GenomeNet

Database: PDB
Entry: 3HVQ
LinkDB: 3HVQ
Original site: 3HVQ 
HEADER    HYDROLASE/HYDROLASE REGULATOR           16-JUN-09   3HVQ              
TITLE     CRYSTAL STRUCTURE OF A COMPLEX BETWEEN PROTEIN PHOSPHATASE 1 ALPHA    
TITLE    2 (PP1) AND THE PP1 BINDING AND PDZ DOMAINS OF NEURABIN                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-ALPHA CATALYTIC   
COMPND   3 SUBUNIT;                                                             
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 FRAGMENT: CATALYTIC SUBUNIT;                                         
COMPND   6 SYNONYM: PP-1A;                                                      
COMPND   7 EC: 3.1.3.16;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: NEURABIN-1;                                                
COMPND  11 CHAIN: C, D;                                                         
COMPND  12 FRAGMENT: PP1 BINDING AND PDZ DOMAINS;                               
COMPND  13 SYNONYM: NEURABIN-I, NEURAL TISSUE-SPECIFIC F-ACTIN-BINDING PROTEIN  
COMPND  14 I, PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 9A, P180, PP1BP175;      
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PPP1A, PPP1CA;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: RP1B;                                     
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  13 ORGANISM_COMMON: RAT;                                                
SOURCE  14 ORGANISM_TAXID: 10116;                                               
SOURCE  15 GENE: PPP1R9A;                                                       
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;                              
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: RP1B                                      
KEYWDS    PP1, NEURABIN, SERINE/THREONINE PHOSPHATASE, POST SYNAPTIC DENSITY,   
KEYWDS   2 GLUTAMETERGIC RECEPTORS, CARBOHYDRATE METABOLISM, CELL CYCLE, CELL   
KEYWDS   3 DIVISION, GLYCOGEN METABOLISM, HYDROLASE, IRON, MANGANESE, METAL-    
KEYWDS   4 BINDING, PHOSPHOPROTEIN, PROTEIN PHOSPHATASE, ACTIN-BINDING, CELL    
KEYWDS   5 JUNCTION, CELL PROJECTION, CYTOSKELETON, DEVELOPMENTAL PROTEIN,      
KEYWDS   6 DIFFERENTIATION, NEUROGENESIS, NUCLEUS, SYNAPSE, SYNAPTOSOME,        
KEYWDS   7 HYDROLASE-HYDROLASE REGULATOR COMPLEX                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.A.CRITTON,M.J.RAGUSA,R.PAGE,W.PETI                                  
REVDAT   3   13-JUL-11 3HVQ    1       VERSN                                    
REVDAT   2   21-APR-10 3HVQ    1       JRNL                                     
REVDAT   1   23-MAR-10 3HVQ    0                                                
JRNL        AUTH   M.J.RAGUSA,B.DANCHECK,D.A.CRITTON,A.C.NAIRN,R.PAGE,W.PETI    
JRNL        TITL   SPINOPHILIN DIRECTS PROTEIN PHOSPHATASE 1 SPECIFICITY BY     
JRNL        TITL 2 BLOCKING SUBSTRATE BINDING SITES.                            
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  17   459 2010              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   20305656                                                     
JRNL        DOI    10.1038/NSMB.1786                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 51001                          
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) : 0.164                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2704                            
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) : 3616                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.19                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1670                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 200                          
REMARK   3   BIN FREE R VALUE                    : 0.2560                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6413                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 32                                      
REMARK   3   SOLVENT ATOMS            : 560                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 25.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.59                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.16000                                              
REMARK   3    B22 (A**2) : -0.02000                                             
REMARK   3    B33 (A**2) : 0.04000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.49000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.202         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.186         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.113         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.339         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.926                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6614 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8935 ; 1.342 ; 1.975       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   806 ; 6.399 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   328 ;37.789 ;24.451       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1150 ;14.436 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    43 ;16.097 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   967 ; 0.093 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5049 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3061 ; 0.196 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4482 ; 0.306 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   581 ; 0.179 ; 0.200       
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):    47 ; 0.151 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    21 ; 0.155 ; 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):  4163 ; 1.824 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6495 ; 2.893 ; 5.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2780 ; 5.135 ; 8.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2440 ; 7.027 ;11.000       
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 : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : C D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C    436       C     499      5                      
REMARK   3           1     D    436       D     499      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    C    (A):    256 ;  0.42 ;  0.50           
REMARK   3   LOOSE POSITIONAL   1    C    (A):    245 ;  0.65 ;  5.00           
REMARK   3   MEDIUM THERMAL     1    C (A**2):    256 ;  0.98 ;  2.00           
REMARK   3   LOOSE THERMAL      1    C (A**2):    245 ;  2.62 ; 10.00           
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      7       A     300      5                      
REMARK   3           1     B      7       B     300      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    A    (A):   1176 ;  0.11 ;  0.50           
REMARK   3   LOOSE POSITIONAL   2    A    (A):   1144 ;  0.34 ;  5.00           
REMARK   3   MEDIUM THERMAL     2    A (A**2):   1176 ;  0.95 ;  2.00           
REMARK   3   LOOSE THERMAL      2    A (A**2):   1144 ;  2.58 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
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     7        A   300                          
