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PDBsum entry 3a12

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
3a12
Jmol
Contents
Protein chains
(+ 4 more) 437 a.a.
Ligands
CAP ×10
Metals
_MG ×10
Waters ×2306
HEADER    LYASE                                   25-MAR-09   3A12
TITLE     CRYSTAL STRUCTURE OF TYPE III RUBISCO COMPLEXED WITH 2-CABP
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE;
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J;
COMPND   4 SYNONYM: RUBISCO;
COMPND   5 EC: 4.1.1.39;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: PYROCOCCUS KODAKARAENSIS;
SOURCE   3 ORGANISM_COMMON: THERMOCOCCUS KODAKARAENSIS;
SOURCE   4 ORGANISM_TAXID: 69014;
SOURCE   5 STRAIN: KOD1;
SOURCE   6 GENE: RBCL, TK2290;
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3)PLYSS;
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET-21A(+)
KEYWDS    RIBULOSE-1, 5-BISPHOSPHATE CARBOXYLASE/OXYGENASE, RUBISCO, LYASE,
KEYWDS   2 CARBON DIOXIDE FIXATION, MAGNESIUM, METAL-BINDING, MONOOXYGENASE,
KEYWDS   3 OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Y.NISHITANI,M.FUJIHASHI,T.DOI,S.YOSHIDA,H.ATOMI,T.IMANAKA,K.MIKI
REVDAT   2   02-FEB-11 3A12    1       JRNL
REVDAT   1   07-APR-10 3A12    0
JRNL        AUTH   Y.NISHITANI,S.YOSHIDA,M.FUJIHASHI,K.KITAGAWA,T.DOI,H.ATOMI,
JRNL        AUTH 2 T.IMANAKA,K.MIKI
JRNL        TITL   STRUCTURE-BASED CATALYTIC OPTIMIZATION OF A TYPE III RUBISCO
JRNL        TITL 2 FROM A HYPERTHERMOPHILE
JRNL        REF    J.BIOL.CHEM.                  V. 285 39339 2010
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   20926376
JRNL        DOI    10.1074/JBC.M110.147587
REMARK   2
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0066
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.39
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5
REMARK   3   NUMBER OF REFLECTIONS             : 257731
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) : 0.201
REMARK   3   R VALUE            (WORKING SET) : 0.199
REMARK   3   FREE R VALUE                     : 0.244
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 13630
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) : 2.30
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 18587
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.22
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2490
REMARK   3   BIN FREE R VALUE SET COUNT          : 975
REMARK   3   BIN FREE R VALUE                    : 0.2990
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 34125
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 220
REMARK   3   SOLVENT ATOMS            : 2306
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 26.40
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.08
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 4.52000
REMARK   3    B22 (A**2) : -2.27000
REMARK   3    B33 (A**2) : -2.25000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.268
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.216
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.146
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.948
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.927
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 35219 ; 0.006 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 47835 ; 0.995 ; 1.958
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  4354 ; 5.230 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1607 ;29.821 ;23.491
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  5588 ;14.192 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   220 ;19.538 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  5065 ; 0.068 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 27118 ; 0.004 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 21648 ; 0.421 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 34454 ; 0.822 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 13571 ; 1.274 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 13381 ; 2.142 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3A12 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-MAR-09.
REMARK 100 THE RCSB ID CODE IS RCSB028677.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 04-JUN-08
REMARK 200  TEMPERATURE           (KELVIN) : 95
REMARK 200  PH                             : 6.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SPRING-8
REMARK 200  BEAMLINE                       : BL41XU
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 271962
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300
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     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.10500
REMARK 200   FOR THE DATA SET  : 15.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.34
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.37900
REMARK 200   FOR SHELL         : 3.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1GEH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 60.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M ACETATE, 0.1M CACL2, 5% PEG6000,
REMARK 280  10% MPD, PH6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       86.64350
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      123.18850
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       86.64350
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      123.18850
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 62500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 124640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -382.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D, E, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      173.28700
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 62190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 124360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -384.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, H, I, J, G
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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH G 592  LIES ON A SPECIAL POSITION.
REMARK 375      HOH I 652  LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A     1
REMARK 465     VAL A     2
REMARK 465     GLU A     3
REMARK 465     LYS A     4
REMARK 465     PHE A     5
REMARK 465     ASP A     6
REMARK 465     THR A     7
REMARK 465     MET B     1
REMARK 465     VAL B     2
REMARK 465     GLU B     3
REMARK 465     LYS B     4
REMARK 465     PHE B     5
REMARK 465     ASP B     6
REMARK 465     MET C     1
REMARK 465     VAL C     2
REMARK 465     GLU C     3
REMARK 465     LYS C     4
REMARK 465     PHE C     5
REMARK 465     ASP C     6
REMARK 465     MET D     1
REMARK 465     VAL D     2
REMARK 465     GLU D     3
REMARK 465     LYS D     4
REMARK 465     PHE D     5
REMARK 465     ASP D     6
REMARK 465     THR D     7
REMARK 465     ILE D     8
REMARK 465     MET E     1
REMARK 465     VAL E     2
REMARK 465     GLU E     3
REMARK 465     LYS E     4
REMARK 465     PHE E     5
REMARK 465     ASP E     6
REMARK 465     LYS E   426
REMARK 465     THR E   427
REMARK 465     MET F     1
REMARK 465     VAL F     2
REMARK 465     GLU F     3
REMARK 465     LYS F     4
REMARK 465     PHE F     5
REMARK 465     ASP F     6
REMARK 465     THR F     7
REMARK 465     ILE F     8
REMARK 465     LEU F    58
REMARK 465     MET G     1
REMARK 465     VAL G     2
REMARK 465     GLU G     3
REMARK 465     LYS G     4
REMARK 465     PHE G     5
REMARK 465     ASP G     6
REMARK 465     THR G     7
REMARK 465     ILE G     8
REMARK 465     MET H     1
REMARK 465     VAL H     2
REMARK 465     GLU H     3
REMARK 465     LYS H     4
REMARK 465     PHE H     5
REMARK 465     ASP H     6
REMARK 465     THR H     7
REMARK 465     MET I     1
REMARK 465     VAL I     2
REMARK 465     GLU I     3
REMARK 465     LYS I     4
REMARK 465     PHE I     5
REMARK 465     ASP I     6
REMARK 465     THR I     7
REMARK 465     ILE I     8
REMARK 465     MET J     1
REMARK 465     VAL J     2
REMARK 465     GLU J     3
REMARK 465     LYS J     4
REMARK 465     PHE J     5
REMARK 465     ASP J     6
REMARK 465     THR J     7
