATED GREEN FLUORESCENT PROTEIN, GENETICALLY ENCODED,   
KEYWDS   2 GFP CALMODULIN M13-PEPTIDE, CALCIUM SENSOR, M13-PEPTIDE, GYG         
KEYWDS   3 NATURALLY MODIFIED TRIPEPTIDE ACTS AS CHROMOPHORE, FLUORESCENT       
KEYWDS   4 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.LEDER,W.STARK,F.FREULER,M.MARSH,M.MEYERHOFER,T.STETTLER,L.M.MAYR,   
AUTHOR   2 O.V.BRITANOVA,L.A.STRUKOVA,D.M.CHUDAKOV                              
REVDAT   6   06-DEC-23 3O78    1       REMARK                                   
REVDAT   5   01-NOV-23 3O78    1       REMARK LINK                              
REVDAT   4   21-JUN-17 3O78    1       COMPND SOURCE                            
REVDAT   3   13-JUN-12 3O78    1       SEQADV                                   
REVDAT   2   25-APR-12 3O78    1       JRNL   VERSN                             
REVDAT   1   29-SEP-10 3O78    0                                                
JRNL        AUTH   L.LEDER,W.STARK,F.FREULER,M.MARSH,M.MEYERHOFER,T.STETTLER,   
JRNL        AUTH 2 L.M.MAYR,O.V.BRITANOVA,L.A.STRUKOVA,D.M.CHUDAKOV,            
JRNL        AUTH 3 E.A.SOUSLOVA                                                 
JRNL        TITL   THE STRUCTURE OF CA2+ SENSOR CASE16 REVEALS THE MECHANISM OF 
JRNL        TITL 2 REACTION TO LOW CA2+ CONCENTRATIONS                          
JRNL        REF    SENSORS (BASEL)               V.  10  8143 2010              
JRNL        REFN                   ESSN 1424-8220                               
JRNL        PMID   22163646                                                     
JRNL        DOI    10.3390/S100908143                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.83                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 22288                          
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) : 0.245                           
REMARK   3   R VALUE            (WORKING SET) : 0.242                           
REMARK   3   FREE R VALUE                     : 0.316                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1173                            
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1627                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.77                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3400                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 85                           
REMARK   3   BIN FREE R VALUE                    : 0.4530                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6338                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 77                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 41.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.43                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.01000                                             
REMARK   3    B22 (A**2) : 0.32000                                              
REMARK   3    B33 (A**2) : 0.69000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.06000                                              
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): 0.450         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.376         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.100        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.904                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.840                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6445 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8674 ; 1.726 ; 1.968       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   795 ; 8.346 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   322 ;35.786 ;25.280       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1163 ;21.239 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    34 ;20.667 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   935 ; 0.106 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4908 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3511 ; 0.268 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4392 ; 0.319 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   352 ; 0.205 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    25 ; 0.178 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    88 ; 0.328 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.372 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 3                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     25       A     270      1                      
REMARK   3           1     B     25       B     270      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1793 ;  0.07 ;  0.05           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    271       A     340      1                      
REMARK   3           1     B    271       B     340      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    A    (A):    542 ;  0.07 ;  0.05           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    341       A     411      1                      
REMARK   3           1     B    341       B     411      1                      
REMARK   3           2     A      1       A      24      1                      