REMARK   3    ORIGIN FOR THE GROUP (A): -20.3906  17.9014  44.6702              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0199 T22:  -0.0151                                     
REMARK   3      T33:  -0.0106 T12:  -0.0089                                     
REMARK   3      T13:  -0.0100 T23:  -0.0028                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4459 L22:   0.2392                                     
REMARK   3      L33:   0.3498 L12:   0.0314                                     
REMARK   3      L13:  -0.1750 L23:  -0.0991                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0122 S12:   0.0302 S13:   0.0106                       
REMARK   3      S21:  -0.0196 S22:   0.0229 S23:   0.0044                       
REMARK   3      S31:   0.0288 S32:  -0.0540 S33:  -0.0107                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     7        B   300                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.8354  18.1608  10.7803              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0159 T22:  -0.0106                                     
REMARK   3      T33:  -0.0197 T12:   0.0039                                     
REMARK   3      T13:  -0.0051 T23:  -0.0020                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3577 L22:   0.4443                                     
REMARK   3      L33:   0.4782 L12:  -0.0381                                     
REMARK   3      L13:  -0.3890 L23:  -0.0589                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0166 S12:   0.0072 S13:   0.0006                       
REMARK   3      S21:  -0.0005 S22:   0.0088 S23:  -0.0183                       
REMARK   3      S31:   0.0001 S32:   0.0001 S33:   0.0077                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   436        C   481                          
REMARK   3    ORIGIN FOR THE GROUP (A): -26.5390  34.6796  46.0824              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0704 T22:  -0.0520                                     
REMARK   3      T33:  -0.0030 T12:   0.0135                                     
REMARK   3      T13:  -0.0051 T23:   0.0068                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1536 L22:   1.2483                                     
REMARK   3      L33:   1.5026 L12:  -0.2715                                     
REMARK   3      L13:  -0.6228 L23:   0.0122                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0103 S12:  -0.0283 S13:   0.2448                       
REMARK   3      S21:  -0.0514 S22:   0.0865 S23:   0.0519                       
REMARK   3      S31:  -0.1409 S32:  -0.0749 S33:  -0.0967                       
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 :   C   482        C   501                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.1873   1.1827  25.2167              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0072 T22:  -0.0152                                     
REMARK   3      T33:  -0.0720 T12:  -0.0453                                     
REMARK   3      T13:  -0.0360 T23:  -0.0459                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1160 L22:   8.5053                                     
REMARK   3      L33:   2.5460 L12:  -4.5235                                     
REMARK   3      L13:  -1.9018 L23:   1.4861                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1612 S12:   0.1215 S13:  -0.2789                       
REMARK   3      S21:  -0.0388 S22:  -0.1840 S23:   0.5745                       
REMARK   3      S31:  -0.1167 S32:  -0.1935 S33:   0.3452                       
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 :   C   502        C   592                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.6949  -6.2935  13.3418              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0299 T22:  -0.0239                                     
REMARK   3      T33:  -0.0149 T12:  -0.0634                                     
REMARK   3      T13:   0.0149 T23:  -0.0603                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5153 L22:   0.8676                                     
REMARK   3      L33:   0.3744 L12:   0.4449                                     
REMARK   3      L13:  -0.6284 L23:  -0.4711                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2143 S12:   0.2629 S13:  -0.3266                       
REMARK   3      S21:  -0.0187 S22:   0.0829 S23:  -0.1079                       
REMARK   3      S31:  -0.0175 S32:  -0.0521 S33:   0.1314                       
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 :   D   435        D   481                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.7709  34.6863  10.3273              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0212 T22:  -0.0435                                     
REMARK   3      T33:  -0.0188 T12:   0.0014                                     
REMARK   3      T13:   0.0160 T23:   0.0082                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6889 L22:   1.0266                                     
REMARK   3      L33:   1.3500 L12:   0.4494                                     
REMARK   3      L13:  -0.3432 L23:  -0.2321                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0908 S12:   0.0021 S13:   0.2028                       
REMARK   3      S21:   0.0164 S22:   0.0710 S23:  -0.0587                       
REMARK   3      S31:  -0.1260 S32:   0.0391 S33:  -0.1617                       
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 :   D   482        D   499                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.2253   1.1069  29.2866              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0520 T22:  -0.0260                                     
REMARK   3      T33:  -0.0264 T12:   0.0786                                     
REMARK   3      T13:  -0.0411 T23:   0.0569                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0553 L22:  18.0193                                     
REMARK   3      L33:   6.8596 L12:   4.5278                                     
REMARK   3      L13:   1.0190 L23:   0.3787                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2076 S12:  -0.1899 S13:  -0.5055                       
REMARK   3      S21:   0.3132 S22:   0.1205 S23:  -0.2995                       
REMARK   3      S31:   0.4351 S32:  -0.0824 S33:   0.0871                       
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 3HVQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUN-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB053640.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-DEC-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 7.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X6A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : SI(111) CHANNEL CUT MONOCHROMATOR  
REMARK 200  OPTICS                         : DOUBLE CRYSTAL CHANNEL CUT,        
REMARK 200                                   SI(111), 1M LONG RH COATED         
REMARK 200                                   TOROIDAL MIRROR FOR VERTICAL AND   