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     ILE A   8    CG1  CG2  CD1
REMARK 470     ASP A  10    CG   OD1  OD2
REMARK 470     GLU A  18    CG   CD   OE1  OE2
REMARK 470     THR A  57    OG1  CG2
REMARK 470     LEU A  58    CG   CD1  CD2
REMARK 470     TYR A  59    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     GLU A  65    CG   CD   OE1  OE2
REMARK 470     GLU A 144    CG   CD   OE1  OE2
REMARK 470     LYS A 148    CG   CD   CE   NZ
REMARK 470     LYS A 153    CG   CD   CE   NZ
REMARK 470     LYS A 175    CG   CD   CE   NZ
REMARK 470     GLU A 203    CG   CD   OE1  OE2
REMARK 470     GLU A 346    CG   CD   OE1  OE2
REMARK 470     LYS A 429    CG   CD   CE   NZ
REMARK 470     THR B   7    OG1  CG2
REMARK 470     ILE B   8    CG1  CG2  CD1
REMARK 470     ASP B  10    CG   OD1  OD2
REMARK 470     THR B  57    OG1  CG2
REMARK 470     LEU B  58    CG   CD1  CD2
REMARK 470     GLU B  65    CG   CD   OE1  OE2
REMARK 470     GLU B 144    CG   CD   OE1  OE2
REMARK 470     GLU B 203    CG   CD   OE1  OE2
REMARK 470     GLU B 346    CG   CD   OE1  OE2
REMARK 470     GLU B 380    CG   CD   OE1  OE2
REMARK 470     THR C   7    OG1  CG2
REMARK 470     ASP C  10    CG   OD1  OD2
REMARK 470     GLU C  35    CG   CD   OE1  OE2
REMARK 470     GLU C  65    CG   CD   OE1  OE2
REMARK 470     GLU C 144    CG   CD   OE1  OE2
REMARK 470     LYS C 153    CG   CD   CE   NZ
REMARK 470     LYS C 211    CG   CD   CE   NZ
REMARK 470     GLU C 346    CG   CD   OE1  OE2
REMARK 470     GLU C 380    CG   CD   OE1  OE2
REMARK 470     ASP C 422    CG   OD1  OD2
REMARK 470     GLU C 423    CG   CD   OE1  OE2
REMARK 470     LYS C 429    CG   CD   CE   NZ
REMARK 470     ASP D  10    CG   OD1  OD2
REMARK 470     LEU D  58    CG   CD1  CD2
REMARK 470     GLU D  65    CG   CD   OE1  OE2
REMARK 470     LYS D 211    CG   CD   CE   NZ
REMARK 470     LYS D 343    CG   CD   CE   NZ
REMARK 470     GLU D 346    CG   CD   OE1  OE2
REMARK 470     LYS D 429    CG   CD   CE   NZ
REMARK 470     THR E   7    OG1  CG2
REMARK 470     ILE E   8    CG1  CG2  CD1
REMARK 470     GLU E  65    CG   CD   OE1  OE2
REMARK 470     GLU E 144    CG   CD   OE1  OE2
REMARK 470     LYS E 153    CG   CD   CE   NZ
REMARK 470     LYS E 211    CG   CD   CE   NZ
REMARK 470     GLU E 346    CG   CD   OE1  OE2
REMARK 470     GLU E 380    CG   CD   OE1  OE2
REMARK 470     GLU E 423    CG   CD   OE1  OE2
REMARK 470     LYS E 429    CG   CD   CE   NZ
REMARK 470     GLU E 436    CG   CD   OE1  OE2
REMARK 470     VAL E 441    CG1  CG2
REMARK 470     ASP F  10    CG   OD1  OD2
REMARK 470     TYR F  17    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     GLU F  18    CG   CD   OE1  OE2
REMARK 470     LYS F  21    CG   CD   CE   NZ
REMARK 470     GLU F  40    CG   CD   OE1  OE2
REMARK 470     THR F  57    OG1  CG2
REMARK 470     TYR F  59    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     GLU F  65    CG   CD   OE1  OE2
REMARK 470     GLU F 144    CG   CD   OE1  OE2
REMARK 470     LYS F 148    CG   CD   CE   NZ
REMARK 470     LYS F 153    CG   CD   CE   NZ
REMARK 470     GLU F 203    CG   CD   OE1  OE2
REMARK 470     LYS F 343    CG   CD   CE   NZ
REMARK 470     GLU F 346    CG   CD   OE1  OE2
REMARK 470     GLU F 380    CG   CD   OE1  OE2
REMARK 470     GLU F 423    CG   CD   OE1  OE2
REMARK 470     LYS F 426    CG   CD   CE   NZ
REMARK 470     LYS F 429    CG   CD   CE   NZ
REMARK 470     ASP G  10    CG   OD1  OD2
REMARK 470     LEU G  58    CG   CD1  CD2
REMARK 470     GLU G  65    CG   CD   OE1  OE2
REMARK 470     GLU G 144    CG   CD   OE1  OE2
REMARK 470     LYS G 175    CG   CD   CE   NZ
REMARK 470     GLU G 203    CG   CD   OE1  OE2
REMARK 470     LYS G 211    CG   CD   CE   NZ
REMARK 470     GLU G 346    CG   CD   OE1  OE2
REMARK 470     GLU G 380    CG   CD   OE1  OE2
REMARK 470     LYS G 429    CG   CD   CE   NZ
REMARK 470     ILE H   8    CG1  CG2  CD1
REMARK 470     ASP H  10    CG   OD1  OD2
REMARK 470     GLU H  65    CG   CD   OE1  OE2
REMARK 470     LYS H 153    CG   CD   CE   NZ
REMARK 470     LYS H 211    CG   CD   CE   NZ
REMARK 470     GLU H 346    CG   CD   OE1  OE2
REMARK 470     GLU H 380    CG   CD   OE1  OE2
REMARK 470     ASP H 422    CG   OD1  OD2
REMARK 470     GLU H 423    CG   CD   OE1  OE2
REMARK 470     LYS H 429    CG   CD   CE   NZ
REMARK 470     ASP I  10    CG   OD1  OD2
REMARK 470     TYR I  59    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     GLU I  65    CG   CD   OE1  OE2
REMARK 470     LYS I 148    CG   CD   CE   NZ
REMARK 470     LYS I 211    CG   CD   CE   NZ
REMARK 470     GLU I 423    CG   CD   OE1  OE2
REMARK 470     ILE J   8    CG1  CG2  CD1
REMARK 470     GLU J  65    CG   CD   OE1  OE2
REMARK 470     GLU J 144    CG   CD   OE1  OE2
REMARK 470     LYS J 153    CG   CD   CE   NZ
REMARK 470     SER J 358    OG
REMARK 470     GLN J 376    CG   CD   OE1  NE2
REMARK 470     GLU J 380    CG   CD   OE1  OE2
REMARK 470     GLN J 410    CG   CD   OE1  NE2
REMARK 470     GLU J 423    CG   CD   OE1  OE2
REMARK 470     LYS J 426    CG   CD   CE   NZ
REMARK 470     THR J 427    OG1  CG2
REMARK 470     LYS J 429    CG   CD   CE   NZ
REMARK 470     VAL J 441    CG1  CG2
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    SER A  51      -97.16   -142.26
REMARK 500    ALA A 109       40.54   -140.14
REMARK 500    THR A 195     -106.12   -122.75
REMARK 500    ASN A 200       79.40   -163.21
REMARK 500    ALA A 232     -177.74   -176.08
REMARK 500    MET A 284      -19.12     94.46
REMARK 500    TYR A 357     -116.60     51.48
REMARK 500    ASP B  14       87.07   -153.84
REMARK 500    SER B  51      -96.64   -135.39
REMARK 500    ALA B 109       37.24   -142.62
REMARK 500    THR B 195     -110.66   -117.69
REMARK 500    ASN B 200       83.68   -161.41
REMARK 500    MET B 284      -20.50     94.80
REMARK 500    TYR B 357     -113.90     48.66
REMARK 500    SER C  51      -93.20   -137.59
REMARK 500    ASP C 154      -44.49   -133.30
REMARK 500    THR C 195     -110.68   -114.49
REMARK 500    ASN C 200       84.01   -164.15
REMARK 500    ALA C 232     -175.10   -177.46
REMARK 500    MET C 284      -16.54     92.64
REMARK 500    ALA C 318       30.12     70.37
REMARK 500    TYR C 357     -114.06     52.82
REMARK 500    SER D  51     -111.15   -141.23
REMARK 500    THR D  56     -154.48   -114.45
REMARK 500    ALA D 109       35.19   -145.39
REMARK 500    ASP D 154      -40.53   -130.71
REMARK 500    THR D 195     -108.09   -118.67
REMARK 500    ASN D 200       81.83   -160.87
REMARK 500    ALA D 232     -178.73   -174.26
REMARK 500    MET D 284      -15.94     93.08
REMARK 500    TYR D 357     -114.45     62.27
REMARK 500    SER E  51     -107.85   -142.28
REMARK 500    ALA E 109       39.46   -140.61
REMARK 500    THR E 195     -104.08   -112.97
REMARK 500    SER E 196       58.09   -142.86
REMARK 500    ASN E 200       80.78   -157.40
REMARK 500    ALA E 232     -173.20   -179.35
REMARK 500    ALA E 283      128.72    -39.88
REMARK 500    MET E 284      -22.10     97.56
REMARK 500    TYR E 357     -116.70     46.67
REMARK 500    ASN E 374       26.63   -148.76
REMARK 500    SER F  51      -96.38   -142.89
REMARK 500    THR F  54      144.31   -172.10
REMARK 500    PRO F  60      100.26    -27.59
REMARK 500    HIS F  78      105.54   -177.57
REMARK 500    ALA F 109       38.40   -145.89
REMARK 500    THR F 195     -104.61   -121.32
REMARK 500    ASN F 200       80.14   -160.52
REMARK 500    ALA F 232     -178.88   -171.66
REMARK 500    MET F 284      -20.99     97.22
REMARK 500
REMARK 500 THIS ENTRY HAS      88 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 445  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX A 189   OQ2
REMARK 620 2 ASP A 191   OD1  88.7
REMARK 620 3 GLU A 192   OE1  85.3  95.0
REMARK 620 4 CAP A 446   O3   84.7 173.4  83.9
REMARK 620 5 CAP A 446   O2   86.0 104.6 158.3  75.4
REMARK 620 6 CAP A 446   O7  161.6  99.4 110.1  87.0  76.1
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG B 445  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX B 189   OQ2
REMARK 620 2 ASP B 191   OD1  83.0
REMARK 620 3 GLU B 192   OE1  88.2  85.9
REMARK 620 4 CAP B 446   O7  170.6  99.3 101.0