REMARK   3           2     B      1       B      24      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    A    (A):    754 ;  0.09 ;  0.05           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3O78 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-AUG-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000060752.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-AUG-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 5.5                                
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 FR-E SUPERBRIGHT            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54179                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23464                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.71                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.51700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3O77                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR: 100MM TRIS HCL (PH 5.5),      
REMARK 280  100MM (NH4)2SO4, 21% PEG 3350; PROTEIN STOCK: 7.6 MG/ML PROTEIN,    
REMARK 280  50MM TRIS HCL (PH 7.4), 150MM NACL; SEED STOCK SOLUTION: 20MM       
REMARK 280  CACL2, 20% PEG 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       50.81750            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7390 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 34860 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   110                                                      
REMARK 465     MET A   111                                                      
REMARK 465     ASP A   112                                                      
REMARK 465     GLU A   113                                                      
REMARK 465     LEU A   114                                                      
REMARK 465     TYR A   115                                                      
REMARK 465     ASN A   116                                                      
REMARK 465     VAL A   117                                                      
REMARK 465     ASP A   118                                                      
REMARK 465     GLY A   119                                                      
REMARK 465     GLY A   120                                                      
REMARK 465     SER A   121                                                      
REMARK 465     ASP B   112                                                      
REMARK 465     GLU B   113                                                      
REMARK 465     LEU B   114                                                      
REMARK 465     TYR B   115                                                      
REMARK 465     ASN B   116                                                      
REMARK 465     VAL B   117                                                      
REMARK 465     ASP B   118                                                      
REMARK 465     GLY B   119                                                      
REMARK 465     GLY B   120                                                      
REMARK 465     SER B   121                                                      
REMARK 465     GLY B   122                                                      
REMARK 465     GLY B   123                                                      
REMARK 465     THR B   124                                                      
REMARK 465     GLY B   125                                                      
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     ILE A 107    CG1  CG2  CD1                                       
REMARK 470     THR A 108    OG1  CG2                                            
REMARK 470     LEU A 109    CG   CD1  CD2                                       
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   NH1  ARG A     6     OE2  GLU B   396              1.80            
REMARK 500   OE1  GLU A   141     NH1  ARG A   246              2.11            
REMARK 500   OE1  GLN A    61     NH2  ARG A   220              2.12            
REMARK 500   OE1  GLN B   272     O    HOH B   419              2.15            
REMARK 500   N    VAL A    71     O    HOH A   447              2.15            
REMARK 500   OE1  GLU B   141     NH1  ARG B   246              2.19            
REMARK 500   N    GLY A     1     O    LYS B   384              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OD1  ASN B    37     OE1  GLU B    50     1455     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    TRP A   9   CB    TRP A   9   CG     -0.111                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 270   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG A 270   NE  -  CZ  -  NH2 ANGL. DEV. =   5.1 DEGREES          
REMARK 500    ARG A 395   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 395   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG B 270   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 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    LYS A  34      -34.01    -34.97                                   
REMARK 500    ASN A  37       46.97     33.44                                   
REMARK 500    ASP A  51       33.46    -97.62                                   
REMARK 500    SER A  53     -166.62    -64.78                                   