REMARK 200                                   HORIZONTAL FOCUSING                
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 53709                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.4000                            
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     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.26300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.000                              
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 ENTRY 3EGG                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M (NH4)2HPO4, 20% PEG 3350, PH       
REMARK 280  7.9, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K                
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       60.43200            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.82750            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       60.43200            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       41.82750            
REMARK 290   SMTRY3   4  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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11100 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 33750 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -76.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4530 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4950 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15370 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 A 460  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 406  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     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     MET A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     LYS A   301                                                      
REMARK 465     ASN A   302                                                      
REMARK 465     LYS A   303                                                      
REMARK 465     GLY A   304                                                      
REMARK 465     LYS A   305                                                      
REMARK 465     TYR A   306                                                      
REMARK 465     GLY A   307                                                      
REMARK 465     GLN A   308                                                      
REMARK 465     PHE A   309                                                      
REMARK 465     SER A   310                                                      
REMARK 465     GLY A   311                                                      
REMARK 465     LEU A   312                                                      
REMARK 465     ASN A   313                                                      
REMARK 465     PRO A   314                                                      
REMARK 465     GLY A   315                                                      
REMARK 465     GLY A   316                                                      
REMARK 465     ARG A   317                                                      
REMARK 465     PRO A   318                                                      
REMARK 465     ILE A   319                                                      
REMARK 465     THR A   320                                                      
REMARK 465     PRO A   321                                                      
REMARK 465     PRO A   322                                                      
REMARK 465     ARG A   323                                                      
REMARK 465     ASN A   324                                                      
REMARK 465     SER A   325                                                      
REMARK 465     ALA A   326                                                      
REMARK 465     LYS A   327                                                      
REMARK 465     ALA A   328                                                      
REMARK 465     LYS A   329                                                      
REMARK 465     LYS A   330                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     MET B     4                                                      
REMARK 465     GLY B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     LYS B   301                                                      
REMARK 465     ASN B   302                                                      
REMARK 465     LYS B   303                                                      
REMARK 465     GLY B   304                                                      
REMARK 465     LYS B   305                                                      
REMARK 465     TYR B   306                                                      
REMARK 465     GLY B   307                                                      
REMARK 465     GLN B   308                                                      
REMARK 465     PHE B   309                                                      
REMARK 465     SER B   310                                                      
REMARK 465     GLY B   311                                                      
REMARK 465     LEU B   312                                                      
REMARK 465     ASN B   313                                                      
REMARK 465     PRO B   314                                                      
REMARK 465     GLY B   315                                                      
REMARK 465     GLY B   316                                                      
REMARK 465     ARG B   317                                                      
REMARK 465     PRO B   318                                                      
REMARK 465     ILE B   319                                                      
REMARK 465     THR B   320                                                      
REMARK 465     PRO B   321                                                      
REMARK 465     PRO B   322                                                      
REMARK 465     ARG B   323                                                      
REMARK 465     ASN B   324                                                      
REMARK 465     SER B   325                                                      
REMARK 465     ALA B   326                                                      
REMARK 465     LYS B   327                                                      
REMARK 465     ALA B   328                                                      
REMARK 465     LYS B   329                                                      
REMARK 465     LYS B   330                                                      
REMARK 465     GLY C   423                                                      
REMARK 465     HIS C   424                                                      
REMARK 465     MET C   425                                                      
REMARK 465     ASP C   426                                                      
REMARK 465     ASP C   427                                                      
REMARK 465     SER C   428                                                      
