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Database: PDB
Entry: 5IY5
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HEADER    OXIDOREDUCTASE                          24-MAR-16   5IY5              
TITLE     ELECTRON TRANSFER COMPLEX OF CYTOCHROME C AND CYTOCHROME C OXIDASE AT 
TITLE    2 2.0 ANGSTROM RESOLUTION                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 1;                            
COMPND   3 CHAIN: A, N;                                                         
COMPND   4 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE I;                         
COMPND   5 EC: 1.9.3.1;                                                         
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 2;                            
COMPND   8 CHAIN: B, O;                                                         
COMPND   9 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE II;                        
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 3;                            
COMPND  12 CHAIN: C, P;                                                         
COMPND  13 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE III;                       
COMPND  14 MOL_ID: 4;                                                           
COMPND  15 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL;   
COMPND  16 CHAIN: D, Q;                                                         
COMPND  17 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE IV,CYTOCHROME C OXIDASE    
COMPND  18 SUBUNIT IV ISOFORM 1,COX IV-1;                                       
COMPND  19 MOL_ID: 5;                                                           
COMPND  20 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL;            
COMPND  21 CHAIN: E, R;                                                         
COMPND  22 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VA;                        
COMPND  23 MOL_ID: 6;                                                           
COMPND  24 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL;            
COMPND  25 CHAIN: F, S;                                                         
COMPND  26 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VIA,CYTOCHROME C OXIDASE   
COMPND  27 POLYPEPTIDE VB;                                                      
COMPND  28 MOL_ID: 7;                                                           
COMPND  29 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 6A2, MITOCHONDRIAL;           
COMPND  30 CHAIN: G, T;                                                         
COMPND  31 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VIA-HEART,COXVIAH,         
COMPND  32 CYTOCHROME C OXIDASE POLYPEPTIDE VIB;                                
COMPND  33 MOL_ID: 8;                                                           
COMPND  34 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 6B1;                          
COMPND  35 CHAIN: H, U;                                                         
COMPND  36 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VII,CYTOCHROME C OXIDASE   
COMPND  37 SUBUNIT AED,CYTOCHROME C OXIDASE SUBUNIT VIB ISOFORM 1,COX VIB-1;    
COMPND  38 MOL_ID: 9;                                                           
COMPND  39 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 6C;                           
COMPND  40 CHAIN: I, V;                                                         
COMPND  41 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VIC,CYTOCHROME C OXIDASE   
COMPND  42 SUBUNIT STA;                                                         
COMPND  43 MOL_ID: 10;                                                          
COMPND  44 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL;           
COMPND  45 CHAIN: J, W;                                                         
COMPND  46 SYNONYM: CYTOCHROME C OXIDASE SUBUNIT VIIIC,VIIIC,CYTOCHROME C       
COMPND  47 OXIDASE SUBUNIT VIIA-HEART,CYTOCHROME C OXIDASE SUBUNIT VIIA-H,      
COMPND  48 CYTOCHROME C OXIDASE SUBUNIT VIIA-MUSCLE,CYTOCHROME C OXIDASE SUBUNIT
COMPND  49 VIIA-M;                                                              
COMPND  50 MOL_ID: 11;                                                          
COMPND  51 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL;            
COMPND  52 CHAIN: K, X;                                                         
COMPND  53 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VIIB,IHQ;                  
COMPND  54 MOL_ID: 12;                                                          
COMPND  55 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL;            
COMPND  56 CHAIN: L, Y;                                                         
COMPND  57 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VIIIA,CYTOCHROME C OXIDASE 
COMPND  58 POLYPEPTIDE VIIC;                                                    
COMPND  59 MOL_ID: 13;                                                          
COMPND  60 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL;            
COMPND  61 CHAIN: M, Z;                                                         
COMPND  62 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VIII-HEART,CYTOCHROME C    
COMPND  63 OXIDASE SUBUNIT 8-1,CYTOCHROME C OXIDASE SUBUNIT 8H,IX,VIIIB;        
COMPND  64 MOL_ID: 14;                                                          
COMPND  65 MOLECULE: CYTOCHROME C;                                              
COMPND  66 CHAIN: 1, 2                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   3 ORGANISM_COMMON: BOVINE;                                             
SOURCE   4 ORGANISM_TAXID: 9913;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   7 ORGANISM_COMMON: BOVINE;                                             
SOURCE   8 ORGANISM_TAXID: 9913;                                                
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  11 ORGANISM_COMMON: BOVINE;                                             
SOURCE  12 ORGANISM_TAXID: 9913;                                                
SOURCE  13 MOL_ID: 4;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  15 ORGANISM_COMMON: BOVINE;                                             
SOURCE  16 ORGANISM_TAXID: 9913;                                                
SOURCE  17 MOL_ID: 5;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  19 ORGANISM_COMMON: BOVINE;                                             
SOURCE  20 ORGANISM_TAXID: 9913;                                                
SOURCE  21 MOL_ID: 6;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  23 ORGANISM_COMMON: BOVINE;                                             
SOURCE  24 ORGANISM_TAXID: 9913;                                                
SOURCE  25 MOL_ID: 7;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  27 ORGANISM_COMMON: BOVINE;                                             
SOURCE  28 ORGANISM_TAXID: 9913;                                                
SOURCE  29 MOL_ID: 8;                                                           
SOURCE  30 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  31 ORGANISM_COMMON: BOVINE;                                             
SOURCE  32 ORGANISM_TAXID: 9913;                                                
SOURCE  33 MOL_ID: 9;                                                           
SOURCE  34 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  35 ORGANISM_COMMON: BOVINE;                                             
SOURCE  36 ORGANISM_TAXID: 9913;                                                
SOURCE  37 MOL_ID: 10;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  39 ORGANISM_COMMON: BOVINE;                                             
SOURCE  40 ORGANISM_TAXID: 9913;                                                
SOURCE  41 MOL_ID: 11;                                                          
SOURCE  42 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  43 ORGANISM_COMMON: BOVINE;                                             
SOURCE  44 ORGANISM_TAXID: 9913;                                                
SOURCE  45 MOL_ID: 12;                                                          
SOURCE  46 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  47 ORGANISM_COMMON: BOVINE;                                             
SOURCE  48 ORGANISM_TAXID: 9913;                                                
SOURCE  49 MOL_ID: 13;                                                          
SOURCE  50 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  51 ORGANISM_COMMON: BOVINE;                                             
SOURCE  52 ORGANISM_TAXID: 9913;                                                
SOURCE  53 MOL_ID: 14;                                                          
SOURCE  54 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;                                 
SOURCE  55 ORGANISM_COMMON: HORSE;                                              
SOURCE  56 ORGANISM_TAXID: 9796                                                 
KEYWDS    OXIDOREDUCTASE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.SHIMADA,J.BABA,S.AOE,A.SHIMADA,E.YAMASHITA,T.TSUKIHARA              
REVDAT   3   09-OCT-19 5IY5    1       COMPND REMARK HET    HETNAM              
REVDAT   3 2                   1       HETSYN FORMUL LINK   SITE                
REVDAT   3 3                   1       ATOM                                     
REVDAT   2   15-FEB-17 5IY5    1       JRNL                                     
REVDAT   1   11-JAN-17 5IY5    0                                                
JRNL        AUTH   S.SHIMADA,K.SHINZAWA-ITOH,J.BABA,S.AOE,A.SHIMADA,            
JRNL        AUTH 2 E.YAMASHITA,J.KANG,M.TATENO,S.YOSHIKAWA,T.TSUKIHARA          
JRNL        TITL   COMPLEX STRUCTURE OF CYTOCHROME C-CYTOCHROME C OXIDASE       
JRNL        TITL 2 REVEALS A NOVEL PROTEIN-PROTEIN INTERACTION MODE             
JRNL        REF    EMBO J.                       V.  36   291 2017              
JRNL        REFN                   ESSN 1460-2075                               
JRNL        PMID   27979921                                                     
JRNL        DOI    10.15252/EMBJ.201695021                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0048                                      
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 377338                         
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) : 0.169                           
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.207                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 19990                           
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 27295                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.64                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3130                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 1459                         
REMARK   3   BIN FREE R VALUE                    : 0.3100                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 30158                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2165                                    
REMARK   3   SOLVENT ATOMS            : 2237                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.15                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.78000                                             
REMARK   3    B22 (A**2) : 3.62000                                              
REMARK   3    B33 (A**2) : -1.78000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.24000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.130         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.128         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.116         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.054         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.951                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 33567 ; 0.026 ; 0.026       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 45237 ; 2.205 ; 2.017       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  3776 ; 6.584 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1303 ;35.558 ;23.078       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  5100 ;16.469 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   131 ;16.908 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  4770 ; 0.150 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 24471 ; 0.024 ; 0.029       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 15126 ; 3.204 ; 3.415       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 18884 ; 4.485 ; 5.085       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 18441 ; 4.651 ;  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):     2 ; 7.540 ; 5.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 14                                
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A N                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     526      6                      
REMARK   3           1     N      1       N     526      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   1    A    (A):   4373 ; 0.160 ; 5.000           
REMARK   3   LOOSE THERMAL      1    A (A**2):   4373 ; 3.040 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B O                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B      1       B     229      6                      
REMARK   3           1     O      1       O     229      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   2    B    (A):   1866 ; 0.290 ; 5.000           
REMARK   3   LOOSE THERMAL      2    B (A**2):   1866 ; 5.240 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : C P                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C      1       C     272      6                      
REMARK   3           1     P      1       P     272      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   3    C    (A):   2573 ; 0.420 ; 5.000           
REMARK   3   LOOSE THERMAL      3    C (A**2):   2573 ; 3.380 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : D Q                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     D      4       D     147      6                      
REMARK   3           1     Q      4       Q     147      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   4    D    (A):   1187 ; 0.660 ; 5.000           
REMARK   3   LOOSE THERMAL      4    D (A**2):   1187 ; 4.580 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 5                                  
REMARK   3     CHAIN NAMES                    : E R                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     E      5       E     109      6                      
REMARK   3           1     R      5       R     109      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   5    E    (A):    852 ; 0.260 ; 5.000           
REMARK   3   LOOSE THERMAL      5    E (A**2):    852 ; 2.220 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 6                                  
REMARK   3     CHAIN NAMES                    : F S                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     F      1       F      99      6                      
REMARK   3           1     S      1       S      99      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   6    F    (A):    749 ; 0.780 ; 5.000           
REMARK   3   LOOSE THERMAL      6    F (A**2):    749 ; 4.480 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 7                                  
REMARK   3     CHAIN NAMES                    : G T                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     G      1       G      85      6                      
REMARK   3           1     T      1       T      85      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   7    G    (A):    704 ; 0.710 ; 5.000           
REMARK   3   LOOSE THERMAL      7    G (A**2):    704 ; 4.570 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 8                                  
REMARK   3     CHAIN NAMES                    : H U                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     H      7       H      85      6                      
REMARK   3           1     U      7       U      85      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   8    H    (A):    662 ; 0.580 ; 5.000           
REMARK   3   LOOSE THERMAL      8    H (A**2):    662 ; 8.610 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 9                                  
REMARK   3     CHAIN NAMES                    : I V                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     I      1       I      73      6                      
REMARK   3           1     V      1       V      73      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   9    I    (A):    601 ; 0.680 ; 5.000           
REMARK   3   LOOSE THERMAL      9    I (A**2):    601 ; 6.300 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 10                                 
REMARK   3     CHAIN NAMES                    : J W                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     J      1       J      59      6                      
REMARK   3           1     W      1       W      59      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL  10    J    (A):    489 ; 0.670 ; 5.000           
REMARK   3   LOOSE THERMAL     10    J (A**2):    489 ; 5.110 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 11                                 
REMARK   3     CHAIN NAMES                    : K X                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     K      6       K      54      6                      
REMARK   3           1     X      6       X      54      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL  11    K    (A):    384 ; 0.230 ; 5.000           
REMARK   3   LOOSE THERMAL     11    K (A**2):    384 ; 6.700 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 12                                 
REMARK   3     CHAIN NAMES                    : L Y                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     L      2       L      47      6                      
REMARK   3           1     Y      2       Y      47      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL  12    L    (A):    380 ; 0.310 ; 5.000           
REMARK   3   LOOSE THERMAL     12    L (A**2):    380 ; 2.560 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 13                                 
REMARK   3     CHAIN NAMES                    : M Z                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     M      1       M      43      6                      
REMARK   3           1     Z      1       Z      43      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL  13    M    (A):    335 ; 0.420 ; 5.000           
REMARK   3   LOOSE THERMAL     13    M (A**2):    335 ; 4.730 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 14                                 
REMARK   3     CHAIN NAMES                    : 1 2                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     1      0       1     105      6                      
REMARK   3           1     2      0       2     105      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL  14   NULL    (A):    869 ; 0.540 ; 5.000         
REMARK   3   LOOSE THERMAL     14   NULL (A**2):    869 ; 8.120 ;10.000         
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 28                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   608                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.4681   0.9203  33.7561              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0454 T22:   0.0234                                     
REMARK   3      T33:   0.0159 T12:   0.0248                                     
REMARK   3      T13:   0.0111 T23:   0.0131                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3642 L22:   0.1375                                     
REMARK   3      L33:   0.4092 L12:   0.0095                                     
REMARK   3      L13:  -0.0744 L23:   0.0750                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0047 S12:   0.0443 S13:   0.0499                       
REMARK   3      S21:  -0.0374 S22:  -0.0024 S23:   0.0074                       
REMARK   3      S31:  -0.0395 S32:  -0.0520 S33:  -0.0023                       
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     1        B   303                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.9593  -9.9148  27.2901              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0550 T22:   0.0623                                     
REMARK   3      T33:   0.0248 T12:   0.0303                                     
REMARK   3      T13:   0.0220 T23:  -0.0097                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5142 L22:   0.1519                                     
REMARK   3      L33:   0.4530 L12:  -0.0779                                     
REMARK   3      L13:  -0.1813 L23:   0.0798                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0153 S12:   0.0420 S13:  -0.0321                       
REMARK   3      S21:  -0.0368 S22:   0.0230 S23:  -0.0508                       
REMARK   3      S31:   0.0232 S32:   0.1012 S33:  -0.0076                       
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     3        C   311                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.3113  19.0985  62.0657              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0980 T22:   0.0315                                     
REMARK   3      T33:   0.0605 T12:   0.0057                                     
REMARK   3      T13:   0.0201 T23:  -0.0337                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2143 L22:   0.2082                                     
REMARK   3      L33:   0.5422 L12:  -0.1037                                     
REMARK   3      L13:  -0.1002 L23:   0.1519                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0145 S12:  -0.0722 S13:   0.1071                       
REMARK   3      S21:   0.0251 S22:   0.0171 S23:  -0.0318                       
REMARK   3      S31:  -0.1503 S32:   0.0157 S33:  -0.0316                       
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 :   D     4        D   201                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.9622 -11.2963  16.9191              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0708 T22:   0.0522                                     
REMARK   3      T33:   0.0271 T12:   0.0263                                     
REMARK   3      T13:  -0.0002 T23:  -0.0120                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5802 L22:   0.0992                                     
REMARK   3      L33:   0.1844 L12:   0.0080                                     
REMARK   3      L13:  -0.0810 L23:   0.0360                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0137 S12:   0.1452 S13:  -0.0466                       
REMARK   3      S21:  -0.0585 S22:  -0.0247 S23:   0.0310                       
REMARK   3      S31:  -0.0029 S32:  -0.0588 S33:   0.0110                       
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 :   E     5        E   202                          
REMARK   3    ORIGIN FOR THE GROUP (A): -38.6200 -31.0599  35.1935              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0675 T22:   0.0576                                     
REMARK   3      T33:   0.0943 T12:  -0.0290                                     
REMARK   3      T13:   0.0143 T23:   0.0154                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7936 L22:   1.0694                                     
REMARK   3      L33:   1.1455 L12:  -0.4925                                     
REMARK   3      L13:  -0.4454 L23:   0.4648                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0560 S12:  -0.2158 S13:  -0.2316                       
REMARK   3      S21:   0.0657 S22:  -0.0127 S23:   0.0621                       
REMARK   3      S31:   0.2230 S32:  -0.0138 S33:   0.0687                       
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 :   F     1        F   102                          
REMARK   3    ORIGIN FOR THE GROUP (A): -31.6217  -0.8769  60.3435              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0469 T22:   0.1775                                     
REMARK   3      T33:   0.0622 T12:   0.0070                                     
REMARK   3      T13:   0.0481 T23:   0.0086                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7078 L22:   0.8464                                     
REMARK   3      L33:   0.5555 L12:   0.4475                                     
REMARK   3      L13:   0.4228 L23:   0.5529                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0934 S12:  -0.1501 S13:   0.0280                       
REMARK   3      S21:   0.1519 S22:  -0.1305 S23:   0.1454                       
REMARK   3      S31:   0.0568 S32:  -0.2502 S33:   0.0371                       
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 :   G     1        G   103                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.4909  23.1535  67.5275              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1308 T22:   0.0767                                     
REMARK   3      T33:   0.1097 T12:  -0.0444                                     
REMARK   3      T13:   0.0077 T23:  -0.0598                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6900 L22:   0.1818                                     
REMARK   3      L33:   1.0847 L12:   0.0329                                     
REMARK   3      L13:  -0.4766 L23:  -0.1268                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0651 S12:  -0.1807 S13:   0.1002                       
REMARK   3      S21:   0.0590 S22:   0.0218 S23:  -0.0722                       
REMARK   3      S31:  -0.1773 S32:   0.2234 S33:  -0.0869                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H     7        H    85                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.8964   2.5680  44.7030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0102 T22:   0.2612                                     
REMARK   3      T33:   0.1353 T12:   0.0045                                     
REMARK   3      T13:  -0.0017 T23:  -0.0694                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7139 L22:   1.6924                                     
REMARK   3      L33:   0.5459 L12:  -0.8053                                     
REMARK   3      L13:   0.0945 L23:   0.3003                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0131 S12:  -0.1505 S13:   0.1169                       
REMARK   3      S21:   0.0734 S22:   0.1688 S23:  -0.3324                       
REMARK   3      S31:   0.0264 S32:   0.2499 S33:  -0.1557                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I     1        I   101                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.3357 -27.8270  21.1523              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1568 T22:   0.0699                                     
REMARK   3      T33:   0.1812 T12:   0.0393                                     
REMARK   3      T13:   0.0475 T23:  -0.0525                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9500 L22:   0.2651                                     