REMARK 500    VAL A  71      143.39     58.80                                   
REMARK 500    THR A 124      -94.74    105.91                                   
REMARK 500    THR A 133      -41.00    -29.69                                   
REMARK 500    LYS A 203        0.14    -67.02                                   
REMARK 500    ASP A 226       13.24     59.00                                   
REMARK 500    GLU A 256        1.19    -61.55                                   
REMARK 500    ASP A 257       12.30   -143.81                                   
REMARK 500    ASN A 268      150.64     71.49                                   
REMARK 500    ASP A 289       66.02    -69.53                                   
REMARK 500    ALA A 326      -67.72    -28.40                                   
REMARK 500    ASP A 347        1.36    -47.93                                   
REMARK 500    ASP A 398       68.71    -66.04                                   
REMARK 500    ASP A 400        3.78    -64.74                                   
REMARK 500    SER B   4      156.16    118.61                                   
REMARK 500    SER B   5      119.10    -34.12                                   
REMARK 500    ARG B   6     -164.41    102.77                                   
REMARK 500    ARG B   7      -15.42     66.10                                   
REMARK 500    GLN B  35       25.16    -67.75                                   
REMARK 500    LYS B  36       21.53   -165.55                                   
REMARK 500    ASN B  37       46.65     36.51                                   
REMARK 500    ASP B  51        9.95    -65.61                                   
REMARK 500    VAL B  71      155.35     -0.05                                   
REMARK 500    LEU B 109      101.54    108.62                                   
REMARK 500    LYS B 203        6.51    -66.81                                   
REMARK 500    GLU B 256       -2.76    -57.78                                   
REMARK 500    LYS B 264        0.26    -68.22                                   
REMARK 500    ASN B 268      151.72     68.75                                   
REMARK 500    ASP B 347       -2.92    -53.02                                   
REMARK 500    ASP B 398       68.01    -67.30                                   
REMARK 500    ASP B 400        6.29    -62.38                                   
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 MET A  212     PRO A  213                   95.64                    
REMARK 500 THR A  415     ALA A  416                  147.16                    
REMARK 500 MET B  212     PRO B  213                  108.05                    
REMARK 500 ASN B  268     THR B  269                  146.82                    
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 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 289   OD1                                                    
REMARK 620 2 ASP A 291   OD1  79.7                                              
REMARK 620 3 ASP A 293   OD1  67.5  85.3                                        
REMARK 620 4 THR A 295   O    58.7 136.7  68.9                                  
REMARK 620 5 GLU A 300   OE1  94.0 122.4 144.5  75.6                            
REMARK 620 6 GLU A 300   OE2  93.3  73.2 153.7 117.4  49.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 325   OD2                                                    
REMARK 620 2 ASP A 327   OD1  63.9                                              
REMARK 620 3 ASN A 329   OD1  76.0  63.7                                        
REMARK 620 4 THR A 331   O    80.9 133.1  79.1                                  
REMARK 620 5 GLU A 336   OE1  80.5  84.8 146.6 120.3                            
REMARK 620 6 GLU A 336   OE2  91.1 131.4 153.1  75.6  48.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 362   OD2                                                    
REMARK 620 2 ASP A 364   OD2  75.1                                              
REMARK 620 3 ASN A 366   OD1  90.8  90.0                                        
REMARK 620 4 TYR A 368   O    97.3 171.2  85.8                                  
REMARK 620 5 GLU A 373   OE2 113.6 111.6 150.4  75.1                            
REMARK 620 6 GLU A 373   OE1  83.7  66.3 156.3 117.8  49.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 398   OD1                                                    
REMARK 620 2 ASP A 400   OD2  95.7                                              
REMARK 620 3 ASP A 402   OD1  89.9  87.0                                        
REMARK 620 4 GLN A 404   O    97.0 153.8  70.3                                  
REMARK 620 5 GLU A 409   OE2 125.3 102.8 141.4  88.2                            
REMARK 620 6 GLU A 409   OE1 104.7  62.9 147.3 134.3  46.5                      
REMARK 620 7 HOH A 448   O   151.2  60.2  74.3  99.9  78.6  79.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 289   OD1                                                    
REMARK 620 2 ASP B 291   OD1  80.3                                              
REMARK 620 3 ASP B 293   OD1  68.1  84.7                                        
REMARK 620 4 THR B 295   O    70.2 146.5  70.0                                  