REMARK 465     ASP C   429                                                      
REMARK 465     GLU C   430                                                      
REMARK 465     ASN C   431                                                      
REMARK 465     ASN C   432                                                      
REMARK 465     TYR C   433                                                      
REMARK 465     TYR C   434                                                      
REMARK 465     GLN C   435                                                      
REMARK 465     GLY D   423                                                      
REMARK 465     HIS D   424                                                      
REMARK 465     MET D   425                                                      
REMARK 465     ASP D   426                                                      
REMARK 465     ASP D   427                                                      
REMARK 465     SER D   428                                                      
REMARK 465     ASP D   429                                                      
REMARK 465     GLU D   430                                                      
REMARK 465     ASN D   431                                                      
REMARK 465     ASN D   432                                                      
REMARK 465     TYR D   433                                                      
REMARK 465     TYR D   434                                                      
REMARK 465     LYS D   500                                                      
REMARK 465     LEU D   501                                                      
REMARK 465     GLU D   502                                                      
REMARK 465     LEU D   503                                                      
REMARK 465     PHE D   504                                                      
REMARK 465     PRO D   505                                                      
REMARK 465     VAL D   506                                                      
REMARK 465     GLU D   507                                                      
REMARK 465     LEU D   508                                                      
REMARK 465     GLU D   509                                                      
REMARK 465     LYS D   510                                                      
REMARK 465     ASP D   511                                                      
REMARK 465     GLU D   512                                                      
REMARK 465     ASP D   513                                                      
REMARK 465     GLY D   514                                                      
REMARK 465     LEU D   515                                                      
REMARK 465     GLY D   516                                                      
REMARK 465     ILE D   517                                                      
REMARK 465     SER D   518                                                      
REMARK 465     ILE D   519                                                      
REMARK 465     ILE D   520                                                      
REMARK 465     GLY D   521                                                      
REMARK 465     MET D   522                                                      
REMARK 465     GLY D   523                                                      
REMARK 465     VAL D   524                                                      
REMARK 465     GLY D   525                                                      
REMARK 465     ALA D   526                                                      
REMARK 465     ASP D   527                                                      
REMARK 465     ALA D   528                                                      
REMARK 465     GLY D   529                                                      
REMARK 465     LEU D   530                                                      
REMARK 465     GLU D   531                                                      
REMARK 465     LYS D   532                                                      
REMARK 465     LEU D   533                                                      
REMARK 465     GLY D   534                                                      
REMARK 465     ILE D   535                                                      
REMARK 465     PHE D   536                                                      
REMARK 465     VAL D   537                                                      
REMARK 465     LYS D   538                                                      
REMARK 465     THR D   539                                                      
REMARK 465     VAL D   540                                                      
REMARK 465     THR D   541                                                      
REMARK 465     GLU D   542                                                      
REMARK 465     GLY D   543                                                      
REMARK 465     GLY D   544                                                      
REMARK 465     ALA D   545                                                      
REMARK 465     ALA D   546                                                      
REMARK 465     GLN D   547                                                      
REMARK 465     ARG D   548                                                      
REMARK 465     ASP D   549                                                      
REMARK 465     GLY D   550                                                      
REMARK 465     ARG D   551                                                      
REMARK 465     ILE D   552                                                      
REMARK 465     GLN D   553                                                      
REMARK 465     VAL D   554                                                      
REMARK 465     ASN D   555                                                      
REMARK 465     ASP D   556                                                      
REMARK 465     GLN D   557                                                      
REMARK 465     ILE D   558                                                      
REMARK 465     VAL D   559                                                      
REMARK 465     GLU D   560                                                      
REMARK 465     VAL D   561                                                      
REMARK 465     ASP D   562                                                      
REMARK 465     GLY D   563                                                      
REMARK 465     ILE D   564                                                      
REMARK 465     SER D   565                                                      
REMARK 465     LEU D   566                                                      
REMARK 465     VAL D   567                                                      
REMARK 465     GLY D   568                                                      
REMARK 465     VAL D   569                                                      
REMARK 465     THR D   570                                                      