REMARK   3      L33:   0.3478 L12:   0.7190                                     
REMARK   3      L13:  -0.5375 L23:  -0.2803                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0298 S12:  -0.0771 S13:  -0.4549                       
REMARK   3      S21:  -0.0494 S22:  -0.0484 S23:  -0.1090                       
REMARK   3      S31:   0.0866 S32:   0.0781 S33:   0.0783                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   J     1        J   102                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.3222  32.5951  47.7737              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2236 T22:   0.0695                                     
REMARK   3      T33:   0.2083 T12:   0.1075                                     
REMARK   3      T13:   0.0209 T23:   0.0107                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8109 L22:   0.3797                                     
REMARK   3      L33:   1.2356 L12:  -0.0806                                     
REMARK   3      L13:  -0.3211 L23:   0.0618                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1423 S12:   0.1174 S13:   0.2593                       
REMARK   3      S21:  -0.0680 S22:   0.0010 S23:   0.0093                       
REMARK   3      S31:  -0.4200 S32:  -0.2542 S33:  -0.1433                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   K     6        K    54                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.7476  -7.2706   2.1483              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2011 T22:   0.2631                                     
REMARK   3      T33:   0.0982 T12:   0.0177                                     
REMARK   3      T13:  -0.0089 T23:  -0.0065                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3462 L22:   0.2311                                     
REMARK   3      L33:   0.4317 L12:  -0.2777                                     
REMARK   3      L13:  -0.1738 L23:   0.1047                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0860 S12:   0.1764 S13:  -0.1454                       
REMARK   3      S21:  -0.0804 S22:  -0.0994 S23:   0.1285                       
REMARK   3      S31:   0.0520 S32:  -0.2241 S33:   0.0134                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L     2        L   102                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.3662  17.5247  23.0532              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1628 T22:   0.0695                                     
REMARK   3      T33:   0.0907 T12:   0.0721                                     
REMARK   3      T13:  -0.0002 T23:   0.0529                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1565 L22:   0.1615                                     
REMARK   3      L33:   1.0173 L12:   0.1945                                     
REMARK   3      L13:  -0.3875 L23:   0.1278                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0205 S12:   0.1232 S13:   0.0960                       
REMARK   3      S21:  -0.1291 S22:  -0.0107 S23:   0.0659                       
REMARK   3      S31:  -0.2086 S32:  -0.0831 S33:   0.0312                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   M     1        M   101                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.2874  12.2816  12.3375              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1816 T22:   0.1156                                     
REMARK   3      T33:   0.0768 T12:   0.0852                                     
REMARK   3      T13:  -0.0182 T23:   0.0630                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3465 L22:   0.3915                                     
REMARK   3      L33:   1.5916 L12:   0.8792                                     
REMARK   3      L13:  -1.0150 L23:  -0.2480                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0326 S12:   0.0930 S13:   0.1266                       
REMARK   3      S21:  -0.0916 S22:   0.0028 S23:   0.0701                       
REMARK   3      S31:  -0.1763 S32:  -0.0531 S33:  -0.0354                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   N     1        N   614                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.2947  -0.9429 105.6131              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0899 T22:   0.0636                                     
REMARK   3      T33:   0.0093 T12:   0.0463                                     
REMARK   3      T13:  -0.0186 T23:  -0.0184                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3129 L22:   0.1462                                     
REMARK   3      L33:   0.5813 L12:  -0.0542                                     
REMARK   3      L13:  -0.1533 L23:   0.0959                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0223 S12:  -0.0881 S13:   0.0159                       
REMARK   3      S21:   0.0985 S22:   0.0663 S23:  -0.0329                       
REMARK   3      S31:   0.0812 S32:   0.1240 S33:  -0.0440                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   O     1        O   301                          
REMARK   3    ORIGIN FOR THE GROUP (A):  44.9092   9.6266  96.5361              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0226 T22:   0.2444                                     
REMARK   3      T33:   0.1207 T12:  -0.0031                                     
REMARK   3      T13:  -0.0322 T23:  -0.1246                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4206 L22:   0.2071                                     
REMARK   3      L33:   0.5042 L12:   0.0634                                     
REMARK   3      L13:  -0.1249 L23:  -0.0520                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0009 S12:  -0.1264 S13:   0.1140                       
REMARK   3      S21:   0.0564 S22:   0.0732 S23:  -0.1087                       
REMARK   3      S31:  -0.0503 S32:   0.2877 S33:  -0.0741                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   P     3        P   310                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.8022 -19.3536  78.1938              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1327 T22:   0.0257                                     
REMARK   3      T33:   0.0167 T12:   0.0200                                     
REMARK   3      T13:   0.0001 T23:  -0.0111                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2952 L22:   0.2616                                     
REMARK   3      L33:   0.5018 L12:   0.0322                                     
REMARK   3      L13:   0.0767 L23:   0.1343                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0043 S12:   0.0402 S13:  -0.0694                       
REMARK   3      S21:   0.0262 S22:   0.0261 S23:  -0.0160                       
REMARK   3      S31:   0.2206 S32:   0.0185 S33:  -0.0217                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Q     4        Q   201                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.1507  11.6181 126.6039              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1912 T22:   0.1353                                     
REMARK   3      T33:   0.0408 T12:   0.0326                                     
REMARK   3      T13:  -0.0252 T23:  -0.0351                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4774 L22:   0.1771                                     
REMARK   3      L33:   0.4745 L12:  -0.1356                                     
REMARK   3      L13:  -0.2486 L23:   0.0997                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0150 S12:  -0.1855 S13:   0.1184                       
REMARK   3      S21:   0.1631 S22:   0.0963 S23:  -0.0471                       
REMARK   3      S31:   0.0082 S32:   0.1707 S33:  -0.0813                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   R     5        R   109                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.4269  31.7685 124.0653              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1834 T22:   0.0315                                     
REMARK   3      T33:   0.0711 T12:   0.0641                                     
REMARK   3      T13:   0.0727 T23:   0.0399                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3984 L22:   0.9173                                     
REMARK   3      L33:   0.8568 L12:   0.2562                                     
REMARK   3      L13:  -0.2503 L23:   0.1948                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0567 S12:   0.0932 S13:   0.3228                       
REMARK   3      S21:   0.0193 S22:   0.0495 S23:   0.0815                       
REMARK   3      S31:  -0.1254 S32:  -0.1025 S33:  -0.1062                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   S     1        S   102                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.9465   1.0314 100.4757              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0805 T22:   0.1854                                     
REMARK   3      T33:   0.0858 T12:   0.0178                                     
REMARK   3      T13:   0.0145 T23:   0.0171                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1772 L22:   0.8635                                     
REMARK   3      L33:   1.5618 L12:  -0.0976                                     
REMARK   3      L13:  -0.2132 L23:   0.9963                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0314 S12:   0.0298 S13:   0.0008                       
REMARK   3      S21:   0.0226 S22:  -0.1229 S23:   0.2251                       
REMARK   3      S31:  -0.0020 S32:  -0.3545 S33:   0.1542                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   T     1        T   103                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.5906 -23.5275  64.7265              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1813 T22:   0.1206                                     
REMARK   3      T33:   0.0562 T12:   0.0732                                     
REMARK   3      T13:   0.0098 T23:  -0.0580                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2388 L22:   0.2829                                     
REMARK   3      L33:   0.5699 L12:   0.0120                                     
REMARK   3      L13:   0.4289 L23:  -0.1114                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0114 S12:   0.2675 S13:  -0.1415                       
REMARK   3      S21:  -0.0385 S22:   0.0480 S23:  -0.0265                       
REMARK   3      S31:   0.1319 S32:   0.1311 S33:  -0.0365                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   U     7        U    85                          
REMARK   3    ORIGIN FOR THE GROUP (A):  54.4694  -2.7229  68.6443              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0176 T22:   0.2729                                     
REMARK   3      T33:   0.1285 T12:   0.0009                                     
REMARK   3      T13:   0.0147 T23:  -0.0758                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7433 L22:   0.4806                                     
REMARK   3      L33:   2.4741 L12:   0.0289                                     
REMARK   3      L13:  -0.8985 L23:   0.5951                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0197 S12:   0.0522 S13:  -0.0283                       
REMARK   3      S21:  -0.0191 S22:   0.0653 S23:  -0.1311                       
REMARK   3      S31:  -0.0858 S32:   0.2743 S33:  -0.0849                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   V     1        V    73                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.8608  27.6905 107.7976              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1635 T22:   0.2830                                     
REMARK   3      T33:   0.2665 T12:  -0.0946                                     
REMARK   3      T13:  -0.0171 T23:  -0.1602                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3000 L22:   0.4629                                     
REMARK   3      L33:   0.5466 L12:  -0.6683                                     
REMARK   3      L13:  -0.7966 L23:  -0.0017                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1483 S12:  -0.0241 S13:   0.4667                       
REMARK   3      S21:   0.0618 S22:   0.0319 S23:  -0.1896                       
REMARK   3      S31:  -0.1914 S32:   0.1306 S33:  -0.1803                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   W     1        W   102                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.5854 -32.5232  99.3213              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3659 T22:   0.0626                                     
REMARK   3      T33:   0.1643 T12:  -0.0293                                     
REMARK   3      T13:   0.0217 T23:   0.0726                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0481 L22:   0.3094                                     
REMARK   3      L33:   1.0828 L12:   0.2867                                     
REMARK   3      L13:   0.2813 L23:   0.1852                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0793 S12:  -0.1862 S13:  -0.3842                       
REMARK   3      S21:   0.1370 S22:   0.0104 S23:  -0.0484                       
REMARK   3      S31:   0.4486 S32:  -0.0630 S33:  -0.0897                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   X     6        X    54                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.3456   7.3514 130.4352              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1867 T22:   0.3957                                     
REMARK   3      T33:   0.0670 T12:   0.0606                                     
REMARK   3      T13:  -0.0843 T23:  -0.1089                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3243 L22:   0.2991                                     
REMARK   3      L33:   1.2262 L12:   0.2862                                     
REMARK   3      L13:  -1.1638 L23:  -0.2447                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0894 S12:  -0.4040 S13:   0.1821                       
REMARK   3      S21:   0.1902 S22:   0.0464 S23:  -0.0653                       
REMARK   3      S31:  -0.0318 S32:   0.2276 S33:  -0.1358                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Y     2        Y   101                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.7001 -17.4810 120.4950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3577 T22:   0.1363                                     
REMARK   3      T33:   0.0671 T12:   0.1264                                     
REMARK   3      T13:   0.0170 T23:   0.0475                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4319 L22:   0.2360                                     
REMARK   3      L33:   0.5051 L12:   0.0925                                     
REMARK   3      L13:   0.1953 L23:   0.2016                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1227 S12:  -0.0252 S13:  -0.0651                       
REMARK   3      S21:   0.1662 S22:   0.1107 S23:  -0.0073                       
REMARK   3      S31:   0.2849 S32:   0.1419 S33:   0.0120                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Z     1        Z   101                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.5186 -12.3533 128.8741              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3323 T22:   0.1922                                     
REMARK   3      T33:   0.0273 T12:   0.1065                                     
REMARK   3      T13:  -0.0690 T23:   0.0186                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1927 L22:   0.7772                                     
REMARK   3      L33:   1.5808 L12:  -1.4902                                     
REMARK   3      L13:  -1.0218 L23:   0.4888                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1619 S12:  -0.2958 S13:  -0.0214                       
REMARK   3      S21:   0.2229 S22:   0.1374 S23:  -0.0344                       
REMARK   3      S31:   0.2618 S32:   0.2868 S33:   0.0245                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   1     0        1   201                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.2784  26.9975  19.8774              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4372 T22:   0.0396                                     
REMARK   3      T33:   0.3755 T12:  -0.1223                                     
REMARK   3      T13:  -0.0205 T23:  -0.0029                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1276 L22:   3.5780                                     
REMARK   3      L33:   3.1804 L12:  -0.1353                                     
REMARK   3      L13:   0.0178 L23:   0.3926                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2675 S12:   0.0343 S13:   0.9187                       
REMARK   3      S21:  -0.1766 S22:   0.1084 S23:  -0.1501                       
REMARK   3      S31:  -0.9610 S32:   0.2729 S33:   0.1591                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   2     0        2   201                          
REMARK   3    ORIGIN FOR THE GROUP (A):  62.6153 -27.2455  93.1504              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5423 T22:   0.3395                                     
REMARK   3      T33:   0.4345 T12:   0.2925                                     
REMARK   3      T13:   0.0276 T23:  -0.0679                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3449 L22:   2.2774                                     
REMARK   3      L33:   2.6393 L12:   1.2177                                     
REMARK   3      L13:   0.8388 L23:   1.2237                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0156 S12:  -0.1238 S13:  -0.6420                       
REMARK   3      S21:   0.1413 S22:  -0.1013 S23:  -0.4206                       
REMARK   3      S31:   1.0162 S32:   0.3031 S33:   0.1169                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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: U VALUES : WITH TLS ADDED                 
REMARK   4                                                                      
REMARK   4 5IY5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-MAR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000219393.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-FEB-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL44XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX300HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 397399                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : 0.09600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.93300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 2DYR AND 1HRC                                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15MM SODIUM PHOSPHATE, PH 8.0, 0.7%      
REMARK 280  FLUORINATED OCTYLMALTOSIDE, 0.2% DECYLMALTOSIDE, 3% ETHYLENE        
REMARK 280  GLYCOL, 5% PEG 4000, BATCH MODE, TEMPERATURE 277.0K                 
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       91.93600            
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                                                    
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: TETRADECAMERIC                    
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: K, L, M, 1                            
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: TETRADECAMERIC                    
REMARK 350 APPLY THE FOLLOWING TO CHAINS: N, O, P, Q, R, S, T, U, V, W,         
REMARK 350                    AND CHAINS: X, Y, Z, 2                            
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 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   NE2  HIS N   240     CE2  TYR N   244              1.34            
REMARK 500   NE2  HIS A   240     CE2  TYR A   244              1.35            
REMARK 500   OB3  CDL P   306     O    HOH P   401              1.65            
REMARK 500   O    LEU I    29     N    ALA I    32              1.71            
REMARK 500   OE2  GLU B   220     O    HOH B   401              1.73            
REMARK 500   C41  CDL T   101     O    HOH A   927              1.82            
REMARK 500   O1   CDL C   306     O    HOH C   401              1.83            
REMARK 500   O    HOH K   121     O    HOH K   122              1.84            
REMARK 500   O    HOH B   543     O    HOH H   138              1.85            
REMARK 500   O    TPO G    11     O    HOH G   201              1.87            
REMARK 500   O    HOH E   338     O    HOH E   389              1.87            
REMARK 500   ND2  ASN C   133     O    HOH C   402              1.89            
REMARK 500   O    LEU V    29     N    PHE V    31              1.91            
REMARK 500   C55  CDL G   101     O    HOH C   526              1.93            
REMARK 500   N    ILE H     8     O    HOH H   101              1.94            
REMARK 500   N    THR I     2     O    HOH I   201              1.94            
REMARK 500   C40  CDL T   101     O    HOH A   927              1.97            
REMARK 500   O    LEU I    29     CA   ALA I    32              1.98            
REMARK 500   N    ASN H    10     O    HOH H   102              1.98            
REMARK 500   O    HOH N   862     O    HOH N   863              2.00            
REMARK 500   CB2  CDL G   101     O    HOH G   244              2.00            
REMARK 500   ND2  ASN P   133     O    HOH P   402              2.02            
REMARK 500   O    MET I    26     CA   GLY I    30              2.05            
REMARK 500   O    HIS F    94     O    HOH F   201              2.06            
REMARK 500   O    HOH N   854     O    HOH N   919              2.06            
REMARK 500   O    HOH A   872     O    HOH A   929              2.10            
REMARK 500   O    MET I    26     N    GLY I    30              2.12            
REMARK 500   O    HOH B   424     O    HOH B   475              2.15            
REMARK 500   OE1  GLU R    44     O    HOH R   201              2.15            
REMARK 500   ND2  ASN N   331     O    HOH N   701              2.16            
REMARK 500   OE2  GLU O   198     O    HOH O   401              2.16            
REMARK 500   O    HOH A   760     O    HOH A   884              2.17            
REMARK 500   O    HOH C   520     O    HOH J   224              2.17            
REMARK 500   O    HOH G   251     O    HOH G   256              2.17            
REMARK 500   O    HOH R   218     O    HOH R   265              2.17            
REMARK 500   O1   CDL G   101     O    HOH G   202              2.18            
REMARK 500   O    PHE I    31     N    PHE I    34              2.18            
REMARK 500   N    LYS H     9     O    HOH H   101              2.18            
REMARK 500   N    LYS G    84     O    HOH G   203              2.19            
REMARK 500   O    LEU I    29     CB   ALA I    32              2.19            
REMARK 500   O    HOH H   146     O    HOH H   176              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   O    HOH F   266     O    HOH U   148     1455     2.11            
REMARK 500   O    HOH F   276     O    HOH U   141     1455     2.14            
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    HIS A  12   CG    HIS A  12   CD2     0.065                       
REMARK 500    GLY A  49   C     GLY A  49   O       0.106                       
REMARK 500    HIS A  61   CG    HIS A  61   CD2     0.106                       
REMARK 500    HIS A 151   CG    HIS A 151   CD2     0.059                       
REMARK 500    HIS A 233   CG    HIS A 233   CD2     0.055                       
REMARK 500    HIS A 256   CG    HIS A 256   CD2     0.067                       
REMARK 500    TRP A 275   CE2   TRP A 275   CD2     0.076                       
REMARK 500    HIS A 291   CG    HIS A 291   CD2     0.054                       
REMARK 500    HIS A 378   CG    HIS A 378   CD2     0.107                       
REMARK 500    HIS A 395   CG    HIS A 395   CD2     0.061                       
REMARK 500    TRP A 396   CE2   TRP A 396   CD2     0.089                       
REMARK 500    TRP A 473   CE2   TRP A 473   CD2     0.080                       
REMARK 500    HIS A 503   CG    HIS A 503   CD2     0.058                       
REMARK 500    HIS B  24   CG    HIS B  24   CD2     0.060                       
REMARK 500    TRP B  65   CE2   TRP B  65   CD2     0.089                       
REMARK 500    GLU B 132   CD    GLU B 132   OE2     0.090                       
REMARK 500    SER B 167   CB    SER B 167   OG     -0.105                       
REMARK 500    HIS C  70   CG    HIS C  70   CD2     0.061                       
REMARK 500    TRP C  99   CE2   TRP C  99   CD2     0.081                       
REMARK 500    TRP C 116   CE2   TRP C 116   CD2     0.090                       
REMARK 500    HIS C 148   CG    HIS C 148   CD2     0.078                       
REMARK 500    HIS C 226   CG    HIS C 226   CD2     0.066                       
REMARK 500    HIS C 232   CG    HIS C 232   CD2     0.069                       
REMARK 500    HIS C 243   CG    HIS C 243   CD2     0.058                       
REMARK 500    TRP C 259   CE2   TRP C 259   CD2     0.074                       
REMARK 500    TRP D  98   CE2   TRP D  98   CD2     0.073                       
REMARK 500    TRP D 115   CE2   TRP D 115   CD2     0.091                       
REMARK 500    TRP D 138   CE2   TRP D 138   CD2     0.075                       
REMARK 500    TRP F  71   CE2   TRP F  71   CD2     0.075                       
REMARK 500    TRP F  73   CE2   TRP F  73   CD2     0.080                       
REMARK 500    HIS F  88   CG    HIS F  88   CD2     0.067                       
REMARK 500    HIS F  94   CG    HIS F  94   CD2     0.067                       
REMARK 500    TRP G  36   CE2   TRP G  36   CD2     0.079                       
REMARK 500    HIS G  67   CG    HIS G  67   CD2     0.058                       
REMARK 500    HIS G  71   CG    HIS G  71   CD2     0.060                       
REMARK 500    ILE H   8   N     ILE H   8   CA      0.130                       
REMARK 500    LYS H   9   C     LYS H   9   O       0.126                       
REMARK 500    TRP H  72   CE2   TRP H  72   CD2     0.073                       
REMARK 500    HIS L   2   CG    HIS L   2   CD2     0.079                       
REMARK 500    HIS N  12   CG    HIS N  12   CD2     0.079                       
REMARK 500    HIS N 151   CG    HIS N 151   CD2     0.058                       
REMARK 500    HIS N 233   CG    HIS N 233   CD2     0.074                       
REMARK 500    TRP N 236   CE2   TRP N 236   CD2     0.093                       
REMARK 500    HIS N 256   CG    HIS N 256   CD2     0.055                       
REMARK 500    TRP N 275   CE2   TRP N 275   CD2     0.092                       
REMARK 500    TRP N 340   CE2   TRP N 340   CD2     0.076                       
REMARK 500    HIS N 378   CG    HIS N 378   CD2     0.070                       
REMARK 500    HIS N 395   CG    HIS N 395   CD2     0.078                       
REMARK 500    HIS N 429   CG    HIS N 429   CD2     0.062                       
REMARK 500    HIS N 503   CG    HIS N 503   CD2     0.055                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      70 BOND DEVIATIONS.                              