REMARK 620 5 GLU B 300   OE1 103.6 121.6 151.7  81.7                            
REMARK 620 6 GLU B 300   OE2 102.3  68.5 152.9 132.3  53.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 325   OD2                                                    
REMARK 620 2 ASP B 327   OD1  66.4                                              
REMARK 620 3 ASN B 329   OD1  70.3  58.7                                        
REMARK 620 4 THR B 331   O    86.7 128.2  71.1                                  
REMARK 620 5 GLU B 336   OE1  89.6  89.9 147.2 135.2                            
REMARK 620 6 GLU B 336   OE2 103.6 144.8 152.8  82.2  55.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 362   OD2                                                    
REMARK 620 2 ASP B 364   OD2  77.5                                              
REMARK 620 3 ASN B 366   OD1  81.7  77.5                                        
REMARK 620 4 TYR B 368   O    91.8 151.0  74.3                                  
REMARK 620 5 GLU B 373   OE1  92.3  73.3 150.8 134.7                            
REMARK 620 6 GLU B 373   OE2 119.3 128.3 147.8  80.5  58.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 398   OD1                                                    
REMARK 620 2 ASP B 400   OD2  92.6                                              
REMARK 620 3 ASP B 402   OD1  84.6  94.6                                        
REMARK 620 4 GLN B 404   O    85.5 163.6  69.0                                  
REMARK 620 5 GLU B 409   OE2 114.5 112.3 145.2  83.1                            
REMARK 620 6 GLU B 409   OE1 105.2  62.1 154.6 134.1  51.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 504                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3O77   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EK4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EK7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EK8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EKH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EKJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EVP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EVR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EVU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EVV   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 UNP RESIDUE 65 SER AND 72 SER OF GREEN FLUORESCENT PROTEIN IN        
REMARK 999 DATABASE UNP P42212 (GFP_AEQVI) SHOULD BE GLY. RESIDUE S65G FORM     
REMARK 999 THE CHROMOPHORE CR2 190. RESIDUE S72G (RESIDUE NUMBER 196 IN THE     
REMARK 999 COORDINATES RESPECTIVELY) IS MUTAGENESIS. THESE SEQUENCE WERE BASED  
REMARK 999 ON REFERENCES IN THE DATABASE UNP P42212.                            
DBREF  3O78 A    5    24  UNP    P11799   MYLK_CHICK    1730   1749             
DBREF  3O78 A   25   116  UNP    P42212   GFP_AEQVI      147    238             
DBREF  3O78 A  126   270  UNP    P42212   GFP_AEQVI        2    146             
DBREF  3O78 A  271   417  UNP    P0DP23   CALM1_HUMAN      3    149             
DBREF  3O78 B    5    24  UNP    P11799   MYLK_CHICK    1730   1749             
DBREF  3O78 B   25   116  UNP    P42212   GFP_AEQVI      147    238             
DBREF  3O78 B  126   270  UNP    P42212   GFP_AEQVI        2    146             
DBREF  3O78 B  271   417  UNP    P0DP23   CALM1_HUMAN      3    149             
SEQADV 3O78 GLY A    1  UNP  P11799              EXPRESSION TAG                 
SEQADV 3O78 PRO A    2  UNP  P11799              EXPRESSION TAG                 
SEQADV 3O78 GLY A    3  UNP  P11799              EXPRESSION TAG                 
SEQADV 3O78 SER A    4  UNP  P11799              EXPRESSION TAG                 
SEQADV 3O78 SER A    5  UNP  P11799    ALA  1730 ENGINEERED MUTATION            
SEQADV 3O78 ASN A   10  UNP  P11799    GLN  1735 ENGINEERED MUTATION            
SEQADV 3O78 LEU A   25  UNP  P42212    SER   147 ENGINEERED MUTATION            
SEQADV 3O78 GLU A   26  UNP  P42212    HIS   148 ENGINEERED MUTATION            
SEQADV 3O78 ALA A   41  UNP  P42212    VAL   163 ENGINEERED MUTATION            
SEQADV 3O78 VAL A   49  UNP  P42212    ILE   171 ENGINEERED MUTATION            
SEQADV 3O78 PHE A   81  UNP  P42212    THR   203 ENGINEERED MUTATION            
SEQADV 3O78 VAL A   84  UNP  P42212    ALA   206 ENGINEERED MUTATION            
SEQADV 3O78 LEU A  109  UNP  P42212    HIS   231 ENGINEERED MUTATION            
SEQADV 3O78 ASN A  116  UNP  P42212    LYS   238 ENGINEERED MUTATION            
SEQADV 3O78 VAL A  117  UNP  P42212              LINKER                         
SEQADV 3O78 ASP A  118  UNP  P42212              LINKER                         
SEQADV 3O78 GLY A  119  UNP  P42212              LINKER                         
SEQADV 3O78 GLY A  120  UNP  P42212              LINKER                         
SEQADV 3O78 SER A  121  UNP  P42212              LINKER                         
SEQADV 3O78 GLY A  122  UNP  P42212              LINKER                         
SEQADV 3O78 GLY A  123  UNP  P42212              LINKER                         
SEQADV 3O78 THR A  124  UNP  P42212              LINKER                         
SEQADV 3O78 GLY A  125  UNP  P42212              LINKER                         
SEQADV 3O78 LEU A  170  UNP  P42212    PHE    46 ENGINEERED MUTATION            