REMARK 465     GLN D   571                                                      
REMARK 465     ASN D   572                                                      
REMARK 465     PHE D   573                                                      
REMARK 465     ALA D   574                                                      
REMARK 465     ALA D   575                                                      
REMARK 465     THR D   576                                                      
REMARK 465     VAL D   577                                                      
REMARK 465     LEU D   578                                                      
REMARK 465     ARG D   579                                                      
REMARK 465     ASN D   580                                                      
REMARK 465     THR D   581                                                      
REMARK 465     LYS D   582                                                      
REMARK 465     GLY D   583                                                      
REMARK 465     ASN D   584                                                      
REMARK 465     VAL D   585                                                      
REMARK 465     ARG D   586                                                      
REMARK 465     PHE D   587                                                      
REMARK 465     VAL D   588                                                      
REMARK 465     ILE D   589                                                      
REMARK 465     GLY D   590                                                      
REMARK 465     ARG D   591                                                      
REMARK 465     GLU D   592                                                      
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  23    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 218    CD   OE1  OE2                                       
REMARK 470     GLU A 230    CD   OE1  OE2                                       
REMARK 470     LYS A 234    CD   CE   NZ                                        
REMARK 470     GLU B  18    CD   OE1  OE2                                       
REMARK 470     ARG B  23    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU B 230    CD   OE1  OE2                                       
REMARK 470     LYS B 234    CE   NZ                                             
REMARK 470     GLU C 450    CD   OE1  OE2                                       
REMARK 470     GLU C 451    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 457    CD   CE   NZ                                        
REMARK 470     ASP C 481    CG   OD1  OD2                                       
REMARK 470     GLU C 502    CD   OE1  OE2                                       
REMARK 470     GLU C 512    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 450    CD   OE1  OE2                                       
REMARK 470     GLU D 451    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 474    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLN A   214     O    HOH A   393              1.62            
REMARK 500   O    GLN B   214     O    HOH B   385              1.84            
REMARK 500   NE2  GLN C   448     O    HOH C   360              1.95            
REMARK 500   OE1  GLU B   184     O    HOH B   429              1.98            
REMARK 500   OE2  GLU B   184     O    HOH B   392              2.08            
REMARK 500   O    HOH D   600     O    HOH D   601              2.08            
REMARK 500   OE2  GLU B   139     O    HOH B   375              2.09            
REMARK 500   ND2  ASN C   572     O    HOH C   242              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  95      158.48     77.84                                   
REMARK 500    ARG A  96      -57.79     68.04                                   
REMARK 500    TYR A 144     -113.35   -135.48                                   
REMARK 500    SER A 224     -153.19     62.88                                   
REMARK 500    ALA A 247     -132.19   -132.33                                   
REMARK 500    HIS A 248      -24.99     83.95                                   
REMARK 500    LYS A 260     -117.89     64.54                                   
REMARK 500    ASN A 271       55.09     37.17                                   
REMARK 500    CYS A 273       34.54     36.72                                   
REMARK 500    LEU A 289       30.28     74.65                                   
REMARK 500    ASP B  95      157.12     81.57                                   
REMARK 500    ARG B  96      -50.38     67.93                                   
REMARK 500    TYR B 144     -116.01   -132.90                                   
REMARK 500    GLN B 214      -70.88    -80.55                                   
REMARK 500    SER B 224     -149.55     64.11                                   
REMARK 500    ALA B 247     -132.95   -137.44                                   
REMARK 500    HIS B 248      -24.99     79.30                                   
REMARK 500    LYS B 260     -107.60     58.69                                   
REMARK 500    ASN B 271       55.92     35.81                                   
REMARK 500    CYS B 273       41.20     35.21                                   
REMARK 500    ASP C 511     -165.30   -115.47                                   
REMARK 500    ASP C 527       33.23    -97.83                                   
REMARK 500    ASN C 555       -8.22     78.64                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 454        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH A 455        DISTANCE =  5.17 ANGSTROMS                       
REMARK 525    HOH C 597        DISTANCE =  5.56 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A   1  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  64   OD2                                                    
REMARK 620 2 ASP A  92   OD2  94.3                                              
REMARK 620 3 PO4 A 332   O1  155.9  97.8                                        
REMARK 620 4 HOH A 333   O    89.2 172.4  76.6                                  
REMARK 620 5 HOH A 335   O    84.5  75.5  78.5  98.2                            
REMARK 620 6 HIS A  66   NE2 104.8  97.9  94.1  87.6 169.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 331  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  92   OD2                                                    
REMARK 620 2 ASN A 124   OD1  96.3                                              
REMARK 620 3 PO4 A 332   O4  101.3  85.0                                        
REMARK 620 4 HOH A 335   O    81.5 161.6  77.6                                  
REMARK 620 5 HIS A 173   NE2  84.3  91.7 173.8 106.2                            
REMARK 620 6 HIS A 248   ND1 162.6  99.3  87.9  86.1  87.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 331  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  64   OD2                                                    
REMARK 620 2 ASP B  92   OD2  94.0                                              
REMARK 620 3 PO4 B 333   O2  162.4  97.5                                        