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    MET A  71   CG  -  SD  -  CE  ANGL. DEV. = -17.7 DEGREES          
REMARK 500    ASP A 486   CB  -  CG  -  OD1 ANGL. DEV. =   9.2 DEGREES          
REMARK 500    ASP A 486   CB  -  CG  -  OD2 ANGL. DEV. =  -8.1 DEGREES          
REMARK 500    ARG B  82   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG B  82   NE  -  CZ  -  NH2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG D  19   NE  -  CZ  -  NH2 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG D  20   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG D  20   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    LEU D  51   CB  -  CG  -  CD2 ANGL. DEV. =  11.0 DEGREES          
REMARK 500    ARG E  90   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    ARG E  90   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    LEU F  96   CB  -  CG  -  CD2 ANGL. DEV. = -11.7 DEGREES          
REMARK 500    ARG G  17   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ILE H   8   CG1 -  CB  -  CG2 ANGL. DEV. =  21.4 DEGREES          
REMARK 500    LYS H   9   CA  -  CB  -  CG  ANGL. DEV. = -21.8 DEGREES          
REMARK 500    LYS H   9   CB  -  CG  -  CD  ANGL. DEV. = -15.7 DEGREES          
REMARK 500    LYS H   9   O   -  C   -  N   ANGL. DEV. =  11.4 DEGREES          
REMARK 500    ILE I  21   CG1 -  CB  -  CG2 ANGL. DEV. = -16.8 DEGREES          
REMARK 500    MET N  71   CG  -  SD  -  CE  ANGL. DEV. = -11.0 DEGREES          
REMARK 500    ARG O  82   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    CYS S  60   O   -  C   -  N   ANGL. DEV. =  10.0 DEGREES          
REMARK 500    PRO S  83   C   -  N   -  CA  ANGL. DEV. = -10.8 DEGREES          
REMARK 500    LYS T   5   CD  -  CE  -  NZ  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    GLY T  12   N   -  CA  -  C   ANGL. DEV. =  16.9 DEGREES          
REMARK 500    ARG U  27   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ASP U  73   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    LEU Z  19   CA  -  CB  -  CG  ANGL. DEV. =  14.7 DEGREES          
REMARK 500    CYS 1  14   CA  -  CB  -  SG  ANGL. DEV. =   6.7 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    ASP A  91     -168.10   -175.18                                   
REMARK 500    GLU A 119     -134.78     46.33                                   
REMARK 500    MET A 292       20.07   -141.91                                   
REMARK 500    MET A 383      -60.68   -107.70                                   
REMARK 500    LEU A 483      -82.58    -94.72                                   
REMARK 500    GLN B  59       72.95   -113.99                                   
REMARK 500    GLU B  60      -46.93   -176.28                                   
REMARK 500    ASN B  92       79.10     62.00                                   
REMARK 500    LEU B 135       -5.99     71.66                                   
REMARK 500    ASP B 158      -98.94   -146.61                                   
REMARK 500    LYS B 171      114.17   -161.41                                   
REMARK 500    ASN C  38       56.76     39.22                                   
REMARK 500    SER C  65      -65.26   -101.90                                   
REMARK 500    GLU C 128     -116.34    -99.67                                   
REMARK 500    HIS C 232       53.54   -162.99                                   
REMARK 500    TRP C 258      -67.20   -102.37                                   
REMARK 500    LYS D   7      -44.10   -144.08                                   
REMARK 500    PRO D 106      124.63    -35.96                                   
REMARK 500    GLN D 132      -43.64   -137.48                                   
REMARK 500    PHE D 134      -80.12   -151.14                                   
REMARK 500    SER F   2      156.22    121.30                                   
REMARK 500    THR F  53     -156.90   -134.30                                   
REMARK 500    ASP F  65       -2.32     70.93                                   
REMARK 500    GLN F  95      -59.92     76.28                                   
REMARK 500    LEU F  96      -38.34     14.14                                   
REMARK 500    ALA F  97       29.77    -75.08                                   
REMARK 500    ALA G   3      -91.75    102.35                                   
REMARK 500    ALA G   4       11.61   -144.40                                   
REMARK 500    LYS G   5     -152.35    -63.92                                   
REMARK 500    ASP G   7      149.09    151.40                                   
REMARK 500    HIS G   8       13.89    159.16                                   
REMARK 500    LEU G  23      -50.30   -133.64                                   
REMARK 500    LEU G  37      -73.50   -112.64                                   
REMARK 500    HIS G  38       27.27    -66.96                                   
REMARK 500    SER G  39     -162.64   -106.84                                   
REMARK 500    HIS G  41       99.98    -59.67                                   
REMARK 500    ALA G  46      119.54    114.50                                   
REMARK 500    SER G  61       33.47    -86.54                                   
REMARK 500    ILE H   8       -0.79    105.72                                   
REMARK 500    LYS H   9     -171.32    -55.04                                   
REMARK 500    ASN H  10       11.50     88.26                                   
REMARK 500    ASP H  49      -76.40    -70.61                                   
REMARK 500    VAL H  50      -47.86    103.68                                   
REMARK 500    THR I   2      121.33     30.18                                   
REMARK 500    ALA I  32     -106.57      9.92                                   
REMARK 500    LYS M  42       93.50    -66.43                                   
REMARK 500    LEU N  48      -65.33    -95.88                                   
REMARK 500    ASP N  50     -165.74    -75.41                                   
REMARK 500    MET N  69      -75.19   -104.92                                   
REMARK 500    ASP N  91     -171.05   -173.19                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     115 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ILE H    8     LYS H    9                  144.23                    
REMARK 500 LYS H    9     ASN H   10                 -135.89                    
REMARK 500 HIS S   94     GLN S   95                 -148.09                    
REMARK 500 GLN S   95     LEU S   96                 -144.24                    
REMARK 500 ALA V   32     THR V   33                  141.37                    
REMARK 500 THR V   33     PHE V   34                 -148.42                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    HIS A 240         0.07    SIDE CHAIN                              
REMARK 500    HIS N 240         0.08    SIDE CHAIN                              
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 952        DISTANCE =  6.53 ANGSTROMS                       
REMARK 525    HOH B 593        DISTANCE =  6.23 ANGSTROMS                       
REMARK 525    HOH C 532        DISTANCE =  5.87 ANGSTROMS                       
REMARK 525    HOH C 533        DISTANCE =  6.08 ANGSTROMS                       
REMARK 525    HOH C 534        DISTANCE =  6.60 ANGSTROMS                       
REMARK 525    HOH C 535        DISTANCE =  7.22 ANGSTROMS                       
REMARK 525    HOH C 536        DISTANCE =  7.45 ANGSTROMS                       
REMARK 525    HOH C 537        DISTANCE =  8.02 ANGSTROMS                       
REMARK 525    HOH F 297        DISTANCE =  6.23 ANGSTROMS                       
REMARK 525    HOH G 260        DISTANCE =  7.69 ANGSTROMS                       
REMARK 525    HOH T 240        DISTANCE =  5.82 ANGSTROMS                       
REMARK 525    HOH T 241        DISTANCE =  6.41 ANGSTROMS                       
REMARK 525    HOH Z1016        DISTANCE =  6.12 ANGSTROMS                       
REMARK 525    HOH 1 353        DISTANCE =  6.59 ANGSTROMS                       
REMARK 525    HOH 2 328        DISTANCE =  5.86 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                              NA A 603  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  40   O                                                      
REMARK 620 2 GLU A  40   OE1  86.1                                              
REMARK 620 3 GLY A  45   O   130.9  99.1                                        
REMARK 620 4 SER A 441   O   113.8  91.2 114.8                                  
REMARK 620 5 HOH A 783   O    85.1 170.6  84.1  95.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEA A 604  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  61   NE2                                                    
REMARK 620 2 HEA A 604   NA   95.7                                              
REMARK 620 3 HEA A 604   NB   87.6  90.7                                        
REMARK 620 4 HEA A 604   NC   86.7 177.6  89.6                                  
REMARK 620 5 HEA A 604   ND   91.9  89.8 179.3  89.9                            
REMARK 620 6 HIS A 378   NE2 177.0  84.0  89.5  93.7  91.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 601  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 240   ND1                                                    
REMARK 620 2 HIS A 290   NE2 106.6                                              
REMARK 620 3 HIS A 291   NE2 145.6  97.9                                        
REMARK 620 4 PER A 606   O2   91.1 121.6  96.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 602  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 368   NE2                                                    
REMARK 620 2 ASP A 369   OD2  94.7                                              
REMARK 620 3 GLU B 198   OE1 172.5  92.8                                        
REMARK 620 4 HOH B 434   O    99.6  93.4  79.2                                  
REMARK 620 5 HOH B 436   O    88.3 173.8  84.4  91.5                            
REMARK 620 6 HOH B 531   O    94.0  87.8  87.0 166.2  86.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEA A 605  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 376   NE2                                                    
REMARK 620 2 HEA A 605   NA   89.2                                              
REMARK 620 3 HEA A 605   NB   89.6  88.9                                        
REMARK 620 4 HEA A 605   NC   94.3 176.5  91.0                                  
REMARK 620 5 HEA A 605   ND   92.9  91.3 177.4  88.7                            
REMARK 620 6 PER A 606   O1  171.3  83.5  85.5  93.0  92.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CUA B 302  CU1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 161   ND1                                                    
REMARK 620 2 CUA B 302  CU2  131.2                                              
REMARK 620 3 CYS B 196   SG  117.2  57.2                                        
REMARK 620 4 CYS B 200   SG  101.4  57.0 114.0                                  
REMARK 620 5 MET B 207   SD  103.1 123.9 114.1 105.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CUA B 302  CU2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 196   SG                                                     
REMARK 620 2 CUA B 302  CU1   57.5                                              
REMARK 620 3 GLU B 198   O    94.6 108.8                                        
REMARK 620 4 CYS B 200   SG  115.8  58.5 100.4                                  
REMARK 620 5 HIS B 204   ND1 128.8 161.9  88.4 113.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 101  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F  60   SG                                                     
REMARK 620 2 CYS F  62   SG  114.4                                              
REMARK 620 3 CYS F  82   SG  107.5 109.9                                        
REMARK 620 4 CYS F  85   SG  105.0 108.8 111.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA N 604  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU N  40   O                                                      
REMARK 620 2 GLU N  40   OE1  86.9                                              
REMARK 620 3 GLY N  45   O   131.4  97.6                                        
REMARK 620 4 SER N 441   O   116.7  84.6 111.9                                  
REMARK 620 5 HOH N 806   O    90.7 177.0  82.8  98.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEA N 605  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS N  61   NE2                                                    
REMARK 620 2 HEA N 605   NA   97.6                                              
REMARK 620 3 HEA N 605   NB   90.1  90.1                                        
REMARK 620 4 HEA N 605   NC   84.8 177.6  90.1                                  
REMARK 620 5 HEA N 605   ND   89.4  90.2 179.5  89.6                            
REMARK 620 6 HIS N 378   NE2 176.1  86.3  90.1  91.3  90.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU N 602  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS N 240   ND1                                                    
REMARK 620 2 HIS N 290   NE2 105.0                                              
REMARK 620 3 HIS N 291   NE2 145.7  97.3                                        
REMARK 620 4 PER N 607   O2   92.5 130.8  92.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG N 603  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS N 368   NE2                                                    
REMARK 620 2 ASP N 369   OD2  98.0                                              
REMARK 620 3 GLU O 198   OE1 176.0  85.3                                        
REMARK 620 4 HOH O 414   O    84.5 175.6  92.4                                  
REMARK 620 5 HOH O 512   O    96.5  89.6  85.8  86.4                            
REMARK 620 6 HOH O 445   O    93.6  93.0  83.9  90.5 169.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEA N 606  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS N 376   NE2                                                    
REMARK 620 2 HEA N 606   NA   90.6                                              
REMARK 620 3 HEA N 606   NB   91.7  89.2                                        
REMARK 620 4 HEA N 606   NC   92.9 176.5  90.9                                  
REMARK 620 5 HEA N 606   ND   90.8  91.1 177.5  88.6                            
REMARK 620 6 PER N 607   O1  170.6  80.0  88.1  96.5  89.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CUA O 301  CU1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS O 161   ND1                                                    
REMARK 620 2 CUA O 301  CU2  129.6                                              
REMARK 620 3 CYS O 196   SG  119.3  44.5                                        
REMARK 620 4 CYS O 200   SG  108.2  44.2  88.1                                  
REMARK 620 5 MET O 207   SD  105.0 124.5 119.4 116.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CUA O 301  CU2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS O 196   SG                                                     
REMARK 620 2 CUA O 301  CU1   45.8                                              
REMARK 620 3 GLU O 198   O    97.4 109.5                                        
REMARK 620 4 CYS O 200   SG   90.3  45.1 101.5                                  
REMARK 620 5 HIS O 204   ND1 142.5 157.2  91.5 123.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA P 302  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU P 236   OE1                                                    
REMARK 620 2 HOH P 492   O    98.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN S 101  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS S  62   SG                                                     
REMARK 620 2 CYS S  82   SG  107.9                                              
REMARK 620 3 CYS S  85   SG  114.7 109.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC 1 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS 1  18   NE2                                                    
REMARK 620 2 HEC 1 201   NA   88.5                                              
REMARK 620 3 HEC 1 201   NB   80.4  87.7                                        
REMARK 620 4 HEC 1 201   NC   90.0 177.5  90.2                                  
REMARK 620 5 HEC 1 201   ND   99.8  92.9 179.4  89.3                            
REMARK 620 6 MET 1  80   SD  171.6  86.1  93.0  95.2  86.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC 2 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS 2  18   NE2                                                    
REMARK 620 2 HEC 2 201   NA   80.2                                              
REMARK 620 3 HEC 2 201   NB   99.5  90.2                                        
REMARK 620 4 HEC 2 201   NC   99.9 176.2  86.1                                  
REMARK 620 5 HEC 2 201   ND   82.0  91.9 177.6  91.8                            
REMARK 620 6 MET 2  80   SD  165.2  87.5  88.7  92.9  90.2                      