SEQADV 3O78 LEU A  188  UNP  P42212    PHE    64 ENGINEERED MUTATION            
SEQADV 3O78 CR2 A  190  UNP  P42212    SER    65 CHROMOPHORE                    
SEQADV 3O78 CR2 A  190  UNP  P42212    TYR    66 CHROMOPHORE                    
SEQADV 3O78 CR2 A  190  UNP  P42212    GLY    67 CHROMOPHORE                    
SEQADV 3O78 LEU A  192  UNP  P42212    VAL    68 ENGINEERED MUTATION            
SEQADV 3O78 LYS A  193  UNP  P42212    GLN    69 ENGINEERED MUTATION            
SEQADV 3O78 ALA A  196  UNP  P42212    SER    72 SEE SEQUENCE DETAILS           
SEQADV 3O78 GLY A  253  UNP  P42212    ASP   129 ENGINEERED MUTATION            
SEQADV 3O78 THR A  269  UNP  P42212    TYR   145 ENGINEERED MUTATION            
SEQADV 3O78 ARG A  270  UNP  P42212    ASN   146 ENGINEERED MUTATION            
SEQADV 3O78 GLY B    1  UNP  P11799              EXPRESSION TAG                 
SEQADV 3O78 PRO B    2  UNP  P11799              EXPRESSION TAG                 
SEQADV 3O78 GLY B    3  UNP  P11799              EXPRESSION TAG                 
SEQADV 3O78 SER B    4  UNP  P11799              EXPRESSION TAG                 
SEQADV 3O78 SER B    5  UNP  P11799    ALA  1730 ENGINEERED MUTATION            
SEQADV 3O78 ASN B   10  UNP  P11799    GLN  1735 ENGINEERED MUTATION            
SEQADV 3O78 LEU B   25  UNP  P42212    SER   147 ENGINEERED MUTATION            
SEQADV 3O78 GLU B   26  UNP  P42212    HIS   148 ENGINEERED MUTATION            
SEQADV 3O78 ALA B   41  UNP  P42212    VAL   163 ENGINEERED MUTATION            
SEQADV 3O78 VAL B   49  UNP  P42212    ILE   171 ENGINEERED MUTATION            
SEQADV 3O78 PHE B   81  UNP  P42212    THR   203 ENGINEERED MUTATION            
SEQADV 3O78 VAL B   84  UNP  P42212    ALA   206 ENGINEERED MUTATION            
SEQADV 3O78 LEU B  109  UNP  P42212    HIS   231 ENGINEERED MUTATION            
SEQADV 3O78 ASN B  116  UNP  P42212    LYS   238 ENGINEERED MUTATION            
SEQADV 3O78 VAL B  117  UNP  P42212              LINKER                         
SEQADV 3O78 ASP B  118  UNP  P42212              LINKER                         
SEQADV 3O78 GLY B  119  UNP  P42212              LINKER                         
SEQADV 3O78 GLY B  120  UNP  P42212              LINKER                         
SEQADV 3O78 SER B  121  UNP  P42212              LINKER                         
SEQADV 3O78 GLY B  122  UNP  P42212              LINKER                         
SEQADV 3O78 GLY B  123  UNP  P42212              LINKER                         
SEQADV 3O78 THR B  124  UNP  P42212              LINKER                         
SEQADV 3O78 GLY B  125  UNP  P42212              LINKER                         
SEQADV 3O78 LEU B  170  UNP  P42212    PHE    46 ENGINEERED MUTATION            
SEQADV 3O78 LEU B  188  UNP  P42212    PHE    64 ENGINEERED MUTATION            
SEQADV 3O78 CR2 B  190  UNP  P42212    SER    65 CHROMOPHORE                    
SEQADV 3O78 CR2 B  190  UNP  P42212    TYR    66 CHROMOPHORE                    
SEQADV 3O78 CR2 B  190  UNP  P42212    GLY    67 CHROMOPHORE                    
SEQADV 3O78 LEU B  192  UNP  P42212    VAL    68 ENGINEERED MUTATION            
SEQADV 3O78 LYS B  193  UNP  P42212    GLN    69 ENGINEERED MUTATION            
SEQADV 3O78 ALA B  196  UNP  P42212    SER    72 SEE SEQUENCE DETAILS           
SEQADV 3O78 GLY B  253  UNP  P42212    ASP   129 ENGINEERED MUTATION            
SEQADV 3O78 THR B  269  UNP  P42212    TYR   145 ENGINEERED MUTATION            
SEQADV 3O78 ARG B  270  UNP  P42212    ASN   146 ENGINEERED MUTATION            
SEQRES   1 A  415  GLY PRO GLY SER SER ARG ARG LYS TRP ASN LYS THR GLY          
SEQRES   2 A  415  HIS ALA VAL ARG ALA ILE GLY ARG LEU SER SER LEU GLU          
SEQRES   3 A  415  ASN VAL TYR ILE MET ALA ASP LYS GLN LYS ASN GLY ILE          
SEQRES   4 A  415  LYS ALA ASN PHE LYS ILE ARG HIS ASN VAL GLU ASP GLY          
SEQRES   5 A  415  SER VAL GLN LEU ALA ASP HIS TYR GLN GLN ASN THR PRO          
SEQRES   6 A  415  ILE GLY ASP GLY PRO VAL LEU LEU PRO ASP ASN HIS TYR          
SEQRES   7 A  415  LEU SER PHE GLN SER VAL LEU SER LYS ASP PRO ASN GLU          
SEQRES   8 A  415  LYS ARG ASP HIS MET VAL LEU LEU GLU PHE VAL THR ALA          
SEQRES   9 A  415  ALA GLY ILE THR LEU GLY MET ASP GLU LEU TYR ASN VAL          
SEQRES  10 A  415  ASP GLY GLY SER GLY GLY THR GLY SER LYS GLY GLU GLU          
SEQRES  11 A  415  LEU PHE THR GLY VAL VAL PRO ILE LEU VAL GLU LEU ASP          
SEQRES  12 A  415  GLY ASP VAL ASN GLY HIS LYS PHE SER VAL SER GLY GLU          
SEQRES  13 A  415  GLY GLU GLY ASP ALA THR TYR GLY LYS LEU THR LEU LYS          
SEQRES  14 A  415  LEU ILE CYS THR THR GLY LYS LEU PRO VAL PRO TRP PRO          
SEQRES  15 A  415  THR LEU VAL THR THR LEU CR2 LEU LYS CYS PHE ALA ARG          
SEQRES  16 A  415  TYR PRO ASP HIS MET LYS GLN HIS ASP PHE PHE LYS SER          
SEQRES  17 A  415  ALA MET PRO GLU GLY TYR VAL GLN GLU ARG THR ILE PHE          
SEQRES  18 A  415  PHE LYS ASP ASP GLY ASN TYR LYS THR ARG ALA GLU VAL          
SEQRES  19 A  415  LYS PHE GLU GLY ASP THR LEU VAL ASN ARG ILE GLU LEU          
SEQRES  20 A  415  LYS GLY ILE GLY PHE LYS GLU ASP GLY ASN ILE LEU GLY          
SEQRES  21 A  415  HIS LYS LEU GLU TYR ASN THR ARG ASP GLN LEU THR GLU          