REMARK 620 4 HOH B 338   O    88.3  80.4  80.6                                  
REMARK 620 5 HOH B 337   O    87.6 174.9  79.8  94.8                            
REMARK 620 6 HIS B  66   NE2 106.1  86.8  87.8 161.4  97.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 332  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  92   OD2                                                    
REMARK 620 2 ASN B 124   OD1  93.0                                              
REMARK 620 3 PO4 B 333   O3   96.7  84.4                                        
REMARK 620 4 HOH B 338   O    81.0 159.3  76.7                                  
REMARK 620 5 HIS B 173   NE2  86.7  85.7 169.7 113.5                            
REMARK 620 6 HIS B 248   ND1 165.4  99.2  92.4  90.2  86.2                      
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 MN A 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 331                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 332                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 331                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 332                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 333                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 334                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 335                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2FN5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2GLE   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1S70   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1FJM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EGH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EGG   RELATED DB: PDB                                   
DBREF  3HVQ A    7   330  UNP    P62136   PP1A_HUMAN       7    330             
DBREF  3HVQ B    7   330  UNP    P62136   PP1A_HUMAN       7    330             
DBREF  3HVQ C  426   592  UNP    O35867   NEB1_RAT       426    592             
DBREF  3HVQ D  426   592  UNP    O35867   NEB1_RAT       426    592             
SEQADV 3HVQ GLY A    2  UNP  P62136              EXPRESSION TAG                 
SEQADV 3HVQ HIS A    3  UNP  P62136              EXPRESSION TAG                 
SEQADV 3HVQ MET A    4  UNP  P62136              EXPRESSION TAG                 
SEQADV 3HVQ GLY A    5  UNP  P62136              EXPRESSION TAG                 
SEQADV 3HVQ SER A    6  UNP  P62136              EXPRESSION TAG                 
SEQADV 3HVQ GLY B    2  UNP  P62136              EXPRESSION TAG                 
SEQADV 3HVQ HIS B    3  UNP  P62136              EXPRESSION TAG                 
SEQADV 3HVQ MET B    4  UNP  P62136              EXPRESSION TAG                 
SEQADV 3HVQ GLY B    5  UNP  P62136              EXPRESSION TAG                 
SEQADV 3HVQ SER B    6  UNP  P62136              EXPRESSION TAG                 
SEQADV 3HVQ GLY C  423  UNP  O35867              EXPRESSION TAG                 
SEQADV 3HVQ HIS C  424  UNP  O35867              EXPRESSION TAG                 
SEQADV 3HVQ MET C  425  UNP  O35867              EXPRESSION TAG                 
SEQADV 3HVQ GLY D  423  UNP  O35867              EXPRESSION TAG                 
SEQADV 3HVQ HIS D  424  UNP  O35867              EXPRESSION TAG                 
SEQADV 3HVQ MET D  425  UNP  O35867              EXPRESSION TAG                 
SEQRES   1 A  329  GLY HIS MET GLY SER LEU ASN LEU ASP SER ILE ILE GLY          
SEQRES   2 A  329  ARG LEU LEU GLU VAL GLN GLY SER ARG PRO GLY LYS ASN          
SEQRES   3 A  329  VAL GLN LEU THR GLU ASN GLU ILE ARG GLY LEU CYS LEU          
SEQRES   4 A  329  LYS SER ARG GLU ILE PHE LEU SER GLN PRO ILE LEU LEU          
SEQRES   5 A  329  GLU LEU GLU ALA PRO LEU LYS ILE CYS GLY ASP ILE HIS          
SEQRES   6 A  329  GLY GLN TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR GLY          
SEQRES   7 A  329  GLY PHE PRO PRO GLU SER ASN TYR LEU PHE LEU GLY ASP          
SEQRES   8 A  329  TYR VAL ASP ARG GLY LYS GLN SER LEU GLU THR ILE CYS          
SEQRES   9 A  329  LEU LEU LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN PHE          
SEQRES  10 A  329  PHE LEU LEU ARG GLY ASN HIS GLU CYS ALA SER ILE ASN          
SEQRES  11 A  329  ARG ILE TYR GLY PHE TYR ASP GLU CYS LYS ARG ARG TYR          
SEQRES  12 A  329  ASN ILE LYS LEU TRP LYS THR PHE THR ASP CYS PHE ASN          
SEQRES  13 A  329  CYS LEU PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE PHE          
SEQRES  14 A  329  CYS CYS HIS GLY GLY LEU SER PRO ASP LEU GLN SER MET          
SEQRES  15 A  329  GLU GLN ILE ARG ARG ILE MET ARG PRO THR ASP VAL PRO          
SEQRES  16 A  329  ASP GLN GLY LEU LEU CYS ASP LEU LEU TRP SER ASP PRO          
SEQRES  17 A  329  ASP LYS ASP VAL GLN GLY TRP GLY GLU ASN ASP ARG GLY          
SEQRES  18 A  329  VAL SER PHE THR PHE GLY ALA GLU VAL VAL ALA LYS PHE          
SEQRES  19 A  329  LEU HIS LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA HIS          
SEQRES  20 A  329  GLN VAL VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS ARG          
SEQRES  21 A  329  GLN LEU VAL THR LEU PHE SER ALA PRO ASN TYR CYS GLY          
SEQRES  22 A  329  GLU PHE ASP ASN ALA GLY ALA MET MET SER VAL ASP GLU          
SEQRES  23 A  329  THR LEU MET CYS SER PHE GLN ILE LEU LYS PRO ALA ASP          
SEQRES  24 A  329  LYS ASN LYS GLY LYS TYR GLY GLN PHE SER GLY LEU ASN          
SEQRES  25 A  329  PRO GLY GLY ARG PRO ILE THR PRO PRO ARG ASN SER ALA          
SEQRES  26 A  329  LYS ALA LYS LYS                                              
SEQRES   1 B  329  GLY HIS MET GLY SER LEU ASN LEU ASP SER ILE ILE GLY          
SEQRES   2 B  329  ARG LEU LEU GLU VAL GLN GLY SER ARG PRO GLY LYS ASN          
SEQRES   3 B  329  VAL GLN LEU THR GLU ASN GLU ILE ARG GLY LEU CYS LEU          
SEQRES   4 B  329  LYS SER ARG GLU ILE PHE LEU SER GLN PRO ILE LEU LEU          
SEQRES   5 B  329  GLU LEU GLU ALA PRO LEU LYS ILE CYS GLY ASP ILE HIS          
SEQRES   6 B  329  GLY GLN TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR GLY          
SEQRES   7 B  329  GLY PHE PRO PRO GLU SER ASN TYR LEU PHE LEU GLY ASP          
SEQRES   8 B  329  TYR VAL ASP ARG GLY LYS GLN SER LEU GLU THR ILE CYS          
SEQRES   9 B  329  LEU LEU LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN PHE          
SEQRES  10 B  329  PHE LEU LEU ARG GLY ASN HIS GLU CYS ALA SER ILE ASN          
SEQRES  11 B  329  ARG ILE TYR GLY PHE TYR ASP GLU CYS LYS ARG ARG TYR          
SEQRES  12 B  329  ASN ILE LYS LEU TRP LYS THR PHE THR ASP CYS PHE ASN          
SEQRES  13 B  329  CYS LEU PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE PHE          
SEQRES  14 B  329  CYS CYS HIS GLY GLY LEU SER PRO ASP LEU GLN SER MET          
SEQRES  15 B  329  GLU GLN ILE ARG ARG ILE MET ARG PRO THR ASP VAL PRO          
SEQRES  16 B  329  ASP GLN GLY LEU LEU CYS ASP LEU LEU TRP SER ASP PRO          
SEQRES  17 B  329  ASP LYS ASP VAL GLN GLY TRP GLY GLU ASN ASP ARG GLY          
SEQRES  18 B  329  VAL SER PHE THR PHE GLY ALA GLU VAL VAL ALA LYS PHE          
SEQRES  19 B  329  LEU HIS LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA HIS          
SEQRES  20 B  329  GLN VAL VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS ARG          