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 CU A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEA A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEA A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PER A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGV A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGV A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TGL B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CUA B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CHD C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEK C 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGV C 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGV C 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CDL C 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CHD C 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 311                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TGL D 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PSC E 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO E 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN F 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO F 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CDL G 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CHD G 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO G 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO I 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CHD J 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TGL L 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMU M 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU N 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG N 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA N 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEA N 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEA N 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PER N 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TGL N 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGV N 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO N 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO N 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CUA O 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CHD P 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA P 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEK P 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGV P 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGV P 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CDL P 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CHD P 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TGL Q 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN S 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO S 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CDL T 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CHD T 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PSC V 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CHD W 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMU Z 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ACE 1 0 and GLY 1 1    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide HEM 1 201 and CYS 1    
REMARK 800  14                                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide HEM 1 201 and CYS 1    
REMARK 800  17                                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ACE 2 0 and GLY 2 1    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide HEM 2 201 and CYS 2    
REMARK 800  17                                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide HEM 2 201 and CYS 2    
REMARK 800  14                                                                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5B3S   RELATED DB: PDB                                   
DBREF  5IY5 A    1   514  UNP    P00396   COX1_BOVIN       1    514             
DBREF  5IY5 B    1   227  UNP    P68530   COX2_BOVIN       1    227             
DBREF  5IY5 C    3   261  UNP    P00415   COX3_BOVIN       3    261             
DBREF  5IY5 D    4   147  UNP    P00423   COX41_BOVIN     26    169             
DBREF  5IY5 E    5   109  UNP    P00426   COX5A_BOVIN     48    152             
DBREF  5IY5 F    1    98  UNP    P00428   COX5B_BOVIN     32    129             
DBREF  5IY5 G    1    84  UNP    P07471   CX6A2_BOVIN     13     96             
DBREF  5IY5 H    7    85  UNP    P00429   CX6B1_BOVIN      8     86             
DBREF  5IY5 I    1    73  UNP    P04038   COX6C_BOVIN      2     74             
DBREF  5IY5 J    1    58  UNP    P07470   CX7A1_BOVIN     22     79             
DBREF  5IY5 K    6    54  UNP    P13183   COX7B_BOVIN     30     78             
DBREF  5IY5 L    2    47  UNP    P00430   COX7C_BOVIN     18     63             
DBREF  5IY5 M    1    43  UNP    P10175   COX8B_BOVIN     25     67             
DBREF  5IY5 N    1   514  UNP    P00396   COX1_BOVIN       1    514             
DBREF  5IY5 O    1   227  UNP    P68530   COX2_BOVIN       1    227             
DBREF  5IY5 P    3   261  UNP    P00415   COX3_BOVIN       3    261             
DBREF  5IY5 Q    4   147  UNP    P00423   COX41_BOVIN     26    169             
DBREF  5IY5 R    5   109  UNP    P00426   COX5A_BOVIN     48    152             
DBREF  5IY5 S    1    98  UNP    P00428   COX5B_BOVIN     32    129             
DBREF  5IY5 T    1    84  UNP    P07471   CX6A2_BOVIN     13     96             
DBREF  5IY5 U    7    85  UNP    P00429   CX6B1_BOVIN      8     86             
DBREF  5IY5 V    1    73  UNP    P04038   COX6C_BOVIN      2     74             
DBREF  5IY5 W    1    58  UNP    P07470   CX7A1_BOVIN     22     79             
DBREF  5IY5 X    6    54  UNP    P13183   COX7B_BOVIN     30     78             
DBREF  5IY5 Y    2    47  UNP    P00430   COX7C_BOVIN     18     63             
DBREF  5IY5 Z    1    43  UNP    P10175   COX8B_BOVIN     25     67             
DBREF  5IY5 1    1   104  UNP    P00004   CYC_HORSE        2    105             
DBREF  5IY5 2    1   104  UNP    P00004   CYC_HORSE        2    105             
SEQADV 5IY5 ACE 1    0  UNP  P00004              ACETYLATION                    
SEQADV 5IY5 ACE 2    0  UNP  P00004              ACETYLATION                    
SEQRES   1 A  514  FME PHE ILE ASN ARG TRP LEU PHE SER THR ASN HIS LYS          
SEQRES   2 A  514  ASP ILE GLY THR LEU TYR LEU LEU PHE GLY ALA TRP ALA          
SEQRES   3 A  514  GLY MET VAL GLY THR ALA LEU SER LEU LEU ILE ARG ALA          
SEQRES   4 A  514  GLU LEU GLY GLN PRO GLY THR LEU LEU GLY ASP ASP GLN          
SEQRES   5 A  514  ILE TYR ASN VAL VAL VAL THR ALA HIS ALA PHE VAL MET          
SEQRES   6 A  514  ILE PHE PHE MET VAL MET PRO ILE MET ILE GLY GLY PHE          
SEQRES   7 A  514  GLY ASN TRP LEU VAL PRO LEU MET ILE GLY ALA PRO ASP          
SEQRES   8 A  514  MET ALA PHE PRO ARG MET ASN ASN MET SER PHE TRP LEU          
SEQRES   9 A  514  LEU PRO PRO SER PHE LEU LEU LEU LEU ALA SER SER MET          
SEQRES  10 A  514  VAL GLU ALA GLY ALA GLY THR GLY TRP THR VAL TYR PRO          
SEQRES  11 A  514  PRO LEU ALA GLY ASN LEU ALA HIS ALA GLY ALA SER VAL          
SEQRES  12 A  514  ASP LEU THR ILE PHE SER LEU HIS LEU ALA GLY VAL SER          
SEQRES  13 A  514  SER ILE LEU GLY ALA ILE ASN PHE ILE THR THR ILE ILE          
SEQRES  14 A  514  ASN MET LYS PRO PRO ALA MET SER GLN TYR GLN THR PRO          
SEQRES  15 A  514  LEU PHE VAL TRP SER VAL MET ILE THR ALA VAL LEU LEU          
SEQRES  16 A  514  LEU LEU SER LEU PRO VAL LEU ALA ALA GLY ILE THR MET          
SEQRES  17 A  514  LEU LEU THR ASP ARG ASN LEU ASN THR THR PHE PHE ASP          
SEQRES  18 A  514  PRO ALA GLY GLY GLY ASP PRO ILE LEU TYR GLN HIS LEU          
SEQRES  19 A  514  PHE TRP PHE PHE GLY HIS PRO GLU VAL TYR ILE LEU ILE          
SEQRES  20 A  514  LEU PRO GLY PHE GLY MET ILE SER HIS ILE VAL THR TYR          
SEQRES  21 A  514  TYR SER GLY LYS LYS GLU PRO PHE GLY TYR MET GLY MET          
SEQRES  22 A  514  VAL TRP ALA MET MET SER ILE GLY PHE LEU GLY PHE ILE          
SEQRES  23 A  514  VAL TRP ALA HIS HIS MET PHE THR VAL GLY MET ASP VAL          
SEQRES  24 A  514  ASP THR ARG ALA TYR PHE THR SER ALA THR MET ILE ILE          
SEQRES  25 A  514  ALA ILE PRO THR GLY VAL LYS VAL PHE SER TRP LEU ALA          
SEQRES  26 A  514  THR LEU HIS GLY GLY ASN ILE LYS TRP SER PRO ALA MET          
SEQRES  27 A  514  MET TRP ALA LEU GLY PHE ILE PHE LEU PHE THR VAL GLY          
SEQRES  28 A  514  GLY LEU THR GLY ILE VAL LEU ALA ASN SER SER LEU ASP          
SEQRES  29 A  514  ILE VAL LEU HIS ASP THR TYR TYR VAL VAL ALA HIS PHE          
SEQRES  30 A  514  HIS TYR VAL LEU SER MET GLY ALA VAL PHE ALA ILE MET          
SEQRES  31 A  514  GLY GLY PHE VAL HIS TRP PHE PRO LEU PHE SER GLY TYR          
SEQRES  32 A  514  THR LEU ASN ASP THR TRP ALA LYS ILE HIS PHE ALA ILE          
SEQRES  33 A  514  MET PHE VAL GLY VAL ASN MET THR PHE PHE PRO GLN HIS          
SEQRES  34 A  514  PHE LEU GLY LEU SER GLY MET PRO ARG ARG TYR SER ASP          
SEQRES  35 A  514  TYR PRO ASP ALA TYR THR MET TRP ASN THR ILE SER SER          
SEQRES  36 A  514  MET GLY SER PHE ILE SER LEU THR ALA VAL MET LEU MET          
SEQRES  37 A  514  VAL PHE ILE ILE TRP GLU ALA PHE ALA SER LYS ARG GLU          
SEQRES  38 A  514  VAL LEU THR VAL ASP LEU THR THR THR ASN LEU GLU TRP          
SEQRES  39 A  514  LEU ASN GLY CYS PRO PRO PRO TYR HIS THR PHE GLU GLU          
SEQRES  40 A  514  PRO THR TYR VAL ASN LEU LYS                                  
SEQRES   1 B  227  FME ALA TYR PRO MET GLN LEU GLY PHE GLN ASP ALA THR          
SEQRES   2 B  227  SER PRO ILE MET GLU GLU LEU LEU HIS PHE HIS ASP HIS          
SEQRES   3 B  227  THR LEU MET ILE VAL PHE LEU ILE SER SER LEU VAL LEU          
SEQRES   4 B  227  TYR ILE ILE SER LEU MET LEU THR THR LYS LEU THR HIS          
SEQRES   5 B  227  THR SER THR MET ASP ALA GLN GLU VAL GLU THR ILE TRP          
SEQRES   6 B  227  THR ILE LEU PRO ALA ILE ILE LEU ILE LEU ILE ALA LEU          
SEQRES   7 B  227  PRO SER LEU ARG ILE LEU TYR MET MET ASP GLU ILE ASN          
SEQRES   8 B  227  ASN PRO SER LEU THR VAL LYS THR MET GLY HIS GLN TRP          
SEQRES   9 B  227  TYR TRP SER TYR GLU TYR THR ASP TYR GLU ASP LEU SER          
SEQRES  10 B  227  PHE ASP SER TYR MET ILE PRO THR SER GLU LEU LYS PRO          
SEQRES  11 B  227  GLY GLU LEU ARG LEU LEU GLU VAL ASP ASN ARG VAL VAL          
SEQRES  12 B  227  LEU PRO MET GLU MET THR ILE ARG MET LEU VAL SER SER          
SEQRES  13 B  227  GLU ASP VAL LEU HIS SER TRP ALA VAL PRO SER LEU GLY          
SEQRES  14 B  227  LEU LYS THR ASP ALA ILE PRO GLY ARG LEU ASN GLN THR          
SEQRES  15 B  227  THR LEU MET SER SER ARG PRO GLY LEU TYR TYR GLY GLN          
SEQRES  16 B  227  CYS SER GLU ILE CYS GLY SER ASN HIS SER PHE MET PRO          
SEQRES  17 B  227  ILE VAL LEU GLU LEU VAL PRO LEU LYS TYR PHE GLU LYS          
SEQRES  18 B  227  TRP SER ALA SER MET LEU                                      
SEQRES   1 C  259  HIS GLN THR HIS ALA TYR HIS MET VAL ASN PRO SER PRO          
SEQRES   2 C  259  TRP PRO LEU THR GLY ALA LEU SER ALA LEU LEU MET THR          
SEQRES   3 C  259  SER GLY LEU THR MET TRP PHE HIS PHE ASN SER MET THR          
SEQRES   4 C  259  LEU LEU MET ILE GLY LEU THR THR ASN MET LEU THR MET          
SEQRES   5 C  259  TYR GLN TRP TRP ARG ASP VAL ILE ARG GLU SER THR PHE          
SEQRES   6 C  259  GLN GLY HIS HIS THR PRO ALA VAL GLN LYS GLY LEU ARG          
SEQRES   7 C  259  TYR GLY MET ILE LEU PHE ILE ILE SER GLU VAL LEU PHE          
SEQRES   8 C  259  PHE THR GLY PHE PHE TRP ALA PHE TYR HIS SER SER LEU          
SEQRES   9 C  259  ALA PRO THR PRO GLU LEU GLY GLY CYS TRP PRO PRO THR          
SEQRES  10 C  259  GLY ILE HIS PRO LEU ASN PRO LEU GLU VAL PRO LEU LEU          
SEQRES  11 C  259  ASN THR SER VAL LEU LEU ALA SER GLY VAL SER ILE THR          
SEQRES  12 C  259  TRP ALA HIS HIS SER LEU MET GLU GLY ASP ARG LYS HIS          
SEQRES  13 C  259  MET LEU GLN ALA LEU PHE ILE THR ILE THR LEU GLY VAL          
SEQRES  14 C  259  TYR PHE THR LEU LEU GLN ALA SER GLU TYR TYR GLU ALA          
SEQRES  15 C  259  PRO PHE THR ILE SER ASP GLY VAL TYR GLY SER THR PHE          
SEQRES  16 C  259  PHE VAL ALA THR GLY PHE HIS GLY LEU HIS VAL ILE ILE          
SEQRES  17 C  259  GLY SER THR PHE LEU ILE VAL CYS PHE PHE ARG GLN LEU          
SEQRES  18 C  259  LYS PHE HIS PHE THR SER ASN HIS HIS PHE GLY PHE GLU          
SEQRES  19 C  259  ALA ALA ALA TRP TYR TRP HIS PHE VAL ASP VAL VAL TRP          
SEQRES  20 C  259  LEU PHE LEU TYR VAL SER ILE TYR TRP TRP GLY SER              
SEQRES   1 D  144  SER VAL VAL LYS SER GLU ASP TYR ALA LEU PRO SER TYR          
SEQRES   2 D  144  VAL ASP ARG ARG ASP TYR PRO LEU PRO ASP VAL ALA HIS          
SEQRES   3 D  144  VAL LYS ASN LEU SER ALA SER GLN LYS ALA LEU LYS GLU          
SEQRES   4 D  144  LYS GLU LYS ALA SER TRP SER SER LEU SER ILE ASP GLU          
SEQRES   5 D  144  LYS VAL GLU LEU TYR ARG LEU LYS PHE LYS GLU SER PHE          
SEQRES   6 D  144  ALA GLU MET ASN ARG SER THR ASN GLU TRP LYS THR VAL          
SEQRES   7 D  144  VAL GLY ALA ALA MET PHE PHE ILE GLY PHE THR ALA LEU          
SEQRES   8 D  144  LEU LEU ILE TRP GLU LYS HIS TYR VAL TYR GLY PRO ILE          
SEQRES   9 D  144  PRO HIS THR PHE GLU GLU GLU TRP VAL ALA LYS GLN THR          
SEQRES  10 D  144  LYS ARG MET LEU ASP MET LYS VAL ALA PRO ILE GLN GLY          
SEQRES  11 D  144  PHE SER ALA LYS TRP ASP TYR ASP LYS ASN GLU TRP LYS          
SEQRES  12 D  144  LYS                                                          
SEQRES   1 E  105  HIS GLU THR ASP GLU GLU PHE ASP ALA ARG TRP VAL THR          
SEQRES   2 E  105  TYR PHE ASN LYS PRO ASP ILE ASP ALA TRP GLU LEU ARG          
SEQRES   3 E  105  LYS GLY MET ASN THR LEU VAL GLY TYR ASP LEU VAL PRO          
SEQRES   4 E  105  GLU PRO LYS ILE ILE ASP ALA ALA LEU ARG ALA CYS ARG          
SEQRES   5 E  105  ARG LEU ASN ASP PHE ALA SER ALA VAL ARG ILE LEU GLU          
SEQRES   6 E  105  VAL VAL LYS ASP LYS ALA GLY PRO HIS LYS GLU ILE TYR          
SEQRES   7 E  105  PRO TYR VAL ILE GLN GLU LEU ARG PRO THR LEU ASN GLU          
SEQRES   8 E  105  LEU GLY ILE SER THR PRO GLU GLU LEU GLY LEU ASP LYS          
SEQRES   9 E  105  VAL                                                          
SEQRES   1 F   98  ALA SER GLY GLY GLY VAL PRO THR ASP GLU GLU GLN ALA          
SEQRES   2 F   98  THR GLY LEU GLU ARG GLU VAL MET LEU ALA ALA ARG LYS          
SEQRES   3 F   98  GLY GLN ASP PRO TYR ASN ILE LEU ALA PRO LYS ALA THR          
SEQRES   4 F   98  SER GLY THR LYS GLU ASP PRO ASN LEU VAL PRO SER ILE          
SEQRES   5 F   98  THR ASN LYS ARG ILE VAL GLY CYS ILE CYS GLU GLU ASP          
SEQRES   6 F   98  ASN SER THR VAL ILE TRP PHE TRP LEU HIS LYS GLY GLU          
SEQRES   7 F   98  ALA GLN ARG CYS PRO SER CYS GLY THR HIS TYR LYS LEU          
SEQRES   8 F   98  VAL PRO HIS GLN LEU ALA HIS                                  
SEQRES   1 G   84  ALA SER ALA ALA LYS GLY ASP HIS GLY GLY TPO GLY ALA          
SEQRES   2 G   84  ARG THR TRP ARG PHE LEU THR PHE GLY LEU ALA LEU PRO          
SEQRES   3 G   84  SER VAL ALA LEU CYS THR LEU ASN SER TRP LEU HIS SER          
SEQRES   4 G   84  GLY HIS ARG GLU ARG PRO ALA PHE ILE PRO TYR HIS HIS          
SEQRES   5 G   84  LEU ARG ILE ARG THR LYS PRO PHE SER TRP GLY ASP GLY          
SEQRES   6 G   84  ASN HIS THR PHE PHE HIS ASN PRO ARG VAL ASN PRO LEU          
SEQRES   7 G   84  PRO THR GLY TYR GLU LYS                                      
SEQRES   1 H   79  LYS ILE LYS ASN TYR GLN THR ALA PRO PHE ASP SER ARG          
SEQRES   2 H   79  PHE PRO ASN GLN ASN GLN THR ARG ASN CYS TRP GLN ASN          
SEQRES   3 H   79  TYR LEU ASP PHE HIS ARG CYS GLU LYS ALA MET THR ALA          
SEQRES   4 H   79  LYS GLY GLY ASP VAL SER VAL CYS GLU TRP TYR ARG ARG          
SEQRES   5 H   79  VAL TYR LYS SER LEU CYS PRO ILE SER TRP VAL SER THR          
SEQRES   6 H   79  TRP ASP ASP ARG ARG ALA GLU GLY THR PHE PRO GLY LYS          
SEQRES   7 H   79  ILE                                                          
SEQRES   1 I   73  SAC THR ALA LEU ALA LYS PRO GLN MET ARG GLY LEU LEU          
SEQRES   2 I   73  ALA ARG ARG LEU ARG PHE HIS ILE VAL GLY ALA PHE MET          
SEQRES   3 I   73  VAL SER LEU GLY PHE ALA THR PHE TYR LYS PHE ALA VAL          
SEQRES   4 I   73  ALA GLU LYS ARG LYS LYS ALA TYR ALA ASP PHE TYR ARG          
SEQRES   5 I   73  ASN TYR ASP SER MET LYS ASP PHE GLU GLU MET ARG LYS          
SEQRES   6 I   73  ALA GLY ILE PHE GLN SER ALA LYS                              
SEQRES   1 J   58  PHE GLU ASN ARG VAL ALA GLU LYS GLN LYS LEU PHE GLN          
SEQRES   2 J   58  GLU ASP ASN GLY LEU PRO VAL HIS LEU LYS GLY GLY ALA          
SEQRES   3 J   58  THR ASP ASN ILE LEU TYR ARG VAL THR MET THR LEU CYS          
SEQRES   4 J   58  LEU GLY GLY THR LEU TYR SER LEU TYR CYS LEU GLY TRP          
SEQRES   5 J   58  ALA SER PHE PRO HIS LYS                                      
SEQRES   1 K   49  ALA PRO ASP PHE HIS ASP LYS TYR GLY ASN ALA VAL LEU          
SEQRES   2 K   49  ALA SER GLY ALA THR PHE CYS VAL ALA VAL TRP VAL TYR          
SEQRES   3 K   49  MET ALA THR GLN ILE GLY ILE GLU TRP ASN PRO SER PRO          
SEQRES   4 K   49  VAL GLY ARG VAL THR PRO LYS GLU TRP ARG                      
SEQRES   1 L   46  HIS TYR GLU GLU GLY PRO GLY LYS ASN ILE PRO PHE SER          
SEQRES   2 L   46  VAL GLU ASN LYS TRP ARG LEU LEU ALA MET MET THR LEU          
SEQRES   3 L   46  PHE PHE GLY SER GLY PHE ALA ALA PRO PHE PHE ILE VAL          
SEQRES   4 L   46  ARG HIS GLN LEU LEU LYS LYS                                  
SEQRES   1 M   43  ILE THR ALA LYS PRO ALA LYS THR PRO THR SER PRO LYS          
SEQRES   2 M   43  GLU GLN ALA ILE GLY LEU SER VAL THR PHE LEU SER PHE          
SEQRES   3 M   43  LEU LEU PRO ALA GLY TRP VAL LEU TYR HIS LEU ASP ASN          
SEQRES   4 M   43  TYR LYS LYS SER                                              
SEQRES   1 N  514  FME PHE ILE ASN ARG TRP LEU PHE SER THR ASN HIS LYS          
SEQRES   2 N  514  ASP ILE GLY THR LEU TYR LEU LEU PHE GLY ALA TRP ALA          
SEQRES   3 N  514  GLY MET VAL GLY THR ALA LEU SER LEU LEU ILE ARG ALA          
SEQRES   4 N  514  GLU LEU GLY GLN PRO GLY THR LEU LEU GLY ASP ASP GLN          
SEQRES   5 N  514  ILE TYR ASN VAL VAL VAL THR ALA HIS ALA PHE VAL MET          
SEQRES   6 N  514  ILE PHE PHE MET VAL MET PRO ILE MET ILE GLY GLY PHE          
SEQRES   7 N  514  GLY ASN TRP LEU VAL PRO LEU MET ILE GLY ALA PRO ASP          