SEQRES  22 A  415  GLU GLN ILE ALA GLU PHE LYS GLU ALA PHE SER LEU PHE          
SEQRES  23 A  415  ASP LYS ASP GLY ASP GLY THR ILE THR THR LYS GLU LEU          
SEQRES  24 A  415  GLY THR VAL MET ARG SER LEU GLY GLN ASN PRO THR GLU          
SEQRES  25 A  415  ALA GLU LEU GLN ASP MET ILE ASN GLU VAL ASP ALA ASP          
SEQRES  26 A  415  GLY ASN GLY THR ILE ASP PHE PRO GLU PHE LEU THR MET          
SEQRES  27 A  415  MET ALA ARG LYS MET LYS ASP THR ASP SER GLU GLU GLU          
SEQRES  28 A  415  ILE ARG GLU ALA PHE ARG VAL PHE ASP LYS ASP GLY ASN          
SEQRES  29 A  415  GLY TYR ILE SER ALA ALA GLU LEU ARG HIS VAL MET THR          
SEQRES  30 A  415  ASN LEU GLY GLU LYS LEU THR ASP GLU GLU VAL ASP GLU          
SEQRES  31 A  415  MET ILE ARG GLU ALA ASP ILE ASP GLY ASP GLY GLN VAL          
SEQRES  32 A  415  ASN TYR GLU GLU PHE VAL GLN MET MET THR ALA LYS              
SEQRES   1 B  415  GLY PRO GLY SER SER ARG ARG LYS TRP ASN LYS THR GLY          
SEQRES   2 B  415  HIS ALA VAL ARG ALA ILE GLY ARG LEU SER SER LEU GLU          
SEQRES   3 B  415  ASN VAL TYR ILE MET ALA ASP LYS GLN LYS ASN GLY ILE          
SEQRES   4 B  415  LYS ALA ASN PHE LYS ILE ARG HIS ASN VAL GLU ASP GLY          
SEQRES   5 B  415  SER VAL GLN LEU ALA ASP HIS TYR GLN GLN ASN THR PRO          
SEQRES   6 B  415  ILE GLY ASP GLY PRO VAL LEU LEU PRO ASP ASN HIS TYR          
SEQRES   7 B  415  LEU SER PHE GLN SER VAL LEU SER LYS ASP PRO ASN GLU          
SEQRES   8 B  415  LYS ARG ASP HIS MET VAL LEU LEU GLU PHE VAL THR ALA          
SEQRES   9 B  415  ALA GLY ILE THR LEU GLY MET ASP GLU LEU TYR ASN VAL          
SEQRES  10 B  415  ASP GLY GLY SER GLY GLY THR GLY SER LYS GLY GLU GLU          
SEQRES  11 B  415  LEU PHE THR GLY VAL VAL PRO ILE LEU VAL GLU LEU ASP          
SEQRES  12 B  415  GLY ASP VAL ASN GLY HIS LYS PHE SER VAL SER GLY GLU          
SEQRES  13 B  415  GLY GLU GLY ASP ALA THR TYR GLY LYS LEU THR LEU LYS          
SEQRES  14 B  415  LEU ILE CYS THR THR GLY LYS LEU PRO VAL PRO TRP PRO          
SEQRES  15 B  415  THR LEU VAL THR THR LEU CR2 LEU LYS CYS PHE ALA ARG          
SEQRES  16 B  415  TYR PRO ASP HIS MET LYS GLN HIS ASP PHE PHE LYS SER          
SEQRES  17 B  415  ALA MET PRO GLU GLY TYR VAL GLN GLU ARG THR ILE PHE          
SEQRES  18 B  415  PHE LYS ASP ASP GLY ASN TYR LYS THR ARG ALA GLU VAL          
SEQRES  19 B  415  LYS PHE GLU GLY ASP THR LEU VAL ASN ARG ILE GLU LEU          
SEQRES  20 B  415  LYS GLY ILE GLY PHE LYS GLU ASP GLY ASN ILE LEU GLY          
SEQRES  21 B  415  HIS LYS LEU GLU TYR ASN THR ARG ASP GLN LEU THR GLU          
SEQRES  22 B  415  GLU GLN ILE ALA GLU PHE LYS GLU ALA PHE SER LEU PHE          
SEQRES  23 B  415  ASP LYS ASP GLY ASP GLY THR ILE THR THR LYS GLU LEU          
SEQRES  24 B  415  GLY THR VAL MET ARG SER LEU GLY GLN ASN PRO THR GLU          
SEQRES  25 B  415  ALA GLU LEU GLN ASP MET ILE ASN GLU VAL ASP ALA ASP          
SEQRES  26 B  415  GLY ASN GLY THR ILE ASP PHE PRO GLU PHE LEU THR MET          
SEQRES  27 B  415  MET ALA ARG LYS MET LYS ASP THR ASP SER GLU GLU GLU          
SEQRES  28 B  415  ILE ARG GLU ALA PHE ARG VAL PHE ASP LYS ASP GLY ASN          
SEQRES  29 B  415  GLY TYR ILE SER ALA ALA GLU LEU ARG HIS VAL MET THR          
SEQRES  30 B  415  ASN LEU GLY GLU LYS LEU THR ASP GLU GLU VAL ASP GLU          
SEQRES  31 B  415  MET ILE ARG GLU ALA ASP ILE ASP GLY ASP GLY GLN VAL          
SEQRES  32 B  415  ASN TYR GLU GLU PHE VAL GLN MET MET THR ALA LYS              
MODRES 3O78 CR2 A  190  SER  CHROMOPHORE                                        
MODRES 3O78 CR2 B  190  SER  CHROMOPHORE                                        
HET    CR2  A 190      19                                                       
HET    CR2  B 190      19                                                       
HET     CA  A 501       1                                                       
HET     CA  A 502       1                                                       
HET     CA  A 503       1                                                       
HET     CA  A 504       1                                                       
HET     CA  B 501       1                                                       
HET     CA  B 502       1                                                       
HET     CA  B 503       1                                                       
HET     CA  B 504       1                                                       
HETNAM     CR2 {(4Z)-2-(AMINOMETHYL)-4-[(4-HYDROXYPHENYL)METHYLIDENE]-          
HETNAM   2 CR2  5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC ACID                  
HETNAM      CA CALCIUM ION                                                      
HETSYN     CR2 CHROMOPHORE (GLY-TYR-GLY)                                        
FORMUL   1  CR2    2(C13 H13 N3 O4)                                             
FORMUL   3   CA    8(CA 2+)                                                     
FORMUL  11  HOH   *77(H2 O)                                                     
HELIX    1   1 SER A    4  SER A   23  1                                  20    
HELIX    2   2 LYS A   34  ASN A   37  5                                   4    
HELIX    3   3 LYS A  127  PHE A  132  5                                   6    