SEQRES  21 B  329  GLN LEU VAL THR LEU PHE SER ALA PRO ASN TYR CYS GLY          
SEQRES  22 B  329  GLU PHE ASP ASN ALA GLY ALA MET MET SER VAL ASP GLU          
SEQRES  23 B  329  THR LEU MET CYS SER PHE GLN ILE LEU LYS PRO ALA ASP          
SEQRES  24 B  329  LYS ASN LYS GLY LYS TYR GLY GLN PHE SER GLY LEU ASN          
SEQRES  25 B  329  PRO GLY GLY ARG PRO ILE THR PRO PRO ARG ASN SER ALA          
SEQRES  26 B  329  LYS ALA LYS LYS                                              
SEQRES   1 C  170  GLY HIS MET ASP ASP SER ASP GLU ASN ASN TYR TYR GLN          
SEQRES   2 C  170  PRO ASP MET GLU TYR SER GLU ILE VAL GLY LEU PRO GLN          
SEQRES   3 C  170  GLU GLU GLU ILE PRO ALA ASN ARG LYS ILE LYS PHE SER          
SEQRES   4 C  170  CYS ALA PRO ILE LYS VAL PHE ASN THR TYR SER ASN GLU          
SEQRES   5 C  170  ASP TYR ASP ARG ARG ASN ASP ASP VAL ASP PRO VAL ALA          
SEQRES   6 C  170  ALA SER ALA GLU TYR GLU LEU GLU LYS ARG VAL GLU LYS          
SEQRES   7 C  170  LEU GLU LEU PHE PRO VAL GLU LEU GLU LYS ASP GLU ASP          
SEQRES   8 C  170  GLY LEU GLY ILE SER ILE ILE GLY MET GLY VAL GLY ALA          
SEQRES   9 C  170  ASP ALA GLY LEU GLU LYS LEU GLY ILE PHE VAL LYS THR          
SEQRES  10 C  170  VAL THR GLU GLY GLY ALA ALA GLN ARG ASP GLY ARG ILE          
SEQRES  11 C  170  GLN VAL ASN ASP GLN ILE VAL GLU VAL ASP GLY ILE SER          
SEQRES  12 C  170  LEU VAL GLY VAL THR GLN ASN PHE ALA ALA THR VAL LEU          
SEQRES  13 C  170  ARG ASN THR LYS GLY ASN VAL ARG PHE VAL ILE GLY ARG          
SEQRES  14 C  170  GLU                                                          
SEQRES   1 D  170  GLY HIS MET ASP ASP SER ASP GLU ASN ASN TYR TYR GLN          
SEQRES   2 D  170  PRO ASP MET GLU TYR SER GLU ILE VAL GLY LEU PRO GLN          
SEQRES   3 D  170  GLU GLU GLU ILE PRO ALA ASN ARG LYS ILE LYS PHE SER          
SEQRES   4 D  170  CYS ALA PRO ILE LYS VAL PHE ASN THR TYR SER ASN GLU          
SEQRES   5 D  170  ASP TYR ASP ARG ARG ASN ASP ASP VAL ASP PRO VAL ALA          
SEQRES   6 D  170  ALA SER ALA GLU TYR GLU LEU GLU LYS ARG VAL GLU LYS          
SEQRES   7 D  170  LEU GLU LEU PHE PRO VAL GLU LEU GLU LYS ASP GLU ASP          
SEQRES   8 D  170  GLY LEU GLY ILE SER ILE ILE GLY MET GLY VAL GLY ALA          
SEQRES   9 D  170  ASP ALA GLY LEU GLU LYS LEU GLY ILE PHE VAL LYS THR          
SEQRES  10 D  170  VAL THR GLU GLY GLY ALA ALA GLN ARG ASP GLY ARG ILE          
SEQRES  11 D  170  GLN VAL ASN ASP GLN ILE VAL GLU VAL ASP GLY ILE SER          
SEQRES  12 D  170  LEU VAL GLY VAL THR GLN ASN PHE ALA ALA THR VAL LEU          
SEQRES  13 D  170  ARG ASN THR LYS GLY ASN VAL ARG PHE VAL ILE GLY ARG          
SEQRES  14 D  170  GLU                                                          
HET     MN  A   1       1                                                       
HET     MN  A 331       1                                                       
HET    PO4  A 332       5                                                       
HET     MN  B 331       1                                                       
HET     MN  B 332       1                                                       
HET    PO4  B 333       5                                                       
HET    GOL  B   1       6                                                       
HET    GOL  B 334       6                                                       
HET    GOL  B 335       6                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5   MN    4(MN 2+)                                                     
FORMUL   7  PO4    2(O4 P 3-)                                                   
FORMUL  11  GOL    3(C3 H8 O3)                                                  
FORMUL  14  HOH   *560(H2 O)                                                    
HELIX    1   1 ASN A    8  GLU A   18  1                                  11    
HELIX    2   2 THR A   31  GLN A   49  1                                  19    
HELIX    3   3 GLN A   68  GLY A   80  1                                  13    
HELIX    4   4 GLN A   99  TYR A  114  1                                  16    
HELIX    5   5 CYS A  127  ARG A  132  1                                   6    
HELIX    6   6 GLY A  135  TYR A  144  1                                  10    
HELIX    7   7 ASN A  145  ASN A  157  1                                  13    
HELIX    8   8 MET A  183  ARG A  188  1                                   6    
HELIX    9   9 GLY A  199  SER A  207  1                                   9    
HELIX   10  10 GLY A  228  ASP A  240  1                                  13    
HELIX   11  11 ASN A  271  GLU A  275  5                                   5    
HELIX   12  12 ASN B    8  GLU B   18  1                                  11    
HELIX   13  13 THR B   31  GLN B   49  1                                  19    
HELIX   14  14 GLN B   68  GLY B   80  1                                  13    
HELIX   15  15 GLN B   99  TYR B  114  1                                  16    
HELIX   16  16 CYS B  127  ARG B  132  1                                   6    
HELIX   17  17 GLY B  135  TYR B  144  1                                  10    
HELIX   18  18 ASN B  145  ASN B  157  1                                  13    
HELIX   19  19 MET B  183  ARG B  188  1                                   6    
HELIX   20  20 GLY B  199  SER B  207  1                                   9    
HELIX   21  21 GLY B  228  ASP B  240  1                                  13    
HELIX   22  22 ASN B  271  GLU B  275  5                                   5    
HELIX   23  23 ASP C  484  GLU C  499  1                                  16    
HELIX   24  24 GLY C  544  GLY C  550  1                                   7    
HELIX   25  25 THR C  570  THR C  581  1                                  12    
HELIX   26  26 ASP D  484  GLU D  499  1                                  16    
SHEET    1   A 6 LEU A  52  LEU A  55  0                                        
SHEET    2   A 6 ALA A 162  VAL A 165  1  O  ILE A 164   N  LEU A  53           
SHEET    3   A 6 ILE A 169  CYS A 172 -1  O  CYS A 171   N  ALA A 163           
SHEET    4   A 6 LEU A 243  ARG A 246  1  O  LEU A 243   N  PHE A 170           
SHEET    5   A 6 LEU A 263  LEU A 266  1  O  LEU A 266   N  ARG A 246           
SHEET    6   A 6 TYR A 255  PHE A 258 -1  N  GLU A 256   O  THR A 265           
SHEET    1   B 7 PHE A 118  LEU A 120  0                                        
SHEET    2   B 7 TYR A  87  PHE A  89  1  N  PHE A  89   O  PHE A 119           
SHEET    3   B 7 LEU A  59  CYS A  62  1  N  LYS A  60   O  LEU A  88           
SHEET    4   B 7 GLY A 280  VAL A 285 -1  O  VAL A 285   N  LEU A  59           
SHEET    5   B 7 MET A 290  PRO A 298 -1  O  LEU A 296   N  GLY A 280           
SHEET    6   B 7 ILE C 465  THR C 470  1  O  PHE C 468   N  LYS A 297           
SHEET    7   B 7 TYR C 440  ILE C 443 -1  N  SER C 441   O  VAL C 467           
SHEET    1   C 6 PHE A 118  LEU A 120  0                                        
SHEET    2   C 6 TYR A  87  PHE A  89  1  N  PHE A  89   O  PHE A 119           
SHEET    3   C 6 LEU A  59  CYS A  62  1  N  LYS A  60   O  LEU A  88           