REMARK 620 5 CAP B 446   O2   94.0 110.1 163.9  76.6
REMARK 620 6 CAP B 446   O3   89.1 169.0  86.1  89.7  78.0
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG C 445  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX C 189   OQ2
REMARK 620 2 ASP C 191   OD1  87.2
REMARK 620 3 GLU C 192   OE1  84.9  85.5
REMARK 620 4 CAP C 446   O2   96.4 106.8 167.6
REMARK 620 5 CAP C 446   O7  174.3  98.1  97.6  80.0
REMARK 620 6 CAP C 446   O3   84.5 170.5  89.2  78.7  90.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG D 445  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX D 189   OQ2
REMARK 620 2 ASP D 191   OD1  91.2
REMARK 620 3 GLU D 192   OE1  87.9  87.8
REMARK 620 4 CAP D 446   O2   98.6 108.6 162.1
REMARK 620 5 CAP D 446   O3   85.2 173.4  86.5  77.5
REMARK 620 6 CAP D 446   O7  171.7  96.7  94.8  76.6  87.1
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG E 445  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX E 189   OQ2
REMARK 620 2 ASP E 191   OD2  92.9
REMARK 620 3 GLU E 192   OE1  78.7  76.5
REMARK 620 4 CAP E 446   O3   85.1 159.4  83.0
REMARK 620 5 CAP E 446   O2   94.4 117.6 164.9  83.0
REMARK 620 6 CAP E 446   O7  176.3  89.2  98.8  91.8  87.3
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG F 445  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 191   OD1
REMARK 620 2 GLU F 192   OE1  82.4
REMARK 620 3 CAP F 446   O3  168.4  88.9
REMARK 620 4 CAP F 446   O7   91.4  97.6  82.1
REMARK 620 5 CAP F 446   O2  111.5 162.3  75.7  72.0
REMARK 620 6 KCX F 189   OQ2 102.8  98.3  86.0 159.9  89.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG G 445  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX G 189   OQ2
REMARK 620 2 ASP G 191   OD2 100.4
REMARK 620 3 GLU G 192   OE1  92.0  73.9
REMARK 620 4 CAP G 446   O7  169.3  89.5  94.5
REMARK 620 5 CAP G 446   O2   94.8 125.2 157.9  76.1
REMARK 620 6 CAP G 446   O3   84.7 157.6  84.2  87.5  75.5
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG H 445  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX H 189   OQ2
REMARK 620 2 GLU H 192   OE1  77.2
REMARK 620 3 CAP H 446   O7  150.0 103.2
REMARK 620 4 CAP H 446   O2   86.0 151.2  80.0
REMARK 620 5 CAP H 446   O3   76.7  79.7  74.0  73.7
REMARK 620 6 ASP H 191   OD2  99.7 118.0 106.0  87.6 161.1
REMARK 620 7 ASP H 191   OD1 107.2  76.0 101.8 132.0 153.6  45.3
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG I 445  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX I 189   OQ2
REMARK 620 2 ASP I 191   OD1  94.9
REMARK 620 3 GLU I 192   OE1  88.7  89.8
REMARK 620 4 CAP I 446   O2   93.0 108.2 161.7
REMARK 620 5 CAP I 446   O3   83.0 176.5  87.3  74.8
REMARK 620 6 CAP I 446   O7  166.9  94.8 100.1  75.6  87.7
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG J 445  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX J 189   OQ2
REMARK 620 2 ASP J 191   OD1  92.3
REMARK 620 3 GLU J 192   OE1  82.4  84.1
REMARK 620 4 CAP J 446   O3   86.7 163.7  79.7
REMARK 620 5 CAP J 446   O2   85.2 115.8 157.0  80.3
REMARK 620 6 CAP J 446   O7  168.4  91.4 108.9  92.8  83.3
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 MG A 445
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A 446
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 445
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP B 446
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 445
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP C 446
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 445
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP D 446
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 445
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E 446
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 445
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP F 446
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 445
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP G 446
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 445
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP H 446
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG I 445
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP I 446
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG J 445
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP J 446
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GEH   RELATED DB: PDB
REMARK 900 THE APO-FORM ABOUT THE SAME ENZYME
REMARK 900 RELATED ID: 3A13   RELATED DB: PDB
DBREF  3A12 A    1   444  UNP    O93627   RBL_PYRKO        1    444
DBREF  3A12 B    1   444  UNP    O93627   RBL_PYRKO        1    444
DBREF  3A12 C    1   444  UNP    O93627   RBL_PYRKO        1    444
DBREF  3A12 D    1   444  UNP    O93627   RBL_PYRKO        1    444
DBREF  3A12 E    1   444  UNP    O93627   RBL_PYRKO        1    444
DBREF  3A12 F    1   444  UNP    O93627   RBL_PYRKO        1    444
DBREF  3A12 G    1   444  UNP    O93627   RBL_PYRKO        1    444
DBREF  3A12 H    1   444  UNP    O93627   RBL_PYRKO        1    444
DBREF  3A12 I    1   444  UNP    O93627   RBL_PYRKO        1    444
DBREF  3A12 J    1   444  UNP    O93627   RBL_PYRKO        1    444
SEQRES   1 A  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL
SEQRES   2 A  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE
SEQRES   3 A  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE
SEQRES   4 A  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR
SEQRES   5 A  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU
SEQRES   6 A  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS
SEQRES   7 A  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR
SEQRES   8 A  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU
SEQRES   9 A  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG
SEQRES  10 A  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU
SEQRES  11 A  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE
SEQRES  12 A  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO
SEQRES  13 A  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER
SEQRES  14 A  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER
SEQRES  15 A  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR
SEQRES  16 A  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE
SEQRES  17 A  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY
SEQRES  18 A  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU
SEQRES  19 A  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU
SEQRES  20 A  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY
SEQRES  21 A  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP
SEQRES  22 A  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA
SEQRES  23 A  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE
SEQRES  24 A  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN
SEQRES  25 A  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY
SEQRES  26 A  444  GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE LEU ARG
SEQRES  27 A  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS
SEQRES  28 A  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO
SEQRES  29 A  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO
SEQRES  30 A  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU
SEQRES  31 A  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA
SEQRES  32 A  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET
SEQRES  33 A  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS
SEQRES  34 A  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR
SEQRES  35 A  444  PRO VAL
SEQRES   1 B  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL
SEQRES   2 B  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE
SEQRES   3 B  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE
SEQRES   4 B  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR
SEQRES   5 B  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU
SEQRES   6 B  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS
SEQRES   7 B  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR
SEQRES   8 B  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU
SEQRES   9 B  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG
SEQRES  10 B  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU
SEQRES  11 B  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE
SEQRES  12 B  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO
SEQRES  13 B  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER
SEQRES  14 B  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER
SEQRES  15 B  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR
SEQRES  16 B  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE
SEQRES  17 B  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY
SEQRES  18 B  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU
SEQRES  19 B  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU
SEQRES  20 B  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY
SEQRES  21 B  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP
SEQRES  22 B  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA
SEQRES  23 B  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE
SEQRES  24 B  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN
SEQRES  25 B  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY
SEQRES  26 B  444  GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE LEU ARG
SEQRES  27 B  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS
SEQRES  28 B  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO
SEQRES  29 B  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO
SEQRES  30 B  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU
SEQRES  31 B  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA
SEQRES  32 B  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET
SEQRES  33 B  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS
SEQRES  34 B  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR
SEQRES  35 B  444  PRO VAL
SEQRES   1 C  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL
SEQRES   2 C  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE
SEQRES   3 C  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE
SEQRES   4 C  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR
SEQRES   5 C  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU
SEQRES   6 C  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS
SEQRES   7 C  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR
SEQRES   8 C  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU
SEQRES   9 C  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG
SEQRES  10 C  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU
SEQRES  11 C  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE
SEQRES  12 C  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO
SEQRES  13 C  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER
SEQRES  14 C  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER
SEQRES  15 C  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR
SEQRES  16 C  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE
SEQRES  17 C  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY
SEQRES  18 C  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU
SEQRES  19 C  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU
SEQRES  20 C  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY
SEQRES  21 C  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP
SEQRES  22 C  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA
SEQRES  23 C  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE
SEQRES  24 C  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN
SEQRES  25 C  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY
SEQRES  26 C  444  GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE LEU ARG
SEQRES  27 C  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS
SEQRES  28 C  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO
SEQRES  29 C  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO
SEQRES  30 C  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU
SEQRES  31 C  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA
SEQRES  32 C  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET
SEQRES  33 C  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS
SEQRES  34 C  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR
SEQRES  35 C  444  PRO VAL
SEQRES   1 D  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL
SEQRES   2 D  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE
SEQRES   3 D  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE
SEQRES   4 D  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR
SEQRES   5 D  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU
SEQRES   6 D  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS
SEQRES   7 D  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR
SEQRES   8 D  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU
SEQRES   9 D  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG
SEQRES  10 D  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU
SEQRES  11 D  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE
SEQRES  12 D  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO
SEQRES  13 D  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER
SEQRES  14 D  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER
SEQRES  15 D  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR
SEQRES  16 D  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE
SEQRES  17 D  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY
SEQRES  18 D  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU
SEQRES  19 D  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU
SEQRES  20 D  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY
SEQRES  21 D  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP
SEQRES  22 D  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA
SEQRES  23 D  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE
SEQRES  24 D  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN
SEQRES  25 D  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY
SEQRES  26 D  444  GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE LEU ARG
SEQRES  27 D  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS
SEQRES  28 D  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO
SEQRES  29 D  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO
SEQRES  30 D  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU
SEQRES  31 D  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA
SEQRES  32 D  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET
SEQRES  33 D  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS
SEQRES  34 D  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR
SEQRES  35 D  444  PRO VAL
SEQRES   1 E  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL
SEQRES   2 E  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE
SEQRES   3 E  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE
SEQRES   4 E  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR
SEQRES   5 E  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU
SEQRES   6 E  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS
SEQRES   7 E  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR
SEQRES   8 E  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU
SEQRES   9 E  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG
SEQRES  10 E  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU
SEQRES  11 E  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE
SEQRES  12 E  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO
SEQRES  13 E  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER
SEQRES  14 E  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER
SEQRES  15 E  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR
SEQRES  16 E  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE
SEQRES  17 E  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY
SEQRES  18 E  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU
SEQRES  19 E  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU
SEQRES  20 E  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY
SEQRES  21 E  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP
SEQRES  22 E  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA
SEQRES  23 E  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE
SEQRES  24 E  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN
SEQRES  25 E  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY
SEQRES  26 E  444  GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE LEU ARG
SEQRES  27 E  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS
SEQRES  28 E  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO
SEQRES  29 E  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO
SEQRES  30 E  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU
SEQRES  31 E  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA
SEQRES  32 E  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET
SEQRES  33 E  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS
SEQRES  34 E  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR
SEQRES  35 E  444  PRO VAL
SEQRES   1 F  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL
SEQRES   2 F  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE
SEQRES   3 F  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE
SEQRES   4 F  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR
SEQRES   5 F  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU
SEQRES   6 F  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS
SEQRES   7 F  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR
SEQRES   8 F  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU
SEQRES   9 F  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG
SEQRES  10 F  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU
SEQRES  11 F  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE
SEQRES  12 F  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO
SEQRES  13 F  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER
SEQRES  14 F  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER
SEQRES  15 F  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR
SEQRES  16 F  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE
SEQRES  17 F  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY
SEQRES  18 F  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU
SEQRES  19 F  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU
SEQRES  20 F  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY
SEQRES  21 F  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP
SEQRES  22 F  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA
SEQRES  23 F  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE
SEQRES  24 F  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN
SEQRES  25 F  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY
SEQRES  26 F  444  GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE LEU ARG
SEQRES  27 F  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS
SEQRES  28 F  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO
SEQRES  29 F  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO
SEQRES  30 F  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU
SEQRES  31 F  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA
SEQRES  32 F  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET
SEQRES  33 F  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS
SEQRES  34 F  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR
SEQRES  35 F  444  PRO VAL
SEQRES   1 G  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL
SEQRES   2 G  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE
SEQRES   3 G  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE
SEQRES   4 G  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR
SEQRES   5 G  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU
SEQRES   6 G  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS
SEQRES   7 G  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR
SEQRES   8 G  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU
SEQRES   9 G  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG
SEQRES  10 G  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU
SEQRES  11 G  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE
SEQRES  12 G  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO
SEQRES  13 G  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER
SEQRES  14 G  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER
SEQRES  15 G  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR
SEQRES  16 G  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE
SEQRES  17 G  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY
SEQRES  18 G  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU
SEQRES  19 G  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU
SEQRES  20 G  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY
SEQRES  21 G  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP
SEQRES  22 G  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA
SEQRES  23 G  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE
SEQRES  24 G  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN
SEQRES  25 G  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY
SEQRES  26 G  444  GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE LEU ARG
SEQRES  27 G  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS
SEQRES  28 G  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO
SEQRES  29 G  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO
SEQRES  30 G  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU
SEQRES  31 G  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA
SEQRES  32 G  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET
SEQRES  33 G  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS
SEQRES  34 G  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR
SEQRES  35 G  444  PRO VAL
SEQRES   1 H  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL
SEQRES   2 H  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE
SEQRES   3 H  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE
SEQRES   4 H  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR
SEQRES   5 H  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU
SEQRES   6 H  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS
SEQRES   7 H  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR
SEQRES   8 H  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU
SEQRES   9 H  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG
SEQRES  10 H  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU
SEQRES  11 H  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE
SEQRES  12 H  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO
SEQRES  13 H  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER
SEQRES  14 H  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER
SEQRES  15 H  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR
SEQRES  16 H  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE
SEQRES  17 H  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY
SEQRES  18 H  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU
SEQRES  19 H  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU
SEQRES  20 H  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY
SEQRES  21 H  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP
SEQRES  22 H  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA
SEQRES  23 H  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE
SEQRES  24 H  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN
SEQRES  25 H  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY
SEQRES  26 H  444  GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE LEU ARG
SEQRES  27 H  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS
SEQRES  28 H  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO
SEQRES  29 H  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO
SEQRES  30 H  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU
SEQRES  31 H  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA
SEQRES  32 H  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET
SEQRES  33 H  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS
SEQRES  34 H  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR
SEQRES  35 H  444  PRO VAL
SEQRES   1 I  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL
SEQRES   2 I  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE
SEQRES   3 I  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE
SEQRES   4 I  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR
SEQRES   5 I  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU
SEQRES   6 I  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS
SEQRES   7 I  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR
SEQRES   8 I  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU
SEQRES   9 I  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG
SEQRES  10 I  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU
SEQRES  11 I  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE
SEQRES  12 I  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO
SEQRES  13 I  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER
SEQRES  14 I  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER
SEQRES  15 I  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR
SEQRES  16 I  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE
SEQRES  17 I  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY
SEQRES  18 I  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU
SEQRES  19 I  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU
SEQRES  20 I  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY
SEQRES  21 I  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP
SEQRES  22 I  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA
SEQRES  23 I  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE
SEQRES  24 I  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN
SEQRES  25 I  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY
SEQRES  26 I  444  GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE LEU ARG
SEQRES  27 I  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS
SEQRES  28 I  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO
SEQRES  29 I  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO
SEQRES  30 I  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU
SEQRES  31 I  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA
SEQRES  32 I  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET
SEQRES  33 I  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS
SEQRES  34 I  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR
SEQRES  35 I  444  PRO VAL
SEQRES   1 J  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL
SEQRES   2 J  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE
SEQRES   3 J  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE
SEQRES   4 J  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR
SEQRES   5 J  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU
SEQRES   6 J  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS
SEQRES   7 J  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR
SEQRES   8 J  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU
SEQRES   9 J  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG
SEQRES  10 J  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU
SEQRES  11 J  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE
SEQRES  12 J  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO
SEQRES  13 J  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER
SEQRES  14 J  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER
SEQRES  15 J  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR
SEQRES  16 J  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE
SEQRES  17 J  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY
SEQRES  18 J  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU
SEQRES  19 J  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU
SEQRES  20 J  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY
SEQRES  21 J  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP
SEQRES  22 J  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA
SEQRES  23 J  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE
SEQRES  24 J  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN
SEQRES  25 J  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY
SEQRES  26 J  444  GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE LEU ARG
SEQRES  27 J  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS
SEQRES  28 J  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO
SEQRES  29 J  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO
SEQRES  30 J  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU
SEQRES  31 J  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA
SEQRES  32 J  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET
SEQRES  33 J  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS
SEQRES  34 J  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR
SEQRES  35 J  444  PRO VAL
MODRES 3A12 KCX A  189  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 3A12 KCX B  189  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 3A12 KCX C  189  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 3A12 KCX D  189  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 3A12 KCX E  189  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 3A12 KCX F  189  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 3A12 KCX G  189  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 3A12 KCX H  189  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 3A12 KCX I  189  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 3A12 KCX J  189  LYS  LYSINE NZ-CARBOXYLIC ACID
HET    KCX  A 189      12
HET    KCX  B 189      12
HET    KCX  C 189      12
HET    KCX  D 189      12
HET    KCX  E 189      12
HET    KCX  F 189      12
HET    KCX  G 189      12
HET    KCX  H 189      12
HET    KCX  I 189      12
HET    KCX  J 189      12
HET     MG  A 445       1
HET    CAP  A 446      21
HET     MG  B 445       1
HET    CAP  B 446      21
HET     MG  C 445       1
HET    CAP  C 446      21
HET     MG  D 445       1
HET    CAP  D 446      21
HET     MG  E 445       1
HET    CAP  E 446      21
HET     MG  F 445       1
HET    CAP  F 446      21
HET     MG  G 445       1
HET    CAP  G 446      21
HET     MG  H 445       1
HET    CAP  H 446      21
HET     MG  I 445       1
HET    CAP  I 446      21
HET     MG  J 445       1
HET    CAP  J 446      21
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID
HETNAM      MG MAGNESIUM ION
HETNAM     CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE
FORMUL   1  KCX    10(C7 H14 N2 O4)
FORMUL  11   MG    10(MG 2+)
FORMUL  12  CAP    10(C6 H14 O13 P2)
FORMUL  31  HOH   *2306(H2 O)
HELIX    1   1 TYR A    9  VAL A   13  5                                   5
HELIX    2   2 THR A   38  SER A   50  1                                  13
HELIX    3   3 GLU A   63  LEU A   70  1                                   8
HELIX    4   4 HIS A   94  PHE A   96  5                                   3
HELIX    5   5 ASN A  100  ALA A  109  1                                  10
HELIX    6   6 GLY A  110  MET A  115  5                                   6
HELIX    7   7 PRO A  129  ARG A  134  1                                   6
HELIX    8   8 PHE A  141  GLU A  151  1                                  11
HELIX    9   9 SER A  169  ASN A  183  1                                  15
HELIX   10  10 ARG A  201  GLY A  221  1                                  21
HELIX   11  11 ASP A  233  LEU A  247  1                                  15
HELIX   12  12 VAL A  256  GLY A  260  1                                   5
HELIX   13  13 GLY A  260  GLY A  275  1                                  16
HELIX   14  14 HIS A  285  ARG A  290  1                                   6
HELIX   15  15 SER A  297  GLY A  309  1                                  13
HELIX   16  16 GLY A  326  GLU A  339  1                                  14
HELIX   17  17 HIS A  371  ASN A  374  5                                   4
HELIX   18  18 ILE A  375  GLY A  383  1                                   9
HELIX   19  19 GLY A  391  GLY A  396  1                                   6
HELIX   20  20 GLY A  400  GLY A  418  1                                  19
HELIX   21  21 PRO A  420  LYS A  426  1                                   7
HELIX   22  22 HIS A  428  GLY A  439  1                                  12
HELIX   23  23 THR B    7  VAL B   13  5                                   7