HELIX    4   4 ALA A  161  TYR A  163  5                                   3    
HELIX    5   5 PRO A  180  VAL A  185  5                                   6    
HELIX    6   6 LEU A  192  ALA A  196  5                                   5    
HELIX    7   7 PRO A  199  LYS A  203  5                                   5    
HELIX    8   8 ASP A  206  ALA A  211  1                                   6    
HELIX    9   9 THR A  274  ASP A  289  1                                  16    
HELIX   10  10 THR A  297  GLY A  309  1                                  13    
HELIX   11  11 THR A  313  GLU A  323  1                                  11    
HELIX   12  12 PHE A  334  ARG A  343  1                                  10    
HELIX   13  13 LYS A  346  ASP A  362  1                                  17    
HELIX   14  14 SER A  370  LEU A  381  1                                  12    
HELIX   15  15 THR A  386  ASP A  398  1                                  13    
HELIX   16  16 ASN A  406  THR A  415  1                                  10    
HELIX   17  17 ARG B    7  SER B   23  1                                  17    
HELIX   18  18 LYS B   34  ASN B   37  5                                   4    
HELIX   19  19 LYS B  127  THR B  133  5                                   7    
HELIX   20  20 ALA B  161  TYR B  163  5                                   3    
HELIX   21  21 PRO B  180  VAL B  185  5                                   6    
HELIX   22  22 LEU B  192  ALA B  196  5                                   5    
HELIX   23  23 PRO B  199  LYS B  203  5                                   5    
HELIX   24  24 ASP B  206  ALA B  211  1                                   6    
HELIX   25  25 THR B  274  ASP B  289  1                                  16    
HELIX   26  26 THR B  297  GLY B  309  1                                  13    
HELIX   27  27 THR B  313  GLU B  323  1                                  11    
HELIX   28  28 PHE B  334  ARG B  343  1                                  10    
HELIX   29  29 LYS B  346  ASP B  362  1                                  17    
HELIX   30  30 SER B  370  LEU B  381  1                                  12    
HELIX   31  31 THR B  386  ASP B  398  1                                  13    
HELIX   32  32 ASN B  406  THR B  415  1                                  10    
SHEET    1   A12 VAL A  28  ASP A  33  0                                        
SHEET    2   A12 GLY A  38  ASN A  48 -1  O  GLY A  38   N  ASP A  33           
SHEET    3   A12 VAL A  54  PRO A  65 -1  O  GLN A  55   N  HIS A  47           
SHEET    4   A12 TYR A 216  PHE A 224 -1  O  VAL A 217   N  THR A  64           
SHEET    5   A12 ASN A 229  GLU A 239 -1  O  VAL A 236   N  TYR A 216           
SHEET    6   A12 THR A 242  ILE A 252 -1  O  VAL A 244   N  LYS A 237           
SHEET    7   A12 VAL A 136  VAL A 146  1  N  ASP A 143   O  LEU A 249           
SHEET    8   A12 HIS A 149  ASP A 160 -1  O  GLY A 157   N  ILE A 138           
SHEET    9   A12 LYS A 165  CYS A 172 -1  O  ILE A 171   N  SER A 154           
SHEET   10   A12 HIS A  95  ALA A 105 -1  N  MET A  96   O  LEU A 170           
SHEET   11   A12 HIS A  77  SER A  86 -1  N  TYR A  78   O  ALA A 105           
SHEET   12   A12 VAL A  28  ASP A  33 -1  N  ILE A  30   O  HIS A  77           
SHEET    1   B 2 THR A 295  ILE A 296  0                                        
SHEET    2   B 2 ILE A 332  ASP A 333 -1  O  ILE A 332   N  ILE A 296           
SHEET    1   C12 VAL B  28  ASP B  33  0                                        
SHEET    2   C12 GLY B  38  ASN B  48 -1  O  GLY B  38   N  ASP B  33           
SHEET    3   C12 VAL B  54  PRO B  65 -1  O  GLN B  55   N  HIS B  47           
SHEET    4   C12 TYR B 216  PHE B 224 -1  O  VAL B 217   N  THR B  64           
SHEET    5   C12 ASN B 229  GLU B 239 -1  O  TYR B 230   N  ILE B 222           
SHEET    6   C12 THR B 242  ILE B 252 -1  O  ILE B 252   N  ASN B 229           
SHEET    7   C12 VAL B 136  VAL B 146  1  N  ASP B 143   O  LEU B 249           
SHEET    8   C12 HIS B 149  ASP B 160 -1  O  GLY B 157   N  ILE B 138           
SHEET    9   C12 LYS B 165  ILE B 171 -1  O  ILE B 171   N  SER B 154           
SHEET   10   C12 HIS B  95  ALA B 105 -1  N  LEU B  98   O  LEU B 168           
SHEET   11   C12 HIS B  77  SER B  86 -1  N  TYR B  78   O  ALA B 105           
SHEET   12   C12 VAL B  28  ASP B  33 -1  N  ILE B  30   O  HIS B  77           
SHEET    1   D 2 THR B 295  ILE B 296  0                                        
SHEET    2   D 2 ILE B 332  ASP B 333 -1  O  ILE B 332   N  ILE B 296           
LINK         C   LEU A 188                 N1  CR2 A 190     1555   1555  1.45  
LINK         C3  CR2 A 190                 N   LEU A 192     1555   1555  1.36  
LINK         C   LEU B 188                 N1  CR2 B 190     1555   1555  1.20  
LINK         C3  CR2 B 190                 N   LEU B 192     1555   1555  1.37  
LINK         OD1 ASP A 289                CA    CA A 501     1555   1555  2.50  
LINK         OD1 ASP A 291                CA    CA A 501     1555   1555  2.32  
LINK         OD1 ASP A 293                CA    CA A 501     1555   1555  2.29  
LINK         O   THR A 295                CA    CA A 501     1555   1555  2.90  
LINK         OE1 GLU A 300                CA    CA A 501     1555   1555  2.24  