SHEET    4   C 6 GLY A 280  VAL A 285 -1  O  VAL A 285   N  LEU A  59           
SHEET    5   C 6 MET A 290  PRO A 298 -1  O  LEU A 296   N  GLY A 280           
SHEET    6   C 6 LYS C 459  PHE C 460  1  O  LYS C 459   N  CYS A 291           
SHEET    1   D 3 ASP A 208  PRO A 209  0                                        
SHEET    2   D 3 PHE A 225  PHE A 227  1  O  PHE A 227   N  ASP A 208           
SHEET    3   D 3 TRP A 216  GLU A 218 -1  N  GLY A 217   O  THR A 226           
SHEET    1   E 6 LEU B  52  LEU B  55  0                                        
SHEET    2   E 6 ALA B 162  VAL B 165  1  O  ILE B 164   N  LEU B  53           
SHEET    3   E 6 ILE B 169  CYS B 171 -1  O  CYS B 171   N  ALA B 163           
SHEET    4   E 6 LEU B 243  ARG B 246  1  O  LEU B 243   N  PHE B 170           
SHEET    5   E 6 LEU B 263  LEU B 266  1  O  VAL B 264   N  ARG B 246           
SHEET    6   E 6 TYR B 255  PHE B 258 -1  N  PHE B 258   O  LEU B 263           
SHEET    1   F 7 PHE B 118  LEU B 120  0                                        
SHEET    2   F 7 TYR B  87  PHE B  89  1  N  PHE B  89   O  PHE B 119           
SHEET    3   F 7 LEU B  59  CYS B  62  1  N  CYS B  62   O  LEU B  88           
SHEET    4   F 7 GLY B 280  VAL B 285 -1  O  MET B 283   N  ILE B  61           
SHEET    5   F 7 MET B 290  PRO B 298 -1  O  LEU B 296   N  GLY B 280           
SHEET    6   F 7 ILE D 465  THR D 470  1  O  PHE D 468   N  ILE B 295           
SHEET    7   F 7 SER D 441  ILE D 443 -1  N  SER D 441   O  VAL D 467           
SHEET    1   G 6 PHE B 118  LEU B 120  0                                        
SHEET    2   G 6 TYR B  87  PHE B  89  1  N  PHE B  89   O  PHE B 119           
SHEET    3   G 6 LEU B  59  CYS B  62  1  N  CYS B  62   O  LEU B  88           
SHEET    4   G 6 GLY B 280  VAL B 285 -1  O  MET B 283   N  ILE B  61           
SHEET    5   G 6 MET B 290  PRO B 298 -1  O  LEU B 296   N  GLY B 280           
SHEET    6   G 6 LYS D 459  PHE D 460  1  O  LYS D 459   N  CYS B 291           
SHEET    1   H 3 ASP B 208  PRO B 209  0                                        
SHEET    2   H 3 PHE B 225  PHE B 227  1  O  PHE B 227   N  ASP B 208           
SHEET    3   H 3 TRP B 216  GLU B 218 -1  N  GLY B 217   O  THR B 226           
SHEET    1   I 4 GLU C 502  GLU C 509  0                                        
SHEET    2   I 4 ASN C 584  ARG C 591 -1  O  ARG C 591   N  GLU C 502           
SHEET    3   I 4 GLN C 557  VAL C 561 -1  N  GLN C 557   O  GLY C 590           
SHEET    4   I 4 ILE C 564  SER C 565 -1  O  ILE C 564   N  VAL C 561           
SHEET    1   J 2 ILE C 517  MET C 522  0                                        
SHEET    2   J 2 GLY C 534  VAL C 540 -1  O  PHE C 536   N  ILE C 520           
LINK         OD2 ASP A  64                MN    MN A   1     1555   1555  2.08  
LINK         OD2 ASP A  92                MN    MN A   1     1555   1555  2.32  
LINK         OD2 ASP A  92                MN    MN A 331     1555   1555  2.24  
LINK         OD1 ASN A 124                MN    MN A 331     1555   1555  2.06  
LINK         OD2 ASP B  64                MN    MN B 331     1555   1555  2.15  
LINK         OD2 ASP B  92                MN    MN B 332     1555   1555  2.24  
LINK         OD2 ASP B  92                MN    MN B 331     1555   1555  2.43  
LINK         OD1 ASN B 124                MN    MN B 332     1555   1555  2.08  
LINK        MN    MN A   1                 O1  PO4 A 332     1555   1555  2.29  
LINK        MN    MN A 331                 O4  PO4 A 332     1555   1555  2.26  
LINK        MN    MN B 331                 O2  PO4 B 333     1555   1555  2.27  
LINK        MN    MN B 332                 O3  PO4 B 333     1555   1555  2.18  
LINK        MN    MN A   1                 O   HOH A 333     1555   1555  2.42  
LINK        MN    MN A   1                 O   HOH A 335     1555   1555  2.13  
LINK        MN    MN A 331                 O   HOH A 335     1555   1555  1.93  
LINK        MN    MN B 331                 O   HOH B 338     1555   1555  1.90  
LINK        MN    MN B 331                 O   HOH B 337     1555   1555  2.41  
LINK        MN    MN B 332                 O   HOH B 338     1555   1555  2.10  
LINK         NE2 HIS B  66                MN    MN B 331     1555   1555  2.16  
LINK         NE2 HIS B 173                MN    MN B 332     1555   1555  2.19  
LINK         NE2 HIS A  66                MN    MN A   1     1555   1555  2.21  
LINK         NE2 HIS A 173                MN    MN A 331     1555   1555  2.23  
LINK         ND1 HIS B 248                MN    MN B 332     1555   1555  2.28  
LINK         ND1 HIS A 248                MN    MN A 331     1555   1555  2.34  
CISPEP   1 ALA A   57    PRO A   58          0         2.46                     
CISPEP   2 PRO A   82    PRO A   83          0         5.92                     
CISPEP   3 ARG A  191    PRO A  192          0        -4.63                     
CISPEP   4 ALA B   57    PRO B   58          0         6.79                     
CISPEP   5 PRO B   82    PRO B   83          0         4.07                     
CISPEP   6 ARG B  191    PRO B  192          0        -1.05                     
SITE     1 AC1  7 ASP A  64  HIS A  66  ASP A  92   MN A 331                    
SITE     2 AC1  7 PO4 A 332  HOH A 333  HOH A 335                               
SITE     1 AC2  7  MN A   1  ASP A  92  ASN A 124  HIS A 173                    
SITE     2 AC2  7 HIS A 248  PO4 A 332  HOH A 335                               
SITE     1 AC3 13  MN A   1  HIS A  66  ASP A  92  ARG A  96                    
SITE     2 AC3 13 ASN A 124  HIS A 125  ARG A 221  HIS A 248                    
SITE     3 AC3 13  MN A 331  HOH A 333  HOH A 335  HOH A 507                    
SITE     4 AC3 13 HOH A 510                                                     
SITE     1 AC4  7 ASP B  64  HIS B  66  ASP B  92   MN B 332                    
SITE     2 AC4  7 PO4 B 333  HOH B 337  HOH B 338                               
SITE     1 AC5  7 ASP B  92  ASN B 124  HIS B 173  HIS B 248                    
SITE     2 AC5  7  MN B 331  PO4 B 333  HOH B 338                               
SITE     1 AC6 15 HIS B  66  ASP B  92  ARG B  96  ASN B 124                    
SITE     2 AC6 15 HIS B 125  ARG B 221  HIS B 248  TYR B 272                    
SITE     3 AC6 15  MN B 331   MN B 332  HOH B 337  HOH B 338                    
SITE     4 AC6 15 HOH B 513  HOH B 515  HOH B 516                               
SITE     1 AC7  6 LYS A  26  GLY B  14  ARG B  15  GLU B  18                    
SITE     2 AC7  6 HOH B 336  HOH B 341                                          
SITE     1 AC8  2 LYS B 260  HOH B 432                                          
SITE     1 AC9  7 CYS B 127  SER B 129  ILE B 130  VAL B 195                    
SITE     2 AC9  7 ASP B 197  TRP B 206  HOH B 422                               
CRYST1  120.864   83.655  108.797  90.00  93.59  90.00 C 1 2 1       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      0.008274  0.000000  0.000519        0.00000                         
SCALE2      0.000000  0.011954  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009209        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system