HELIX   24  24 THR B   38  SER B   51  1                                  14
HELIX   25  25 GLU B   63  SER B   71  1                                   9
HELIX   26  26 HIS B   94  PHE B   96  5                                   3
HELIX   27  27 ASN B  100  ALA B  109  1                                  10
HELIX   28  28 GLY B  110  MET B  115  5                                   6
HELIX   29  29 PRO B  129  ARG B  134  1                                   6
HELIX   30  30 PHE B  141  GLU B  151  1                                  11
HELIX   31  31 SER B  169  ASN B  183  1                                  15
HELIX   32  32 ARG B  201  GLY B  221  1                                  21
HELIX   33  33 ASP B  233  LEU B  247  1                                  15
HELIX   34  34 VAL B  256  GLY B  260  1                                   5
HELIX   35  35 GLY B  260  TYR B  274  1                                  15
HELIX   36  36 HIS B  285  ARG B  290  1                                   6
HELIX   37  37 SER B  297  GLY B  309  1                                  13
HELIX   38  38 GLY B  326  GLU B  339  1                                  14
HELIX   39  39 HIS B  371  ASN B  374  5                                   4
HELIX   40  40 ILE B  375  GLY B  383  1                                   9
HELIX   41  41 GLY B  391  GLY B  396  1                                   6
HELIX   42  42 GLY B  400  GLY B  418  1                                  19
HELIX   43  43 PRO B  420  ALA B  425  1                                   6
HELIX   44  44 HIS B  428  GLY B  439  1                                  12
HELIX   45  45 ILE C    8  VAL C   13  5                                   6
HELIX   46  46 THR C   38  SER C   50  1                                  13
HELIX   47  47 GLU C   63  SER C   71  1                                   9
HELIX   48  48 HIS C   94  PHE C   96  5                                   3
HELIX   49  49 ASN C  100  ALA C  109  1                                  10
HELIX   50  50 GLY C  110  MET C  115  5                                   6
HELIX   51  51 PRO C  129  ARG C  134  1                                   6
HELIX   52  52 PHE C  141  GLU C  151  1                                  11
HELIX   53  53 SER C  169  ASN C  183  1                                  15
HELIX   54  54 ARG C  201  GLY C  221  1                                  21
HELIX   55  55 ASP C  233  GLY C  248  1                                  16
HELIX   56  56 VAL C  256  GLY C  260  1                                   5
HELIX   57  57 GLY C  260  TYR C  274  1                                  15
HELIX   58  58 HIS C  285  ARG C  290  1                                   6
HELIX   59  59 SER C  297  GLY C  309  1                                  13
HELIX   60  60 GLY C  326  GLU C  339  1                                  14
HELIX   61  61 HIS C  371  ASN C  374  5                                   4
HELIX   62  62 ILE C  375  GLY C  383  1                                   9
HELIX   63  63 GLY C  391  GLY C  396  1                                   6
HELIX   64  64 GLY C  400  GLN C  417  1                                  18
HELIX   65  65 PRO C  420  ALA C  425  1                                   6
HELIX   66  66 HIS C  428  GLY C  439  1                                  12
HELIX   67  67 TYR D    9  VAL D   13  5                                   5
HELIX   68  68 THR D   38  SER D   50  1                                  13
HELIX   69  69 GLU D   63  SER D   71  1                                   9
HELIX   70  70 HIS D   94  PHE D   96  5                                   3
HELIX   71  71 ASN D  100  ALA D  109  1                                  10
HELIX   72  72 GLY D  110  MET D  115  5                                   6
HELIX   73  73 PRO D  129  ARG D  134  1                                   6
HELIX   74  74 PHE D  141  GLU D  151  1                                  11
HELIX   75  75 SER D  169  ASN D  183  1                                  15
HELIX   76  76 ARG D  201  GLY D  221  1                                  21
HELIX   77  77 ASP D  233  LEU D  247  1                                  15
HELIX   78  78 VAL D  256  GLY D  260  1                                   5
HELIX   79  79 GLY D  260  TYR D  274  1                                  15
HELIX   80  80 HIS D  285  ARG D  290  1                                   6
HELIX   81  81 SER D  297  GLY D  309  1                                  13
HELIX   82  82 GLY D  326  GLU D  339  1                                  14
HELIX   83  83 HIS D  371  ASN D  374  5                                   4
HELIX   84  84 ILE D  375  GLY D  383  1                                   9
HELIX   85  85 GLY D  391  GLY D  396  1                                   6
HELIX   86  86 GLY D  400  GLY D  418  1                                  19
HELIX   87  87 PRO D  420  LYS D  426  1                                   7
HELIX   88  88 HIS D  428  GLY D  439  1                                  12
HELIX   89  89 ILE E    8  VAL E   13  5                                   6
HELIX   90  90 THR E   38  SER E   50  1                                  13
HELIX   91  91 GLU E   63  SER E   71  1                                   9
HELIX   92  92 HIS E   94  PHE E   96  5                                   3
HELIX   93  93 ASN E  100  ALA E  109  1                                  10
HELIX   94  94 GLY E  110  MET E  115  5                                   6
HELIX   95  95 PRO E  129  ARG E  134  1                                   6
HELIX   96  96 PHE E  141  GLU E  151  1                                  11
HELIX   97  97 SER E  169  ASN E  183  1                                  15
HELIX   98  98 ARG E  201  GLY E  221  1                                  21
HELIX   99  99 ASP E  233  GLY E  248  1                                  16
HELIX  100 100 VAL E  256  GLY E  260  1                                   5
HELIX  101 101 GLY E  260  TYR E  274  1                                  15
HELIX  102 102 HIS E  285  ARG E  290  1                                   6
HELIX  103 103 SER E  297  GLY E  309  1                                  13
HELIX  104 104 GLY E  326  GLU E  339  1                                  14
HELIX  105 105 ILE E  375  GLY E  383  1                                   9
HELIX  106 106 GLY E  391  GLY E  396  1                                   6
HELIX  107 107 GLY E  400  GLN E  417  1                                  18
HELIX  108 108 PRO E  420  ALA E  425  1                                   6
HELIX  109 109 HIS E  428  GLY E  439  1                                  12
HELIX  110 110 TYR F    9  VAL F   13  5                                   5
HELIX  111 111 THR F   38  SER F   50  1                                  13
HELIX  112 112 GLU F   63  SER F   71  1                                   9
HELIX  113 113 HIS F   94  PHE F   96  5                                   3
HELIX  114 114 ASN F  100  ALA F  109  1                                  10
HELIX  115 115 GLY F  110  MET F  115  5                                   6
HELIX  116 116 PRO F  129  ARG F  134  1                                   6
HELIX  117 117 PHE F  141  GLU F  151  1                                  11
HELIX  118 118 SER F  169  ASN F  183  1                                  15
HELIX  119 119 ARG F  201  GLY F  221  1                                  21
HELIX  120 120 ASP F  233  GLY F  248  1                                  16
HELIX  121 121 VAL F  256  GLY F  260  1                                   5
HELIX  122 122 GLY F  260  GLY F  275  1                                  16
HELIX  123 123 HIS F  285  ARG F  290  1                                   6
HELIX  124 124 SER F  297  GLY F  309  1                                  13
HELIX  125 125 GLY F  326  GLU F  339  1                                  14
HELIX  126 126 HIS F  371  GLY F  383  1                                  13
HELIX  127 127 GLY F  391  GLY F  396  1                                   6
HELIX  128 128 GLY F  400  GLN F  417  1                                  18
HELIX  129 129 PRO F  420  ALA F  425  1                                   6