SEQRES   8 N  514  MET ALA PHE PRO ARG MET ASN ASN MET SER PHE TRP LEU          
SEQRES   9 N  514  LEU PRO PRO SER PHE LEU LEU LEU LEU ALA SER SER MET          
SEQRES  10 N  514  VAL GLU ALA GLY ALA GLY THR GLY TRP THR VAL TYR PRO          
SEQRES  11 N  514  PRO LEU ALA GLY ASN LEU ALA HIS ALA GLY ALA SER VAL          
SEQRES  12 N  514  ASP LEU THR ILE PHE SER LEU HIS LEU ALA GLY VAL SER          
SEQRES  13 N  514  SER ILE LEU GLY ALA ILE ASN PHE ILE THR THR ILE ILE          
SEQRES  14 N  514  ASN MET LYS PRO PRO ALA MET SER GLN TYR GLN THR PRO          
SEQRES  15 N  514  LEU PHE VAL TRP SER VAL MET ILE THR ALA VAL LEU LEU          
SEQRES  16 N  514  LEU LEU SER LEU PRO VAL LEU ALA ALA GLY ILE THR MET          
SEQRES  17 N  514  LEU LEU THR ASP ARG ASN LEU ASN THR THR PHE PHE ASP          
SEQRES  18 N  514  PRO ALA GLY GLY GLY ASP PRO ILE LEU TYR GLN HIS LEU          
SEQRES  19 N  514  PHE TRP PHE PHE GLY HIS PRO GLU VAL TYR ILE LEU ILE          
SEQRES  20 N  514  LEU PRO GLY PHE GLY MET ILE SER HIS ILE VAL THR TYR          
SEQRES  21 N  514  TYR SER GLY LYS LYS GLU PRO PHE GLY TYR MET GLY MET          
SEQRES  22 N  514  VAL TRP ALA MET MET SER ILE GLY PHE LEU GLY PHE ILE          
SEQRES  23 N  514  VAL TRP ALA HIS HIS MET PHE THR VAL GLY MET ASP VAL          
SEQRES  24 N  514  ASP THR ARG ALA TYR PHE THR SER ALA THR MET ILE ILE          
SEQRES  25 N  514  ALA ILE PRO THR GLY VAL LYS VAL PHE SER TRP LEU ALA          
SEQRES  26 N  514  THR LEU HIS GLY GLY ASN ILE LYS TRP SER PRO ALA MET          
SEQRES  27 N  514  MET TRP ALA LEU GLY PHE ILE PHE LEU PHE THR VAL GLY          
SEQRES  28 N  514  GLY LEU THR GLY ILE VAL LEU ALA ASN SER SER LEU ASP          
SEQRES  29 N  514  ILE VAL LEU HIS ASP THR TYR TYR VAL VAL ALA HIS PHE          
SEQRES  30 N  514  HIS TYR VAL LEU SER MET GLY ALA VAL PHE ALA ILE MET          
SEQRES  31 N  514  GLY GLY PHE VAL HIS TRP PHE PRO LEU PHE SER GLY TYR          
SEQRES  32 N  514  THR LEU ASN ASP THR TRP ALA LYS ILE HIS PHE ALA ILE          
SEQRES  33 N  514  MET PHE VAL GLY VAL ASN MET THR PHE PHE PRO GLN HIS          
SEQRES  34 N  514  PHE LEU GLY LEU SER GLY MET PRO ARG ARG TYR SER ASP          
SEQRES  35 N  514  TYR PRO ASP ALA TYR THR MET TRP ASN THR ILE SER SER          
SEQRES  36 N  514  MET GLY SER PHE ILE SER LEU THR ALA VAL MET LEU MET          
SEQRES  37 N  514  VAL PHE ILE ILE TRP GLU ALA PHE ALA SER LYS ARG GLU          
SEQRES  38 N  514  VAL LEU THR VAL ASP LEU THR THR THR ASN LEU GLU TRP          
SEQRES  39 N  514  LEU ASN GLY CYS PRO PRO PRO TYR HIS THR PHE GLU GLU          
SEQRES  40 N  514  PRO THR TYR VAL ASN LEU LYS                                  
SEQRES   1 O  227  FME ALA TYR PRO MET GLN LEU GLY PHE GLN ASP ALA THR          
SEQRES   2 O  227  SER PRO ILE MET GLU GLU LEU LEU HIS PHE HIS ASP HIS          
SEQRES   3 O  227  THR LEU MET ILE VAL PHE LEU ILE SER SER LEU VAL LEU          
SEQRES   4 O  227  TYR ILE ILE SER LEU MET LEU THR THR LYS LEU THR HIS          
SEQRES   5 O  227  THR SER THR MET ASP ALA GLN GLU VAL GLU THR ILE TRP          
SEQRES   6 O  227  THR ILE LEU PRO ALA ILE ILE LEU ILE LEU ILE ALA LEU          
SEQRES   7 O  227  PRO SER LEU ARG ILE LEU TYR MET MET ASP GLU ILE ASN          
SEQRES   8 O  227  ASN PRO SER LEU THR VAL LYS THR MET GLY HIS GLN TRP          
SEQRES   9 O  227  TYR TRP SER TYR GLU TYR THR ASP TYR GLU ASP LEU SER          
SEQRES  10 O  227  PHE ASP SER TYR MET ILE PRO THR SER GLU LEU LYS PRO          
SEQRES  11 O  227  GLY GLU LEU ARG LEU LEU GLU VAL ASP ASN ARG VAL VAL          
SEQRES  12 O  227  LEU PRO MET GLU MET THR ILE ARG MET LEU VAL SER SER          
SEQRES  13 O  227  GLU ASP VAL LEU HIS SER TRP ALA VAL PRO SER LEU GLY          
SEQRES  14 O  227  LEU LYS THR ASP ALA ILE PRO GLY ARG LEU ASN GLN THR          
SEQRES  15 O  227  THR LEU MET SER SER ARG PRO GLY LEU TYR TYR GLY GLN          
SEQRES  16 O  227  CYS SER GLU ILE CYS GLY SER ASN HIS SER PHE MET PRO          
SEQRES  17 O  227  ILE VAL LEU GLU LEU VAL PRO LEU LYS TYR PHE GLU LYS          
SEQRES  18 O  227  TRP SER ALA SER MET LEU                                      
SEQRES   1 P  259  HIS GLN THR HIS ALA TYR HIS MET VAL ASN PRO SER PRO          
SEQRES   2 P  259  TRP PRO LEU THR GLY ALA LEU SER ALA LEU LEU MET THR          
SEQRES   3 P  259  SER GLY LEU THR MET TRP PHE HIS PHE ASN SER MET THR          
SEQRES   4 P  259  LEU LEU MET ILE GLY LEU THR THR ASN MET LEU THR MET          
SEQRES   5 P  259  TYR GLN TRP TRP ARG ASP VAL ILE ARG GLU SER THR PHE          
SEQRES   6 P  259  GLN GLY HIS HIS THR PRO ALA VAL GLN LYS GLY LEU ARG          
SEQRES   7 P  259  TYR GLY MET ILE LEU PHE ILE ILE SER GLU VAL LEU PHE          
SEQRES   8 P  259  PHE THR GLY PHE PHE TRP ALA PHE TYR HIS SER SER LEU          
SEQRES   9 P  259  ALA PRO THR PRO GLU LEU GLY GLY CYS TRP PRO PRO THR          
SEQRES  10 P  259  GLY ILE HIS PRO LEU ASN PRO LEU GLU VAL PRO LEU LEU          
SEQRES  11 P  259  ASN THR SER VAL LEU LEU ALA SER GLY VAL SER ILE THR          
SEQRES  12 P  259  TRP ALA HIS HIS SER LEU MET GLU GLY ASP ARG LYS HIS          
SEQRES  13 P  259  MET LEU GLN ALA LEU PHE ILE THR ILE THR LEU GLY VAL          
SEQRES  14 P  259  TYR PHE THR LEU LEU GLN ALA SER GLU TYR TYR GLU ALA          
SEQRES  15 P  259  PRO PHE THR ILE SER ASP GLY VAL TYR GLY SER THR PHE          
SEQRES  16 P  259  PHE VAL ALA THR GLY PHE HIS GLY LEU HIS VAL ILE ILE          
SEQRES  17 P  259  GLY SER THR PHE LEU ILE VAL CYS PHE PHE ARG GLN LEU          
SEQRES  18 P  259  LYS PHE HIS PHE THR SER ASN HIS HIS PHE GLY PHE GLU          
SEQRES  19 P  259  ALA ALA ALA TRP TYR TRP HIS PHE VAL ASP VAL VAL TRP          
SEQRES  20 P  259  LEU PHE LEU TYR VAL SER ILE TYR TRP TRP GLY SER              
SEQRES   1 Q  144  SER VAL VAL LYS SER GLU ASP TYR ALA LEU PRO SER TYR          
SEQRES   2 Q  144  VAL ASP ARG ARG ASP TYR PRO LEU PRO ASP VAL ALA HIS          
SEQRES   3 Q  144  VAL LYS ASN LEU SER ALA SER GLN LYS ALA LEU LYS GLU          
SEQRES   4 Q  144  LYS GLU LYS ALA SER TRP SER SER LEU SER ILE ASP GLU          
SEQRES   5 Q  144  LYS VAL GLU LEU TYR ARG LEU LYS PHE LYS GLU SER PHE          
SEQRES   6 Q  144  ALA GLU MET ASN ARG SER THR ASN GLU TRP LYS THR VAL          
SEQRES   7 Q  144  VAL GLY ALA ALA MET PHE PHE ILE GLY PHE THR ALA LEU          
SEQRES   8 Q  144  LEU LEU ILE TRP GLU LYS HIS TYR VAL TYR GLY PRO ILE          
SEQRES   9 Q  144  PRO HIS THR PHE GLU GLU GLU TRP VAL ALA LYS GLN THR          
SEQRES  10 Q  144  LYS ARG MET LEU ASP MET LYS VAL ALA PRO ILE GLN GLY          
SEQRES  11 Q  144  PHE SER ALA LYS TRP ASP TYR ASP LYS ASN GLU TRP LYS          
SEQRES  12 Q  144  LYS                                                          
SEQRES   1 R  105  HIS GLU THR ASP GLU GLU PHE ASP ALA ARG TRP VAL THR          
SEQRES   2 R  105  TYR PHE ASN LYS PRO ASP ILE ASP ALA TRP GLU LEU ARG          
SEQRES   3 R  105  LYS GLY MET ASN THR LEU VAL GLY TYR ASP LEU VAL PRO          
SEQRES   4 R  105  GLU PRO LYS ILE ILE ASP ALA ALA LEU ARG ALA CYS ARG          
SEQRES   5 R  105  ARG LEU ASN ASP PHE ALA SER ALA VAL ARG ILE LEU GLU          
SEQRES   6 R  105  VAL VAL LYS ASP LYS ALA GLY PRO HIS LYS GLU ILE TYR          
SEQRES   7 R  105  PRO TYR VAL ILE GLN GLU LEU ARG PRO THR LEU ASN GLU          
SEQRES   8 R  105  LEU GLY ILE SER THR PRO GLU GLU LEU GLY LEU ASP LYS          
SEQRES   9 R  105  VAL                                                          
SEQRES   1 S   98  ALA SER GLY GLY GLY VAL PRO THR ASP GLU GLU GLN ALA          
SEQRES   2 S   98  THR GLY LEU GLU ARG GLU VAL MET LEU ALA ALA ARG LYS          
SEQRES   3 S   98  GLY GLN ASP PRO TYR ASN ILE LEU ALA PRO LYS ALA THR          
SEQRES   4 S   98  SER GLY THR LYS GLU ASP PRO ASN LEU VAL PRO SER ILE          
SEQRES   5 S   98  THR ASN LYS ARG ILE VAL GLY CYS ILE CYS GLU GLU ASP          
SEQRES   6 S   98  ASN SER THR VAL ILE TRP PHE TRP LEU HIS LYS GLY GLU          
SEQRES   7 S   98  ALA GLN ARG CYS PRO SER CYS GLY THR HIS TYR LYS LEU          
SEQRES   8 S   98  VAL PRO HIS GLN LEU ALA HIS                                  
SEQRES   1 T   84  ALA SER ALA ALA LYS GLY ASP HIS GLY GLY TPO GLY ALA          
SEQRES   2 T   84  ARG THR TRP ARG PHE LEU THR PHE GLY LEU ALA LEU PRO          
SEQRES   3 T   84  SER VAL ALA LEU CYS THR LEU ASN SER TRP LEU HIS SER          
SEQRES   4 T   84  GLY HIS ARG GLU ARG PRO ALA PHE ILE PRO TYR HIS HIS          
SEQRES   5 T   84  LEU ARG ILE ARG THR LYS PRO PHE SER TRP GLY ASP GLY          
SEQRES   6 T   84  ASN HIS THR PHE PHE HIS ASN PRO ARG VAL ASN PRO LEU          
SEQRES   7 T   84  PRO THR GLY TYR GLU LYS                                      
SEQRES   1 U   79  LYS ILE LYS ASN TYR GLN THR ALA PRO PHE ASP SER ARG          
SEQRES   2 U   79  PHE PRO ASN GLN ASN GLN THR ARG ASN CYS TRP GLN ASN          
SEQRES   3 U   79  TYR LEU ASP PHE HIS ARG CYS GLU LYS ALA MET THR ALA          
SEQRES   4 U   79  LYS GLY GLY ASP VAL SER VAL CYS GLU TRP TYR ARG ARG          
SEQRES   5 U   79  VAL TYR LYS SER LEU CYS PRO ILE SER TRP VAL SER THR          
SEQRES   6 U   79  TRP ASP ASP ARG ARG ALA GLU GLY THR PHE PRO GLY LYS          
SEQRES   7 U   79  ILE                                                          
SEQRES   1 V   73  SAC THR ALA LEU ALA LYS PRO GLN MET ARG GLY LEU LEU          
SEQRES   2 V   73  ALA ARG ARG LEU ARG PHE HIS ILE VAL GLY ALA PHE MET          
SEQRES   3 V   73  VAL SER LEU GLY PHE ALA THR PHE TYR LYS PHE ALA VAL          
SEQRES   4 V   73  ALA GLU LYS ARG LYS LYS ALA TYR ALA ASP PHE TYR ARG          
SEQRES   5 V   73  ASN TYR ASP SER MET LYS ASP PHE GLU GLU MET ARG LYS          
SEQRES   6 V   73  ALA GLY ILE PHE GLN SER ALA LYS                              
SEQRES   1 W   58  PHE GLU ASN ARG VAL ALA GLU LYS GLN LYS LEU PHE GLN          
SEQRES   2 W   58  GLU ASP ASN GLY LEU PRO VAL HIS LEU LYS GLY GLY ALA          
SEQRES   3 W   58  THR ASP ASN ILE LEU TYR ARG VAL THR MET THR LEU CYS          
SEQRES   4 W   58  LEU GLY GLY THR LEU TYR SER LEU TYR CYS LEU GLY TRP          
SEQRES   5 W   58  ALA SER PHE PRO HIS LYS                                      
SEQRES   1 X   49  ALA PRO ASP PHE HIS ASP LYS TYR GLY ASN ALA VAL LEU          
SEQRES   2 X   49  ALA SER GLY ALA THR PHE CYS VAL ALA VAL TRP VAL TYR          
SEQRES   3 X   49  MET ALA THR GLN ILE GLY ILE GLU TRP ASN PRO SER PRO          
SEQRES   4 X   49  VAL GLY ARG VAL THR PRO LYS GLU TRP ARG                      
SEQRES   1 Y   46  HIS TYR GLU GLU GLY PRO GLY LYS ASN ILE PRO PHE SER          
SEQRES   2 Y   46  VAL GLU ASN LYS TRP ARG LEU LEU ALA MET MET THR LEU          
SEQRES   3 Y   46  PHE PHE GLY SER GLY PHE ALA ALA PRO PHE PHE ILE VAL          
SEQRES   4 Y   46  ARG HIS GLN LEU LEU LYS LYS                                  
SEQRES   1 Z   43  ILE THR ALA LYS PRO ALA LYS THR PRO THR SER PRO LYS          
SEQRES   2 Z   43  GLU GLN ALA ILE GLY LEU SER VAL THR PHE LEU SER PHE          
SEQRES   3 Z   43  LEU LEU PRO ALA GLY TRP VAL LEU TYR HIS LEU ASP ASN          
SEQRES   4 Z   43  TYR LYS LYS SER                                              
SEQRES   1 1  105  ACE GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN          
SEQRES   2 1  105  LYS CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS          
SEQRES   3 1  105  HIS LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG          
SEQRES   4 1  105  LYS THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA          
SEQRES   5 1  105  ASN LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU          
SEQRES   6 1  105  MET GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY          
SEQRES   7 1  105  THR LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU          
SEQRES   8 1  105  ARG GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN          
SEQRES   9 1  105  GLU                                                          
SEQRES   1 2  105  ACE GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN          
SEQRES   2 2  105  LYS CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS          
SEQRES   3 2  105  HIS LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG          
SEQRES   4 2  105  LYS THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA          
SEQRES   5 2  105  ASN LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU          
SEQRES   6 2  105  MET GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY          
SEQRES   7 2  105  THR LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU          
SEQRES   8 2  105  ARG GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN          
SEQRES   9 2  105  GLU                                                          
MODRES 5IY5 FME A    1  MET  MODIFIED RESIDUE                                   
MODRES 5IY5 FME B    1  MET  MODIFIED RESIDUE                                   
MODRES 5IY5 TPO G   11  THR  MODIFIED RESIDUE                                   
MODRES 5IY5 SAC I    1  SER  MODIFIED RESIDUE                                   
MODRES 5IY5 FME N    1  MET  MODIFIED RESIDUE                                   
MODRES 5IY5 FME O    1  MET  MODIFIED RESIDUE                                   
MODRES 5IY5 TPO T   11  THR  MODIFIED RESIDUE                                   
MODRES 5IY5 SAC V    1  SER  MODIFIED RESIDUE                                   
HET    FME  A   1      10                                                       
HET    FME  B   1      10                                                       
HET    TPO  G  11      11                                                       
HET    SAC  I   1       9                                                       
HET    FME  N   1      10                                                       
HET    FME  O   1      10                                                       
HET    TPO  T  11      11                                                       
HET    SAC  V   1       9                                                       
HET    ACE  1   0       3                                                       
HET    ACE  2   0       3                                                       
HET     CU  A 601       1                                                       
HET     MG  A 602       1                                                       
HET     NA  A 603       1                                                       
HET    HEA  A 604      69                                                       
HET    HEA  A 605      60                                                       
HET    PER  A 606       2                                                       
HET    PGV  A 607      51                                                       
HET    PGV  A 608      51                                                       
HET    TGL  B 301      63                                                       
HET    CUA  B 302       2                                                       
HET    EDO  B 303       4                                                       
HET    CHD  C 301      29                                                       
HET     NA  C 302       1                                                       
HET    PEK  C 303      53                                                       
HET    PGV  C 304      51                                                       
HET    PGV  C 305      51                                                       
HET    CDL  C 306     100                                                       
HET    CHD  C 307      29                                                       
HET    UNL  C 308      18                                                       
HET    UNL  C 309      17                                                       
HET    UNL  C 310       7                                                       
HET    EDO  C 311       4                                                       
HET    TGL  D 201      63                                                       
HET    PSC  E 201      52                                                       
HET    EDO  E 202       4                                                       
HET     ZN  F 101       1                                                       
HET    EDO  F 102       4                                                       
HET    CDL  G 101     100                                                       
HET    CHD  G 102      29                                                       
HET    EDO  G 103       4                                                       
HET    EDO  I 101       4                                                       
HET    CHD  J 101      29                                                       
HET    UNL  J 102      10                                                       
HET    TGL  L 101      63                                                       
HET    UNL  L 102      10                                                       
HET    DMU  M 101      33                                                       
HET    UNL  N 601      17                                                       
HET     CU  N 602       1                                                       
HET     MG  N 603       1                                                       
HET     NA  N 604       1                                                       
HET    HEA  N 605      69                                                       
HET    HEA  N 606      60                                                       
HET    PER  N 607       2                                                       
HET    TGL  N 608      63                                                       
HET    UNL  N 609      16                                                       
HET    UNL  N 610      18                                                       
HET    UNL  N 611      12                                                       