LINK         OE2 GLU A 300                CA    CA A 501     1555   1555  2.81  
LINK         OD2 ASP A 325                CA    CA A 502     1555   1555  2.25  
LINK         OD1 ASP A 327                CA    CA A 502     1555   1555  2.77  
LINK         OD1 ASN A 329                CA    CA A 502     1555   1555  2.44  
LINK         O   THR A 331                CA    CA A 502     1555   1555  2.32  
LINK         OE1 GLU A 336                CA    CA A 502     1555   1555  2.65  
LINK         OE2 GLU A 336                CA    CA A 502     1555   1555  2.70  
LINK         OD2 ASP A 362                CA    CA A 503     1555   1555  2.55  
LINK         OD2 ASP A 364                CA    CA A 503     1555   1555  2.21  
LINK         OD1 ASN A 366                CA    CA A 503     1555   1555  2.18  
LINK         O   TYR A 368                CA    CA A 503     1555   1555  2.14  
LINK         OE2 GLU A 373                CA    CA A 503     1555   1555  2.55  
LINK         OE1 GLU A 373                CA    CA A 503     1555   1555  2.67  
LINK         OD1 ASP A 398                CA    CA A 504     1555   1555  2.12  
LINK         OD2 ASP A 400                CA    CA A 504     1555   1555  2.74  
LINK         OD1 ASP A 402                CA    CA A 504     1555   1555  2.53  
LINK         O   GLN A 404                CA    CA A 504     1555   1555  2.23  
LINK         OE2 GLU A 409                CA    CA A 504     1555   1555  2.60  
LINK         OE1 GLU A 409                CA    CA A 504     1555   1555  2.90  
LINK         O   HOH A 448                CA    CA A 504     1555   1555  2.54  
LINK         OD1 ASP B 289                CA    CA B 501     1555   1555  2.29  
LINK         OD1 ASP B 291                CA    CA B 501     1555   1555  2.39  
LINK         OD1 ASP B 293                CA    CA B 501     1555   1555  2.42  
LINK         O   THR B 295                CA    CA B 501     1555   1555  2.58  
LINK         OE1 GLU B 300                CA    CA B 501     1555   1555  2.08  
LINK         OE2 GLU B 300                CA    CA B 501     1555   1555  2.61  
LINK         OD2 ASP B 325                CA    CA B 502     1555   1555  2.15  
LINK         OD1 ASP B 327                CA    CA B 502     1555   1555  2.70  
LINK         OD1 ASN B 329                CA    CA B 502     1555   1555  2.66  
LINK         O   THR B 331                CA    CA B 502     1555   1555  2.35  
LINK         OE1 GLU B 336                CA    CA B 502     1555   1555  2.35  
LINK         OE2 GLU B 336                CA    CA B 502     1555   1555  2.39  
LINK         OD2 ASP B 362                CA    CA B 503     1555   1555  2.50  
LINK         OD2 ASP B 364                CA    CA B 503     1555   1555  2.33  
LINK         OD1 ASN B 366                CA    CA B 503     1555   1555  2.66  
LINK         O   TYR B 368                CA    CA B 503     1555   1555  2.19  
LINK         OE1 GLU B 373                CA    CA B 503     1555   1555  2.20  
LINK         OE2 GLU B 373                CA    CA B 503     1555   1555  2.24  
LINK         OD1 ASP B 398                CA    CA B 504     1555   1555  2.30  
LINK         OD2 ASP B 400                CA    CA B 504     1555   1555  2.29  
LINK         OD1 ASP B 402                CA    CA B 504     1555   1555  2.56  
LINK         O   GLN B 404                CA    CA B 504     1555   1555  2.41  
LINK         OE2 GLU B 409                CA    CA B 504     1555   1555  2.47  
LINK         OE1 GLU B 409                CA    CA B 504     1555   1555  2.58  
SITE     1 AC1  5 ASP A 289  ASP A 291  ASP A 293  THR A 295                    
SITE     2 AC1  5 GLU A 300                                                     
SITE     1 AC2  5 ASP A 325  ASP A 327  ASN A 329  THR A 331                    
SITE     2 AC2  5 GLU A 336                                                     
SITE     1 AC3  5 ASP A 362  ASP A 364  ASN A 366  TYR A 368                    
SITE     2 AC3  5 GLU A 373                                                     
SITE     1 AC4  6 ASP A 398  ASP A 400  ASP A 402  GLN A 404                    
SITE     2 AC4  6 GLU A 409  HOH A 448                                          
SITE     1 AC5  5 ASP B 289  ASP B 291  ASP B 293  THR B 295                    
SITE     2 AC5  5 GLU B 300                                                     
SITE     1 AC6  5 ASP B 325  ASP B 327  ASN B 329  THR B 331                    
SITE     2 AC6  5 GLU B 336                                                     
SITE     1 AC7  5 ASP B 362  ASP B 364  ASN B 366  TYR B 368                    
SITE     2 AC7  5 GLU B 373                                                     
SITE     1 AC8  5 ASP B 398  ASP B 400  ASP B 402  GLN B 404                    
SITE     2 AC8  5 GLU B 409                                                     
CRYST1   46.374  101.635   82.211  90.00  91.45  90.00 P 1 21 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      0.021564  0.000000  0.000547        0.00000                         
SCALE2      0.000000  0.009839  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012168        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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