HET    PGV  N 612      51                                                       
HET    EDO  N 613       4                                                       
HET    EDO  N 614       4                                                       
HET    CUA  O 301       2                                                       
HET    CHD  P 301      29                                                       
HET     NA  P 302       1                                                       
HET    PEK  P 303      53                                                       
HET    PGV  P 304      51                                                       
HET    PGV  P 305      51                                                       
HET    CDL  P 306     100                                                       
HET    CHD  P 307      29                                                       
HET    UNL  P 308      20                                                       
HET    UNL  P 309      16                                                       
HET    UNL  P 310       7                                                       
HET    TGL  Q 201      63                                                       
HET     ZN  S 101       1                                                       
HET    EDO  S 102       4                                                       
HET    CDL  T 101     100                                                       
HET    UNL  T 102      18                                                       
HET    CHD  T 103      29                                                       
HET    PSC  V 101      52                                                       
HET    CHD  W 101      29                                                       
HET    UNL  W 102       9                                                       
HET    UNL  Y 101      10                                                       
HET    DMU  Z 101      33                                                       
HET    HEC  1 201      43                                                       
HET    HEC  2 201      43                                                       
HETNAM     FME N-FORMYLMETHIONINE                                               
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SAC N-ACETYL-SERINE                                                  
HETNAM     ACE ACETYL GROUP                                                     
HETNAM      CU COPPER (II) ION                                                  
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      NA SODIUM ION                                                       
HETNAM     HEA HEME-A                                                           
HETNAM     PER PEROXIDE ION                                                     
HETNAM     PGV (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)                
HETNAM   2 PGV  PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-            
HETNAM   3 PGV  OCTADEC-11-ENOATE                                               
HETNAM     TGL TRISTEAROYLGLYCEROL                                              
HETNAM     CUA DINUCLEAR COPPER ION                                             
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     CHD CHOLIC ACID                                                      
HETNAM     PEK (1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-              
HETNAM   2 PEK  [(STEAROYLOXY)METHYL]ETHYL (5E,8E,11E,14E)-ICOSA-5,8,           
HETNAM   3 PEK  11,14-TETRAENOATE                                               
HETNAM     CDL CARDIOLIPIN                                                      
HETNAM     UNL UNKNOWN LIGAND                                                   
HETNAM     PSC (7R,17E,20E)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-                  
HETNAM   2 PSC  [(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSA-          
HETNAM   3 PSC  17,20-DIEN-1-AMINIUM 4-OXIDE                                    
HETNAM      ZN ZINC ION                                                         
HETNAM     DMU DECYL-BETA-D-MALTOPYRANOSIDE                                     
HETNAM     HEC HEME C                                                           
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     PGV PHOSPHATIDYLGLYCEROL, 2-VACCENOYL-1-PALMITOYL-SN-                
HETSYN   2 PGV  GLYCEROL-3-PHOSPHOGLYCEROL                                      
HETSYN     TGL TRIACYLGLYCEROL                                                  
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     PEK PHOSPHATIDYLETHANOLAMINE, 2-ARACHIDONOYL-1-STEAROYL-SN-          
HETSYN   2 PEK  GLYCEROL-3-PHOSPHOETHANOLAMINE                                  
HETSYN     CDL DIPHOSPHATIDYL GLYCEROL; BIS-(1,2-DIACYL-SN-GLYCERO-3-           
HETSYN   2 CDL  PHOSPHO)-1',3'-SN-GLYCEROL                                      
HETSYN     PSC PHOSPHATIDYLCHOLINE, 2-LINOLEOYL-1-PALMITOYL-SN-                 
HETSYN   2 PSC  GYCEROL-3-PHOSPHOCHOLINE                                        
HETSYN     DMU DECYLMALTOSIDE                                                   
FORMUL   1  FME    4(C6 H11 N O3 S)                                             
FORMUL   7  TPO    2(C4 H10 N O6 P)                                             
FORMUL   9  SAC    2(C5 H9 N O4)                                                
FORMUL  27  ACE    2(C2 H4 O)                                                   
FORMUL  29   CU    2(CU 2+)                                                     
FORMUL  30   MG    2(MG 2+)                                                     
FORMUL  31   NA    4(NA 1+)                                                     
FORMUL  32  HEA    4(C49 H56 FE N4 O6)                                          
FORMUL  34  PER    2(O2 2-)                                                     
FORMUL  35  PGV    7(C40 H77 O10 P)                                             
FORMUL  37  TGL    5(C57 H110 O6)                                               
FORMUL  38  CUA    2(CU2)                                                       
FORMUL  39  EDO    9(C2 H6 O2)                                                  
FORMUL  40  CHD    8(C24 H40 O5)                                                
FORMUL  42  PEK    2(C43 H78 N O8 P)                                            
FORMUL  45  CDL    4(C81 H156 O17 P2 2-)                                        
FORMUL  52  PSC    2(C42 H81 N O8 P 1+)                                         
FORMUL  54   ZN    2(ZN 2+)                                                     
FORMUL  64  DMU    2(C22 H42 O11)                                               
FORMUL  01  HEC    2(C34 H34 FE N4 O4)                                          
FORMUL  03  HOH   *2237(H2 O)                                                   
HELIX    1 AA1 FME A    1  LEU A    7  1                                   7    
HELIX    2 AA2 ASN A   11  GLY A   42  1                                  32    
HELIX    3 AA3 ASP A   50  PHE A   68  1                                  19    
HELIX    4 AA4 MET A   69  ILE A   75  1                                   7    
HELIX    5 AA5 GLY A   77  ILE A   87  1                                  11    
HELIX    6 AA6 PHE A   94  LEU A  104  1                                  11    
HELIX    7 AA7 LEU A  104  VAL A  118  1                                  15    
HELIX    8 AA8 GLY A  140  MET A  171  1                                  32    
HELIX    9 AA9 SER A  177  THR A  181  5                                   5    
HELIX   10 AB1 PRO A  182  LEU A  215  1                                  34    
HELIX   11 AB2 ASP A  221  GLY A  225  5                                   5    
HELIX   12 AB3 ASP A  227  SER A  262  1                                  36    
HELIX   13 AB4 GLY A  269  GLY A  284  1                                  16    
HELIX   14 AB5 PHE A  285  ILE A  286  5                                   2    
HELIX   15 AB6 VAL A  287  MET A  292  5                                   6    
HELIX   16 AB7 ASP A  298  ILE A  312  1                                  15    
HELIX   17 AB8 ILE A  312  HIS A  328  1                                  17    
HELIX   18 AB9 SER A  335  ALA A  359  1                                  25    
HELIX   19 AC1 ASN A  360  HIS A  368  1                                   9    
HELIX   20 AC2 THR A  370  SER A  382  1                                  13    
HELIX   21 AC3 MET A  383  GLY A  402  1                                  20    
HELIX   22 AC4 ASN A  406  SER A  434  1                                  29    
HELIX   23 AC5 PRO A  444  ALA A  446  5                                   3    
HELIX   24 AC6 TYR A  447  LYS A  479  1                                  33    
HELIX   25 AC7 LEU A  487  LEU A  495  5                                   9    
HELIX   26 AC8 SER B   14  LEU B   46  1                                  33    
HELIX   27 AC9 GLU B   60  GLU B   89  1                                  30    
HELIX   28 AD1 PRO B  124  LEU B  128  5                                   5    
HELIX   29 AD2 PRO B  166  GLY B  169  5                                   4    
HELIX   30 AD3 ASN B  203  PHE B  206  5                                   4    
HELIX   31 AD4 PRO B  215  LEU B  227  1                                  13    
HELIX   32 AD5 PRO C   15  ASN C   38  1                                  24    
HELIX   33 AD6 MET C   40  THR C   66  1                                  27    
HELIX   34 AD7 THR C   72  ALA C  107  1                                  36    
HELIX   35 AD8 THR C  109  GLY C  113  5                                   5    
HELIX   36 AD9 GLU C  128  GLU C  153  1                                  26    
HELIX   37 AE1 ASP C  155  ALA C  184  1                                  30    
HELIX   38 AE2 ASP C  190  LYS C  224  1                                  35    
HELIX   39 AE3 HIS C  232  ILE C  256  1                                  25    
HELIX   40 AE4 GLU D    9  LEU D   13  5                                   5    
HELIX   41 AE5 SER D   34  GLU D   44  1                                  11    
HELIX   42 AE6 LYS D   45  ALA D   46  5                                   2    
HELIX   43 AE7 SER D   47  LEU D   51  5                                   5    
HELIX   44 AE8 SER D   52  PHE D   64  1                                  13    
HELIX   45 AE9 SER D   67  ASN D   72  1                                   6    
HELIX   46 AF1 ASN D   76  VAL D  103  1                                  28    
HELIX   47 AF2 PRO D  108  PHE D  111  5                                   4    
HELIX   48 AF3 GLU D  112  MET D  126  1                                  15    
HELIX   49 AF4 PHE D  134  ALA D  136  5                                   3    
HELIX   50 AF5 THR E    7  LYS E   21  1                                  15    
HELIX   51 AF6 ASP E   25  VAL E   37  1                                  13    
HELIX   52 AF7 GLU E   44  LEU E   58  1                                  15    
HELIX   53 AF8 ASP E   60  ALA E   75  1                                  16    
HELIX   54 AF9 GLU E   80  GLY E   97  1                                  18    
HELIX   55 AG1 THR F    8  ALA F   13  1                                   6    
HELIX   56 AG2 THR F   14  LYS F   26  1                                  13    
HELIX   57 AG3 TPO G   11  LEU G   23  1                                  13    
HELIX   58 AG4 LEU G   23  TRP G   36  1                                  14    
HELIX   59 AG5 GLN H   25  LYS H   46  1                                  22    
HELIX   60 AG6 VAL H   50  VAL H   52  5                                   3    
HELIX   61 AG7 CYS H   53  CYS H   64  1                                  12    
HELIX   62 AG8 PRO H   65  GLY H   79  1                                  15    
HELIX   63 AG9 GLY I   11  PHE I   31  1                                  21    
HELIX   64 AH1 ALA I   32  VAL I   39  1                                   8    
HELIX   65 AH2 VAL I   39  ASN I   53  1                                  15    
HELIX   66 AH3 ASP I   55  ALA I   66  1                                  12    
HELIX   67 AH4 ARG J    4  GLN J   13  1                                  10    
HELIX   68 AH5 PRO J   19  LYS J   23  5                                   5    
HELIX   69 AH6 GLY J   25  PHE J   55  1                                  31    
HELIX   70 AH7 ASP K    8  GLN K   35  1                                  28    
HELIX   71 AH8 ASN L   17  LYS L   47  1                                  31    
HELIX   72 AH9 SER M   11  HIS M   36  1                                  26    
HELIX   73 AI1 HIS M   36  LYS M   42  1                                   7    
HELIX   74 AI2 PHE N    2  LEU N    7  1                                   6    
HELIX   75 AI3 ASN N   11  GLY N   42  1                                  32    
HELIX   76 AI4 ASP N   50  PHE N   68  1                                  19    
HELIX   77 AI5 MET N   69  ILE N   75  1                                   7    
HELIX   78 AI6 GLY N   77  ILE N   87  1                                  11    
HELIX   79 AI7 PHE N   94  LEU N  104  1                                  11    
HELIX   80 AI8 LEU N  104  VAL N  118  1                                  15    
HELIX   81 AI9 GLY N  140  MET N  171  1                                  32    
HELIX   82 AJ1 SER N  177  THR N  181  5                                   5    
HELIX   83 AJ2 PRO N  182  LEU N  215  1                                  34    
HELIX   84 AJ3 ASP N  221  GLY N  225  5                                   5    
HELIX   85 AJ4 ASP N  227  SER N  262  1                                  36    
HELIX   86 AJ5 GLY N  269  GLY N  284  1                                  16    
HELIX   87 AJ6 PHE N  285  ILE N  286  5                                   2    
HELIX   88 AJ7 VAL N  287  PHE N  293  5                                   7    
HELIX   89 AJ8 ASP N  298  ILE N  312  1                                  15    
HELIX   90 AJ9 ILE N  312  HIS N  328  1                                  17    
HELIX   91 AK1 SER N  335  ASN N  360  1                                  26    
HELIX   92 AK2 ASN N  360  HIS N  368  1                                   9    
HELIX   93 AK3 THR N  370  MET N  383  1                                  14    
HELIX   94 AK4 MET N  383  GLY N  402  1                                  20    
HELIX   95 AK5 ASN N  406  SER N  434  1                                  29    
HELIX   96 AK6 PRO N  444  ALA N  446  5                                   3    
HELIX   97 AK7 TYR N  447  LYS N  479  1                                  33    
HELIX   98 AK8 LEU N  487  LEU N  495  5                                   9    
HELIX   99 AK9 SER O   14  LEU O   46  1                                  33    
HELIX  100 AL1 GLU O   60  GLU O   89  1                                  30    
HELIX  101 AL2 PRO O  124  LEU O  128  5                                   5    
HELIX  102 AL3 PRO O  166  GLY O  169  5                                   4    
HELIX  103 AL4 ASN O  203  PHE O  206  5                                   4    
HELIX  104 AL5 PRO O  215  SER O  225  1                                  11    
HELIX  105 AL6 PRO P   15  PHE P   37  1                                  23    
HELIX  106 AL7 MET P   40  THR P   66  1                                  27    
HELIX  107 AL8 THR P   72  ALA P  107  1                                  36    
HELIX  108 AL9 THR P  109  GLY P  113  5                                   5    
HELIX  109 AM1 GLU P  128  GLU P  153  1                                  26    
HELIX  110 AM2 ASP P  155  ALA P  184  1                                  30    
HELIX  111 AM3 ASP P  190  LYS P  224  1                                  35    
HELIX  112 AM4 HIS P  232  TYR P  257  1                                  26    
HELIX  113 AM5 GLU Q    9  LEU Q   13  5                                   5    
HELIX  114 AM6 SER Q   34  GLU Q   44  1                                  11    
HELIX  115 AM7 LYS Q   45  ALA Q   46  5                                   2    
HELIX  116 AM8 SER Q   47  LEU Q   51  5                                   5    
HELIX  117 AM9 SER Q   52  PHE Q   64  1                                  13    
HELIX  118 AN1 SER Q   67  ASN Q   72  1                                   6    
HELIX  119 AN2 ASN Q   76  VAL Q  103  1                                  28    
HELIX  120 AN3 PRO Q  108  PHE Q  111  5                                   4    
HELIX  121 AN4 GLU Q  112  MET Q  126  1                                  15    
HELIX  122 AN5 PHE Q  134  ALA Q  136  5                                   3    
HELIX  123 AN6 THR R    7  LYS R   21  1                                  15    
HELIX  124 AN7 ASP R   25  VAL R   37  1                                  13    
HELIX  125 AN8 GLU R   44  LEU R   58  1                                  15    
HELIX  126 AN9 ASP R   60  ALA R   75  1                                  16    
HELIX  127 AO1 GLU R   80  GLY R   97  1                                  18    
HELIX  128 AO2 THR S    8  ALA S   13  1                                   6    
HELIX  129 AO3 THR S   14  LYS S   26  1                                  13    
HELIX  130 AO4 GLY T   12  LEU T   23  1                                  12    
HELIX  131 AO5 LEU T   23  TRP T   36  1                                  14    
HELIX  132 AO6 GLN U   25  LYS U   46  1                                  22    
HELIX  133 AO7 ASP U   49  VAL U   52  5                                   4    
HELIX  134 AO8 CYS U   53  CYS U   64  1                                  12    
HELIX  135 AO9 PRO U   65  GLY U   79  1                                  15    
HELIX  136 AP1 GLY V   11  LEU V   29  1                                  19    
HELIX  137 AP2 THR V   33  VAL V   39  1                                   7    
HELIX  138 AP3 VAL V   39  ASN V   53  1                                  15    
HELIX  139 AP4 ASP V   55  ALA V   66  1                                  12    
HELIX  140 AP5 ARG W    4  GLU W   14  1                                  11    
HELIX  141 AP6 GLY W   25  PHE W   55  1                                  31    
HELIX  142 AP7 ASP X    8  ILE X   36  1                                  29    
HELIX  143 AP8 ASN Y   17  LEU Y   45  1                                  29    
HELIX  144 AP9 SER Z   11  HIS Z   36  1                                  26    
HELIX  145 AQ1 HIS Z   36  LYS Z   42  1                                   7    
HELIX  146 AQ2 ASP 1    2  CYS 1   14  1                                  13    
HELIX  147 AQ3 THR 1   49  ASN 1   54  1                                   6    
HELIX  148 AQ4 LYS 1   60  ASN 1   70  1                                  11    
HELIX  149 AQ5 ASN 1   70  ILE 1   75  1                                   6    
HELIX  150 AQ6 LYS 1   87  THR 1  102  1                                  16    
HELIX  151 AQ7 ASP 2    2  CYS 2   14  1                                  13    
HELIX  152 AQ8 THR 2   49  ASN 2   54  1                                   6    
HELIX  153 AQ9 GLU 2   61  LEU 2   68  1                                   8    
HELIX  154 AR1 ASN 2   70  ILE 2   75  1                                   6    
HELIX  155 AR2 LYS 2   87  ASN 2  103  1                                  17    
SHEET    1 AA1 3 TYR A 510  VAL A 511  0                                        
SHEET    2 AA1 3 LYS F  55  CYS F  60  1  O  GLY F  59   N  TYR A 510           
SHEET    3 AA1 3 ILE F  70  HIS F  75 -1  O  LEU F  74   N  ARG F  56           
SHEET    1 AA2 5 LEU B 116  SER B 120  0                                        
SHEET    2 AA2 5 TYR B 105  TYR B 110 -1  N  TYR B 110   O  LEU B 116           
SHEET    3 AA2 5 LEU B  95  HIS B 102 -1  N  LYS B  98   O  GLU B 109           
SHEET    4 AA2 5 ILE B 150  SER B 156  1  O  ARG B 151   N  LEU B  95           
SHEET    5 AA2 5 ASN B 180  LEU B 184 -1  O  LEU B 184   N  ILE B 150           
SHEET    1 AA3 3 VAL B 142  PRO B 145  0                                        
SHEET    2 AA3 3 PRO B 208  VAL B 214  1  O  VAL B 210   N  VAL B 142           
SHEET    3 AA3 3 GLY B 190  GLN B 195 -1  N  TYR B 192   O  LEU B 211           
SHEET    1 AA4 2 HIS B 161  VAL B 165  0                                        
SHEET    2 AA4 2 LEU B 170  ALA B 174 -1  O  THR B 172   N  TRP B 163           
SHEET    1 AA5 2 TRP D 138  ASP D 139  0                                        
SHEET    2 AA5 2 GLU D 144  TRP D 145 -1  O  GLU D 144   N  ASP D 139           
SHEET    1 AA6 3 ASN F  47  SER F  51  0                                        
SHEET    2 AA6 3 HIS F  88  PRO F  93  1  O  LYS F  90   N  VAL F  49           
SHEET    3 AA6 3 GLN F  80  ARG F  81 -1  N  GLN F  80   O  TYR F  89           
SHEET    1 AA7 3 TYR N 510  VAL N 511  0                                        
SHEET    2 AA7 3 LYS S  55  CYS S  60  1  O  ILE S  57   N  TYR N 510           
SHEET    3 AA7 3 ILE S  70  HIS S  75 -1  O  ILE S  70   N  CYS S  60           
SHEET    1 AA8 5 LEU O 116  SER O 120  0                                        
SHEET    2 AA8 5 TYR O 105  TYR O 110 -1  N  TYR O 110   O  LEU O 116           
SHEET    3 AA8 5 LEU O  95  HIS O 102 -1  N  LYS O  98   O  GLU O 109           
SHEET    4 AA8 5 ILE O 150  SER O 156  1  O  ARG O 151   N  VAL O  97           
SHEET    5 AA8 5 ASN O 180  LEU O 184 -1  O  LEU O 184   N  ILE O 150           
SHEET    1 AA9 3 VAL O 142  PRO O 145  0                                        
SHEET    2 AA9 3 PRO O 208  VAL O 214  1  O  VAL O 210   N  VAL O 142           
SHEET    3 AA9 3 GLY O 190  GLN O 195 -1  N  GLY O 194   O  ILE O 209           
SHEET    1 AB1 2 HIS O 161  VAL O 165  0                                        
SHEET    2 AB1 2 LEU O 170  ALA O 174 -1  O  ALA O 174   N  HIS O 161           
SHEET    1 AB2 2 TRP Q 138  ASP Q 139  0                                        
SHEET    2 AB2 2 GLU Q 144  TRP Q 145 -1  O  GLU Q 144   N  ASP Q 139           
SHEET    1 AB3 3 ASN S  47  SER S  51  0                                        
SHEET    2 AB3 3 HIS S  88  PRO S  93  1  O  LYS S  90   N  VAL S  49           
SHEET    3 AB3 3 GLN S  80  ARG S  81 -1  N  GLN S  80   O  TYR S  89           
SSBOND   1 CYS H   29    CYS H   64                          1555   1555  2.09  
SSBOND   2 CYS H   39    CYS H   53                          1555   1555  2.05  
SSBOND   3 CYS O  196    CYS O  200                          1555   1555  2.82  
SSBOND   4 CYS U   29    CYS U   64                          1555   1555  2.10  
SSBOND   5 CYS U   39    CYS U   53                          1555   1555  2.09  
LINK         C   FME A   1                 N   PHE A   2     1555   1555  1.33  
LINK         O   GLU A  40                NA    NA A 603     1555   1555  2.28  
LINK         OE1 GLU A  40                NA    NA A 603     1555   1555  2.27  
LINK         O   GLY A  45                NA    NA A 603     1555   1555  2.28  
LINK         NE2 HIS A  61                FE   HEA A 604     1555   1555  1.88  
LINK         ND1 HIS A 240                CU    CU A 601     1555   1555  2.03  
LINK         NE2 HIS A 290                CU    CU A 601     1555   1555  2.09  
LINK         NE2 HIS A 291                CU    CU A 601     1555   1555  1.94  
LINK         NE2 HIS A 368                MG    MG A 602     1555   1555  2.04  
LINK         OD2 ASP A 369                MG    MG A 602     1555   1555  2.10  
LINK         NE2 HIS A 376                FE   HEA A 605     1555   1555  2.04  
LINK         NE2 HIS A 378                FE   HEA A 604     1555   1555  1.92  
LINK         O   SER A 441                NA    NA A 603     1555   1555  2.29  
LINK         C   FME B   1                 N   ALA B   2     1555   1555  1.34  
LINK         ND1 HIS B 161                CU1  CUA B 302     1555   1555  2.08  
LINK         SG  CYS B 196                CU2  CUA B 302     1555   1555  2.31  
LINK         SG  CYS B 196                CU1  CUA B 302     1555   1555  2.32  
LINK         O   GLU B 198                CU2  CUA B 302     1555   1555  2.26  
LINK         OE1 GLU B 198                MG    MG A 602     1555   1555  2.14  
LINK         SG  CYS B 200                CU2  CUA B 302     1555   1555  2.32  
LINK         SG  CYS B 200                CU1  CUA B 302     1555   1555  2.35  
LINK         ND1 HIS B 204                CU2  CUA B 302     1555   1555  1.98  
LINK         SD  MET B 207                CU1  CUA B 302     1555   1555  2.37  
LINK         OE1 GLU C 236                NA    NA C 302     1555   1555  2.17  
LINK         SG  CYS F  60                ZN    ZN F 101     1555   1555  2.33  
LINK         SG  CYS F  62                ZN    ZN F 101     1555   1555  2.38  
LINK         SG  CYS F  82                ZN    ZN F 101     1555   1555  2.36  
LINK         SG  CYS F  85                ZN    ZN F 101     1555   1555  2.37  
LINK         C   GLY G  10                 N   TPO G  11     1555   1555  1.34  
LINK         C   TPO G  11                 N   GLY G  12     1555   1555  1.34  
LINK         C   SAC I   1                 N   THR I   2     1555   1555  1.34  
LINK         C   FME N   1                 N   PHE N   2     1555   1555  1.32  
LINK         O   GLU N  40                NA    NA N 604     1555   1555  2.32  
LINK         OE1 GLU N  40                NA    NA N 604     1555   1555  2.24  
LINK         O   GLY N  45                NA    NA N 604     1555   1555  2.27  
LINK         NE2 HIS N  61                FE   HEA N 605     1555   1555  1.94  
LINK         ND1 HIS N 240                CU    CU N 602     1555   1555  2.05  
LINK         NE2 HIS N 290                CU    CU N 602     1555   1555  2.04  
LINK         NE2 HIS N 291                CU    CU N 602     1555   1555  1.97  
LINK         NE2 HIS N 368                MG    MG N 603     1555   1555  2.00  
LINK         OD2 ASP N 369                MG    MG N 603     1555   1555  2.18  
LINK         NE2 HIS N 376                FE   HEA N 606     1555   1555  2.05  
LINK         NE2 HIS N 378                FE   HEA N 605     1555   1555  1.95  
LINK         O   SER N 441                NA    NA N 604     1555   1555  2.29  
LINK         C   FME O   1                 N   ALA O   2     1555   1555  1.34  
LINK         ND1 HIS O 161                CU1  CUA O 301     1555   1555  2.06  
LINK         SG  CYS O 196                CU1  CUA O 301     1555   1555  2.04  
LINK         SG  CYS O 196                CU2  CUA O 301     1555   1555  1.99  
LINK         O   GLU O 198                CU2  CUA O 301     1555   1555  2.14  
LINK         OE1 GLU O 198                MG    MG N 603     1555   1555  2.12  
LINK         SG  CYS O 200                CU1  CUA O 301     1555   1555  2.01  
LINK         SG  CYS O 200                CU2  CUA O 301     1555   1555  1.98  
LINK         ND1 HIS O 204                CU2  CUA O 301     1555   1555  2.01  
LINK         SD  MET O 207                CU1  CUA O 301     1555   1555  2.30  
LINK         OE1 GLU P 236                NA    NA P 302     1555   1555  2.21  
LINK         SG  CYS S  62                ZN    ZN S 101     1555   1555  2.42  
LINK         SG  CYS S  82                ZN    ZN S 101     1555   1555  2.17  
LINK         SG  CYS S  85                ZN    ZN S 101     1555   1555  2.13  
LINK         C   GLY T  10                 N   TPO T  11     1555   1555  1.35  
LINK         C   TPO T  11                 N   GLY T  12     1555   1555  1.35  
LINK         C   SAC V   1                 N   THR V   2     1555   1555  1.34  
LINK         C   ACE 1   0                 N   GLY 1   1     1555   1555  1.32  
LINK         SG  CYS 1  14                 CAB HEC 1 201     1555   1555  1.90  
LINK         NE2 HIS 1  18                FE   HEC 1 201     1555   1555  2.09  
LINK         SD  MET 1  80                FE   HEC 1 201     1555   1555  2.56  
LINK         C   ACE 2   0                 N   GLY 2   1     1555   1555  1.35  
LINK         SG  CYS 2  14                 CAB HEC 2 201     1555   1555  1.90  
LINK         SG  CYS 2  17                 CAC HEC 2 201     1555   1555  1.94  
LINK         NE2 HIS 2  18                FE   HEC 2 201     1555   1555  2.62  
LINK         SD  MET 2  80                FE   HEC 2 201     1555   1555  2.56  
LINK        CU    CU A 601                 O2  PER A 606     1555   1555  2.44  
LINK        MG    MG A 602                 O   HOH B 434     1555   1555  2.23  
LINK        MG    MG A 602                 O   HOH B 436     1555   1555  2.32  
LINK        MG    MG A 602                 O   HOH B 531     1555   1555  2.30  
LINK        NA    NA A 603                 O   HOH A 783     1555   1555  2.33  
LINK        FE   HEA A 605                 O1  PER A 606     1555   1555  2.08  
LINK        CU    CU N 602                 O2  PER N 607     1555   1555  2.33  
LINK        MG    MG N 603                 O   HOH O 414     1555   1555  2.37  
LINK        MG    MG N 603                 O   HOH O 512     1555   1555  2.31  
LINK        MG    MG N 603                 O   HOH O 445     1555   1555  2.31  
LINK        NA    NA N 604                 O   HOH N 806     1555   1555  2.34  
LINK        FE   HEA N 606                 O1  PER N 607     1555   1555  2.09  
LINK        NA    NA P 302                 O   HOH P 492     1555   1555  2.04  
LINK         SG  CYS 1  17                 CAC HEC 1 201     1555   1555  2.06  
CISPEP   1 PRO A  130    PRO A  131          0        -4.63                     
CISPEP   2 CYS A  498    PRO A  499          0        -9.10                     
CISPEP   3 GLN B  103    TRP B  104          0        -4.09                     
CISPEP   4 TRP C  116    PRO C  117          0        -2.86                     
CISPEP   5 PRO N  130    PRO N  131          0         0.31                     
CISPEP   6 CYS N  498    PRO N  499          0       -12.41                     
CISPEP   7 GLN O  103    TRP O  104          0        -9.40                     
CISPEP   8 TRP P  116    PRO P  117          0        -1.29                     
SITE     1 AC1  4 HIS A 240  HIS A 290  HIS A 291  PER A 606                    
SITE     1 AC2  6 HIS A 368  ASP A 369  GLU B 198  HOH B 434                    
SITE     2 AC2  6 HOH B 436  HOH B 531                                          
SITE     1 AC3  4 GLU A  40  GLY A  45  SER A 441  HOH A 783                    
SITE     1 AC4 31 ALA A  24  GLY A  27  MET A  28  THR A  31                    
SITE     2 AC4 31 SER A  34  ILE A  37  ARG A  38  TYR A  54                    
SITE     3 AC4 31 VAL A  58  HIS A  61  ALA A  62  MET A  65                    
SITE     4 AC4 31 VAL A  70  ILE A  73  GLY A 125  TRP A 126                    
SITE     5 AC4 31 TYR A 371  PHE A 377  HIS A 378  SER A 382                    
SITE     6 AC4 31 VAL A 386  PHE A 393  MET A 417  PHE A 425                    
SITE     7 AC4 31 GLN A 428  ARG A 438  ARG A 439  MET A 468                    
SITE     8 AC4 31 HOH A 735  HOH A 740  HOH A 749                               
SITE     1 AC5 31 TRP A 126  TRP A 236  VAL A 243  TYR A 244                    
SITE     2 AC5 31 HIS A 290  HIS A 291  THR A 309  ILE A 312                    
SITE     3 AC5 31 ALA A 313  GLY A 317  GLY A 352  GLY A 355                    
SITE     4 AC5 31 ILE A 356  LEU A 358  ALA A 359  ASP A 364                    
SITE     5 AC5 31 HIS A 368  VAL A 373  HIS A 376  PHE A 377                    
SITE     6 AC5 31 VAL A 380  LEU A 381  ARG A 438  PER A 606                    
SITE     7 AC5 31 HOH A 750  HOH A 767  HOH A 772  HOH A 791                    
SITE     8 AC5 31 ILE B  34  PRO B  69  ILE B  72                               
SITE     1 AC6  5 HIS A 240  VAL A 243  HIS A 291   CU A 601                    
SITE     2 AC6  5 HEA A 605                                                     
SITE     1 AC7  8 ASN A 406  TRP A 409  HOH A 701  HOH A 833                    
SITE     2 AC7  8 PHE D  87  PHE K   9  GLN M  15  HOH M 216                    
SITE     1 AC8 15 PHE A  94  PRO A  95  ARG A  96  MET A  97                    
SITE     2 AC8 15 HOH A 748  HOH A 759  HIS C   9  ASN C  50                    
SITE     3 AC8 15 TRP C  57  TRP C  58  GLU C  64  HIS C  71                    
SITE     4 AC8 15 GLY C  82  PEK C 303  PGV C 304                               
SITE     1 AC9  7 ASN A 422  LEU A 433  LEU B  28  PHE B  32                    
SITE     2 AC9  7 SER B  35  SER B  36  HOH B 465                               
SITE     1 AD1  6 HIS B 161  CYS B 196  GLU B 198  CYS B 200                    
SITE     2 AD1  6 HIS B 204  MET B 207                                          
SITE     1 AD2  8 TYR A 447  ALA B   2  GLN B  10  LEU B 136                    
SITE     2 AD2  8 PRO B 166  TYR B 193  HOH B 471  HOH B 483                    
SITE     1 AD3 10 HIS A 233  ASP A 300  THR A 301  TYR A 304                    
SITE     2 AD3 10 TRP C  99  HIS C 103  PGV C 305  HOH C 497                    
SITE     3 AD3 10 HOH C 500  CDL T 101                                          
SITE     1 AD4  3 HIS C 148  HIS C 232  GLU C 236                               
SITE     1 AD5 18 HIS A 151  VAL A 155  PGV A 608  TYR C 181                    
SITE     2 AD5 18 TYR C 182  ALA C 184  PHE C 186  THR C 187                    
SITE     3 AD5 18 ILE C 188  PHE C 198  GLY C 202  TRP G  62                    
SITE     4 AD5 18 THR G  68  PHE G  69  PHE G  70  HIS G  71                    
SITE     5 AD5 18 ASN G  76  HOH G 226                                          
SITE     1 AD6 20 PGV A 608  MET C  51  MET C  54  VAL C  61                    
SITE     2 AD6 20 SER C  65  THR C  66  GLU C  90  ILE C 210                    
SITE     3 AD6 20 PHE C 214  ARG C 221  HIS C 226  PHE C 227                    
SITE     4 AD6 20 HIS C 231  PHE C 233  GLY C 234  CDL C 306                    
SITE     5 AD6 20 HOH C 436  HOH C 438  HOH C 485  HOH F 227                    
SITE     1 AD7 14 ASP A 298  HOH B 529  TRP C  99  TYR C 102                    
SITE     2 AD7 14 HIS C 103  ALA C 107  CHD C 301  HOH C 427                    
SITE     3 AD7 14 HOH C 431  HOH C 502  ASN H  22  TRP P 258                    
SITE     4 AD7 14 CDL T 101  HOH T 241                                          
SITE     1 AD8 19 MET C  51  LEU C  52  MET C  54  TYR C  55                    
SITE     2 AD8 19 ARG C  59  ARG C  63  PHE C  67  THR C 213                    
SITE     3 AD8 19 PHE C 220  LYS C 224  HIS C 226  PGV C 304                    
SITE     4 AD8 19 HOH C 401  HOH C 406  HOH C 470  HOH C 471                    
SITE     5 AD8 19 HOH C 534  HOH C 536  LYS J   8                               
SITE     1 AD9  4 ARG C 156  GLN C 161  PHE C 164  PHE J   1                    
SITE     1 AE1  4 GLU C 111  HOH C 420  HOH C 506  HOH H 128                    
SITE     1 AE2 11 TRP A 334  MET A 339  GLY A 343  LYS B  49                    
SITE     2 AE2 11 ARG D  73  GLU D  77  TRP D  78  HOH D 303                    
SITE     3 AE2 11 HOH D 306  HOH D 392  HIS I  20                               
SITE     1 AE3 17 PHE A 321  LEU B  37  ILE B  41  HIS B  52                    
SITE     2 AE3 17 MET B  56  ASP B  57  GLU B  60  VAL B  61                    
SITE     3 AE3 17 TRP B  65  LEU B  68  HOH B 554  HIS E   5                    
SITE     4 AE3 17 GLU E   6  THR E   7  ASP E   8  PHE E  11                    
SITE     5 AE3 17 HOH I 221                                                     
SITE     1 AE4  4 GLU E 102  HOH E 301  HOH E 307  HOH E 391                    
SITE     1 AE5  4 CYS F  60  CYS F  62  CYS F  82  CYS F  85                    
SITE     1 AE6  5 HIS C 231  HOH C 424  ASP F   9  GLU F  17                    
SITE     2 AE6  5 HOH F 221                                                     
SITE     1 AE7 19 VAL C 142  HOH C 526  LEU G  23  SER G  27                    
SITE     2 AE7 19 LEU G  30  CYS G  31  ASN G  34  LEU G  37                    
SITE     3 AE7 19 HIS G  38  HOH G 202  HOH G 244  TYR N 304                    
SITE     4 AE7 19 SER N 307  ILE N 311  ALA O  77  LEU O  78                    
SITE     5 AE7 19 LEU O  81  TYR O  85  HOH O 465                               
SITE     1 AE8  9 ARG G  14  ARG G  17  GLY G  22  HOH G 208                    
SITE     2 AE8  9 HOH G 216  MET N 271  TRP N 275  GLU O  62                    
SITE     3 AE8  9 THR O  63                                                     
SITE     1 AE9  6 GLY C 120  ALA G  46  PHE G  47  ILE G  48                    
SITE     2 AE9  6 ARG G  54  HOH G 229                                          
SITE     1 AF1  3 TYR I  54  ASP I  55  GLU I  62                               
SITE     1 AF2  5 TYR J  32  MET J  36  THR J  37  LEU J  40                    
SITE     2 AF2  5 HOH J 221                                                     
SITE     1 AF3 12 THR A  17  TRP A  25  PHE A 400  PRO L  12                    
SITE     2 AF3 12 PHE L  13  SER L  14  ARG L  20  MET L  25                    
SITE     3 AF3 12 LEU L  27  PHE L  28  PHE L  29  SER L  31                    
SITE     1 AF4  8 TRP D  98  LEU M  28  GLY M  31  TRP M  32                    
SITE     2 AF4  8 LEU M  34  TYR M  35  HIS M  36  HOH M 211                    
SITE     1 AF5  4 HIS N 240  HIS N 290  HIS N 291  PER N 607                    
SITE     1 AF6  6 HIS N 368  ASP N 369  GLU O 198  HOH O 414                    
SITE     2 AF6  6 HOH O 445  HOH O 512                                          
SITE     1 AF7  4 GLU N  40  GLY N  45  SER N 441  HOH N 806                    
SITE     1 AF8 32 ALA N  24  MET N  28  THR N  31  SER N  34                    
SITE     2 AF8 32 ILE N  37  ARG N  38  TYR N  54  VAL N  58                    
SITE     3 AF8 32 HIS N  61  ALA N  62  MET N  65  VAL N  70                    
SITE     4 AF8 32 GLY N 125  TRP N 126  TYR N 371  PHE N 377                    
SITE     5 AF8 32 HIS N 378  SER N 382  VAL N 386  MET N 390                    
SITE     6 AF8 32 PHE N 393  PHE N 425  GLN N 428  ARG N 438                    
SITE     7 AF8 32 ARG N 439  TYR N 440  VAL N 465  MET N 468                    
SITE     8 AF8 32 ILE N 472  HOH N 743  HOH N 766  HOH N 794                    
SITE     1 AF9 28 TRP N 126  TRP N 236  VAL N 243  TYR N 244                    
SITE     2 AF9 28 HIS N 290  HIS N 291  THR N 309  ILE N 312                    
SITE     3 AF9 28 THR N 316  GLY N 317  GLY N 352  GLY N 355                    
SITE     4 AF9 28 LEU N 358  ALA N 359  ASP N 364  HIS N 368                    
SITE     5 AF9 28 VAL N 373  HIS N 376  PHE N 377  VAL N 380                    
SITE     6 AF9 28 LEU N 381  ARG N 438  PER N 607  HOH N 715                    
SITE     7 AF9 28 HOH N 745  HOH N 785  HOH N 834  ILE O  34                    
SITE     1 AG1  5 HIS N 240  VAL N 243  HIS N 291   CU N 602                    
SITE     2 AG1  5 HEA N 606                                                     
SITE     1 AG2 10 PHE N 346  TYR N 379  ASN N 422  HIS N 429                    
SITE     2 AG2 10 PHE N 430  LEU N 433  LEU O  28  PHE O  32                    
SITE     3 AG2 10 SER O  35  LEU O  39                                          
SITE     1 AG3 16 PHE N  94  PRO N  95  ARG N  96  MET N  97                    
SITE     2 AG3 16 HOH N 730  HOH N 772  HIS P   9  ASN P  50                    
SITE     3 AG3 16 MET P  54  TRP P  57  TRP P  58  GLU P  64                    
SITE     4 AG3 16 HIS P  71  GLY P  82  PHE P  93  PEK P 303                    
SITE     1 AG4  6 TYR N 260  TYR N 261  HIS N 395  HOH N 716                    
SITE     2 AG4  6 HOH N 731  ILE Z   1                                          
SITE     1 AG5  1 LEU P  22                                                     
SITE     1 AG6  6 HIS O 161  CYS O 196  GLU O 198  CYS O 200                    
SITE     2 AG6  6 HIS O 204  MET O 207                                          
SITE     1 AG7  7 HIS N 233  ASP N 300  THR N 301  TYR N 304                    
SITE     2 AG7  7 TRP P  99  HIS P 103  PGV P 305                               
SITE     1 AG8  4 HIS P 148  HIS P 232  GLU P 236  HOH P 492                    
SITE     1 AG9 20 HIS N 151  VAL N 155  PGV N 612  TYR P 181                    
SITE     2 AG9 20 TYR P 182  ALA P 184  PHE P 186  THR P 187                    
SITE     3 AG9 20 ILE P 188  PHE P 198  GLY P 202  PHE P 203                    
SITE     4 AG9 20 GLY P 205  HOH P 457  TRP T  62  THR T  68                    
SITE     5 AG9 20 PHE T  69  PHE T  70  HIS T  71  ASN T  76                    
SITE     1 AH1 19 MET P  51  TRP P  58  VAL P  61  SER P  65                    
SITE     2 AH1 19 THR P  66  PHE P  86  ILE P 210  PHE P 214                    
SITE     3 AH1 19 ARG P 221  HIS P 226  PHE P 227  HIS P 231                    
SITE     4 AH1 19 HIS P 232  PHE P 233  GLY P 234  HOH P 418                    
SITE     5 AH1 19 HOH P 426  HOH P 476  HOH S 211                               
SITE     1 AH2  8 TRP P  99  HIS P 103  ALA P 107  CHD P 301                    
SITE     2 AH2  8 HOH P 481  ASN U  24  HOH U 103  HOH U 136                    
SITE     1 AH3 16 MET P  51  LEU P  52  TYR P  55  ARG P  59                    
SITE     2 AH3 16 ILE P  62  PHE P  67  THR P 213  ILE P 216                    
SITE     3 AH3 16 VAL P 217  PHE P 220  LYS P 224  HIS P 226                    
SITE     4 AH3 16 HOH P 401  HOH P 403  HOH P 411  HOH P 425                    
SITE     1 AH4  5 ARG P 156  PHE P 164  LEU P 223  HOH P 504                    
SITE     2 AH4  5 PHE W   1                                                     
SITE     1 AH5 11 TRP N 334  PHE N 414  HOH N 737  ILE O  42                    
SITE     2 AH5 11 THR Q  75  GLU Q  77  TRP Q  78  ILE Q  89                    
SITE     3 AH5 11 HOH Q 310  ARG V  16  HIS V  20                               
SITE     1 AH6  4 CYS S  60  CYS S  62  CYS S  82  CYS S  85                    
SITE     1 AH7  5 HOH P 467  ASP S   9  GLU S  17  HOH S 221                    
SITE     2 AH7  5 HOH S 241                                                     
SITE     1 AH8 19 PHE A 282  ILE A 286  ASP A 300  TYR A 304                    
SITE     2 AH8 19 ILE A 311  HOH A 911  HOH A 927  ALA B  70                    
SITE     3 AH8 19 ILE B  74  LEU B  78  LEU B  81  HOH B 533                    
SITE     4 AH8 19 CHD C 301  PGV C 305  LEU P 127  SER T  27                    
SITE     5 AH8 19 CYS T  31  ASN T  34  HIS T  38                               
SITE     1 AH9 11 MET A 271  TRP A 275  THR B  63  THR B  66                    
SITE     2 AH9 11 ARG T  14  ARG T  17  PHE T  18  PHE T  21                    
SITE     3 AH9 11 GLY T  22  HOH T 205  HOH T 215                               
SITE     1 AI1 18 PHE N 268  PHE N 321  ALA N 325  HIS N 328                    
SITE     2 AI1 18 MET O  45  HIS O  52  MET O  56  ASP O  57                    
SITE     3 AI1 18 VAL O  61  TRP O  65  LEU O  68  HIS R   5                    
SITE     4 AI1 18 ASP R   8  ARG V  10  LEU V  17  ARG V  18                    
SITE     5 AI1 18 HOH V 201  HOH V 212                                          
SITE     1 AI2  7 ILE N   3  PHE N   8  TYR W  32  ARG W  33                    
SITE     2 AI2  7 MET W  36  LEU W  40  HOH W 204                               
SITE     1 AI3  9 LEU N  35  PHE N 459  TRP Q  98  HOH Q 359                    
SITE     2 AI3  9 LEU Z  27  LEU Z  28  GLY Z  31  TRP Z  32                    
SITE     3 AI3  9 HIS Z  36                                                     
SITE     1 AI4  5 ASP 1   2  VAL 1   3  GLU 1  92  ASP 1  93                    
SITE     2 AI4  5 ALA 1  96                                                     
SITE     1 AI5 21 PHE 1  10  LYS 1  13  ALA 1  15  GLN 1  16                    
SITE     2 AI5 21 CYS 1  17  HIS 1  18  THR 1  28  PRO 1  30                    
SITE     3 AI5 21 THR 1  40  GLY 1  41  TYR 1  48  THR 1  49                    
SITE     4 AI5 21 ASN 1  52  TRP 1  59  TYR 1  67  LEU 1  68                    
SITE     5 AI5 21 THR 1  78  LYS 1  79  MET 1  80  ILE 1  81                    
SITE     6 AI5 21 PHE 1  82                                                     
SITE     1 AI6 21 LYS 1  13  CYS 1  14  ALA 1  15  GLN 1  16                    
SITE     2 AI6 21 HIS 1  18  THR 1  28  GLY 1  29  PRO 1  30                    
SITE     3 AI6 21 THR 1  40  GLY 1  41  TYR 1  48  THR 1  49                    
SITE     4 AI6 21 ASN 1  52  TRP 1  59  TYR 1  67  LEU 1  68                    
SITE     5 AI6 21 THR 1  78  LYS 1  79  MET 1  80  ILE 1  81                    
SITE     6 AI6 21 PHE 1  82                                                     
SITE     1 AI7  1 ASP 2   2                                                     
SITE     1 AI8 21 LYS 2  13  CYS 2  14  ALA 2  15  GLN 2  16                    
SITE     2 AI8 21 HIS 2  18  THR 2  28  GLY 2  29  LEU 2  35                    
SITE     3 AI8 21 THR 2  40  PHE 2  46  TYR 2  48  THR 2  49                    
SITE     4 AI8 21 ASN 2  52  TRP 2  59  LEU 2  68  THR 2  78                    
SITE     5 AI8 21 LYS 2  79  MET 2  80  ILE 2  81  PHE 2  82                    
SITE     6 AI8 21 HOH 2 317                                                     
SITE     1 AI9 21 PHE 2  10  LYS 2  13  ALA 2  15  GLN 2  16                    
SITE     2 AI9 21 CYS 2  17  HIS 2  18  THR 2  28  LEU 2  35                    
SITE     3 AI9 21 THR 2  40  PHE 2  46  TYR 2  48  THR 2  49                    
SITE     4 AI9 21 ASN 2  52  TRP 2  59  LEU 2  68  THR 2  78                    
SITE     5 AI9 21 LYS 2  79  MET 2  80  ILE 2  81  PHE 2  82                    
SITE     6 AI9 21 HOH 2 317                                                     
CRYST1  113.290  183.872  148.929  90.00 102.12  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      0.008827  0.000000  0.001896        0.00000                         
SCALE2      0.000000  0.005439  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006868        0.00000                         
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   2  0.831972 -0.010747 -0.554713       40.34046    1                    
MTRIX2   2 -0.007647 -0.999940  0.007905       -0.83419    1                    
MTRIX3   2 -0.554765 -0.002335 -0.832004      132.57309    1                    
MTRIX1   3  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   3  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   3  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   4  0.831330 -0.003219 -0.555770       40.30796    1                    
MTRIX2   4 -0.002600 -0.999995  0.001903       -0.35593    1                    
MTRIX3   4 -0.555773 -0.000137 -0.831334      132.49832    1                    
MTRIX1   5  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   5  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   5  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   6  0.832054 -0.010883 -0.554587       40.27772    1                    
MTRIX2   6 -0.010091 -0.999939  0.004483       -0.51278    1                    
MTRIX3   6 -0.554602  0.001866 -0.832114      132.60425    1                    
MTRIX1   7  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   7  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   7  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   8  0.836256 -0.021573 -0.547914       39.45975    1                    
MTRIX2   8 -0.015942 -0.999760  0.015033       -1.30309    1                    
MTRIX3   8 -0.548107 -0.003837 -0.836399      132.80051    1                    
MTRIX1   9  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   9  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   9  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1  10  0.833846 -0.029407 -0.551213       40.22459    1                    
MTRIX2  10 -0.019535 -0.999526  0.023773       -2.48523    1                    
MTRIX3  10 -0.551651 -0.009055 -0.834026      132.64902    1                    
MTRIX1  11  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2  11  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3  11  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1  12  0.821611 -0.008057 -0.569992       42.05060    1                    
MTRIX2  12  0.000334 -0.999893  0.014616       -1.31192    1                    
MTRIX3  12 -0.570048 -0.012199 -0.821521      131.52568    1                    
MTRIX1  13  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2  13  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3  13  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1  14  0.831893 -0.034914 -0.553837       39.39650    1                    
MTRIX2  14 -0.022329 -0.999317  0.029458       -1.81845    1                    
MTRIX3  14 -0.554487 -0.012139 -0.832104      132.51799    1                    
MTRIX1  15  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2  15  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3  15  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1  16  0.799820  0.022778 -0.599808       45.55457    1                    
MTRIX2  16  0.020668 -0.999732 -0.010405       -0.59304    1                    
MTRIX3  16 -0.599885 -0.004075 -0.800076      132.28874    1                    
MTRIX1  17  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2  17  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3  17  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1  18  0.835980 -0.019898 -0.548399       39.52701    1                    
MTRIX2  18 -0.007473 -0.999663  0.024879       -2.57625    1                    
MTRIX3  18 -0.548709 -0.016700 -0.835847      133.01914    1                    
MTRIX1  19  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2  19  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3  19  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1  20  0.825431  0.005776 -0.564474       41.86627    1                    
MTRIX2  20  0.003982 -0.999982 -0.004409        0.43834    1                    
MTRIX3  20 -0.564489  0.001391 -0.825439      131.75992    1                    
MTRIX1  21  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2  21  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3  21  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1  22  0.834354 -0.021583 -0.550807       39.91309    1                    
MTRIX2  22 -0.011835 -0.999704  0.021245       -2.22789    1                    
MTRIX3  22 -0.551103 -0.011207 -0.834362      132.75342    1                    
MTRIX1  23  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2  23  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3  23  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1  24  0.832704 -0.009258 -0.553641       40.26115    1                    
MTRIX2  24 -0.007505 -0.999957  0.005432       -0.47406    1                    
MTRIX3  24 -0.553667 -0.000368 -0.832738      132.63144    1                    
MTRIX1  25  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2  25  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3  25  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1  26  0.829286 -0.035633 -0.557687       40.64849    1                    
MTRIX2  26 -0.011914 -0.998865  0.046107       -5.73668    1                    
MTRIX3  26 -0.558697 -0.031591 -0.828770      131.89973    1                    
MTRIX1  27  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2  27  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3  27  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1  28  0.830096 -0.035940 -0.556461       40.14864    1                    
MTRIX2  28 -0.049126 -0.998754 -0.008776        3.66861    1                    
MTRIX3  28 -0.555452  0.034621 -0.830827      132.95052    1                    
HETATM    1  N   FME A   1     -24.488  26.901  38.498  1.00 44.73           N  
ANISOU    1  N   FME A   1     5762   5360   5871   1290     75    169       N  
HETATM    2  CN  FME A   1     -23.323  26.777  39.122  1.00 52.15           C  
ANISOU    2  CN  FME A   1     6729   6260   6825   1234     93    149       C  
HETATM    3  O1  FME A   1     -22.506  27.578  39.402  1.00 64.42           O  
ANISOU    3  O1  FME A   1     8324   7741   8409   1226    111    146       O  
HETATM    4  CA  FME A   1     -24.965  25.468  38.469  1.00 47.48           C  
ANISOU    4  CA  FME A   1     6060   5799   6179   1257     58    157       C  
HETATM    5  CB  FME A   1     -26.304  25.084  37.878  1.00 52.44           C  
ANISOU    5  CB  FME A   1     6640   6503   6778   1298     35    168       C  
HETATM    6  CG  FME A   1     -26.929  24.109  38.863  1.00 71.87           C  
ANISOU    6  CG  FME A   1     9050   9033   9222   1271     34    122       C  
HETATM    7  SD  FME A   1     -27.583  24.979  40.275  1.00 88.01           S  
ANISOU    7  SD  FME A   1    11081  11061  11297   1310     51     73       S  
HETATM    8  CE  FME A   1     -26.535  24.752  41.711  1.00 70.51           C  
ANISOU    8  CE  FME A   1     8882   8809   9098   1246     77     27       C  
HETATM    9  C   FME A   1     -23.875  24.566  37.925  1.00 44.06           C  
ANISOU    9  C   FME A   1     5644   5368   5728   1192     57    175       C  
HETATM   10  O   FME A   1     -23.483  23.630  38.594  1.00 40.78           O  
ANISOU   10  O   FME A   1     5213   4978   5301   1139     61    146       O  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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