HELIX  130 130 HIS F  428  GLY F  439  1                                  12
HELIX  131 131 TYR G    9  VAL G   13  5                                   5
HELIX  132 132 THR G   38  SER G   50  1                                  13
HELIX  133 133 GLU G   63  SER G   71  1                                   9
HELIX  134 134 HIS G   94  PHE G   96  5                                   3
HELIX  135 135 ASN G  100  ALA G  109  1                                  10
HELIX  136 136 GLY G  110  MET G  115  5                                   6
HELIX  137 137 PRO G  129  ARG G  134  1                                   6
HELIX  138 138 PHE G  141  GLU G  151  1                                  11
HELIX  139 139 SER G  169  ASN G  183  1                                  15
HELIX  140 140 ARG G  201  GLY G  221  1                                  21
HELIX  141 141 ASP G  233  LEU G  247  1                                  15
HELIX  142 142 VAL G  256  GLY G  260  1                                   5
HELIX  143 143 GLY G  260  TYR G  274  1                                  15
HELIX  144 144 HIS G  285  ARG G  290  1                                   6
HELIX  145 145 SER G  297  GLY G  309  1                                  13
HELIX  146 146 GLY G  326  GLU G  339  1                                  14
HELIX  147 147 HIS G  371  ASN G  374  5                                   4
HELIX  148 148 ILE G  375  GLY G  383  1                                   9
HELIX  149 149 GLY G  391  GLY G  396  1                                   6
HELIX  150 150 GLY G  400  GLY G  418  1                                  19
HELIX  151 151 PRO G  420  ALA G  425  1                                   6
HELIX  152 152 HIS G  428  GLY G  439  1                                  12
HELIX  153 153 TYR H    9  VAL H   13  5                                   5
HELIX  154 154 THR H   38  SER H   50  1                                  13
HELIX  155 155 GLU H   63  SER H   71  1                                   9
HELIX  156 156 HIS H   94  PHE H   96  5                                   3
HELIX  157 157 ASN H  100  ALA H  109  1                                  10
HELIX  158 158 GLY H  110  MET H  115  5                                   6
HELIX  159 159 PRO H  129  ARG H  134  1                                   6
HELIX  160 160 PHE H  141  GLU H  151  1                                  11
HELIX  161 161 SER H  169  ASN H  183  1                                  15
HELIX  162 162 ARG H  201  GLY H  221  1                                  21
HELIX  163 163 ASP H  233  LEU H  247  1                                  15
HELIX  164 164 VAL H  256  GLY H  260  1                                   5
HELIX  165 165 GLY H  260  TYR H  274  1                                  15
HELIX  166 166 HIS H  285  ARG H  290  1                                   6
HELIX  167 167 SER H  297  GLY H  309  1                                  13
HELIX  168 168 GLY H  326  GLU H  339  1                                  14
HELIX  169 169 HIS H  371  ASN H  374  5                                   4
HELIX  170 170 ILE H  375  GLY H  383  1                                   9
HELIX  171 171 GLY H  391  GLY H  396  1                                   6
HELIX  172 172 GLY H  400  GLN H  417  1                                  18
HELIX  173 173 PRO H  420  THR H  427  1                                   8
HELIX  174 174 HIS H  428  GLY H  439  1                                  12
HELIX  175 175 TYR I    9  VAL I   13  5                                   5
HELIX  176 176 THR I   38  SER I   50  1                                  13
HELIX  177 177 GLU I   63  SER I   71  1                                   9
HELIX  178 178 HIS I   94  PHE I   96  5                                   3
HELIX  179 179 ASN I  100  ALA I  109  1                                  10
HELIX  180 180 GLY I  110  MET I  115  5                                   6
HELIX  181 181 PRO I  129  ARG I  134  1                                   6
HELIX  182 182 PHE I  141  GLU I  151  1                                  11
HELIX  183 183 SER I  169  ASN I  183  1                                  15
HELIX  184 184 ARG I  201  GLY I  221  1                                  21
HELIX  185 185 ASP I  233  GLY I  248  1                                  16
HELIX  186 186 VAL I  256  GLY I  260  1                                   5
HELIX  187 187 GLY I  260  TYR I  274  1                                  15
HELIX  188 188 HIS I  285  ARG I  290  1                                   6
HELIX  189 189 SER I  297  GLY I  309  1                                  13
HELIX  190 190 GLY I  326  GLU I  339  1                                  14
HELIX  191 191 HIS I  371  ASN I  374  5                                   4
HELIX  192 192 ILE I  375  GLY I  383  1                                   9
HELIX  193 193 GLY I  391  GLY I  396  1                                   6
HELIX  194 194 GLY I  400  GLY I  418  1                                  19
HELIX  195 195 PRO I  420  LYS I  426  1                                   7
HELIX  196 196 HIS I  428  GLY I  439  1                                  12
HELIX  197 197 ILE J    8  VAL J   13  5                                   6
HELIX  198 198 THR J   38  SER J   50  1                                  13
HELIX  199 199 GLU J   63  SER J   71  1                                   9
HELIX  200 200 HIS J   94  PHE J   96  5                                   3
HELIX  201 201 ASN J  100  ALA J  109  1                                  10
HELIX  202 202 GLY J  110  MET J  115  5                                   6
HELIX  203 203 PRO J  129  ARG J  134  1                                   6
HELIX  204 204 PHE J  141  GLU J  151  1                                  11
HELIX  205 205 SER J  169  ASN J  183  1                                  15
HELIX  206 206 ARG J  201  GLY J  221  1                                  21
HELIX  207 207 ASP J  233  LEU J  247  1                                  15
HELIX  208 208 VAL J  256  GLY J  260  1                                   5
HELIX  209 209 GLY J  260  TYR J  274  1                                  15
HELIX  210 210 HIS J  285  ARG J  290  1                                   6
HELIX  211 211 SER J  297  GLY J  309  1                                  13
HELIX  212 212 GLY J  326  GLU J  339  1                                  14
HELIX  213 213 ILE J  375  GLY J  383  1                                   9
HELIX  214 214 GLY J  391  GLY J  396  1                                   6
HELIX  215 215 GLY J  400  GLY J  418  1                                  19
HELIX  216 216 PRO J  420  ALA J  425  1                                   6
HELIX  217 217 HIS J  428  GLY J  439  1                                  12
SHEET    1   A 5 LYS A  73  ASP A  79  0
SHEET    2   A 5 TRP A  85  PRO A  92 -1  O  ALA A  90   N  LYS A  73
SHEET    3   A 5 ASP A  24  PRO A  33 -1  N  PHE A  29   O  VAL A  87
SHEET    4   A 5 VAL A 118  TYR A 127 -1  O  LYS A 119   N  THR A  32
SHEET    5   A 5 GLY A 295  ILE A 296  1  O  GLY A 295   N  LEU A 121
SHEET    1   B 9 ILE A 157  VAL A 160  0
SHEET    2   B 9 TYR A 187  KCX A 189  1  O  KCX A 189   N  VAL A 160
SHEET    3   B 9 THR A 225  ASN A 229  1  O  PHE A 227   N  MET A 188
SHEET    4   B 9 HIS A 251  ASP A 255  1  O  MET A 253   N  ALA A 228
SHEET    5   B 9 ALA A 277  HIS A 281  1  O  HIS A 281   N  VAL A 254
SHEET    6   B 9 GLN A 312  HIS A 314  1  O  GLN A 312   N  GLY A 280
SHEET    7   B 9 PHE A 363  SER A 367  1  O  THR A 365   N  LEU A 313
SHEET    8   B 9 VAL A 387  GLN A 389  1  O  VAL A 387   N  SER A 366
SHEET    9   B 9 ILE A 157  VAL A 160  1  N  ILE A 157   O  LEU A 388
SHEET    1   C 2 HIS A 341  TYR A 342  0
SHEET    2   C 2 GLN A 354  LYS A 355 -1  O  GLN A 354   N  TYR A 342
SHEET    1   D 5 LYS B  73  ASP B  79  0
SHEET    2   D 5 TRP B  85  PRO B  92 -1  O  ILE B  86   N  HIS B  78
SHEET    3   D 5 ASP B  24  PRO B  33 -1  N  ILE B  25   O  TYR B  91
SHEET    4   D 5 VAL B 118  TYR B 127 -1  O  LYS B 119   N  THR B  32
SHEET    5   D 5 GLY B 295  ILE B 296  1  O  GLY B 295   N  LEU B 123
SHEET    1   E 9 ILE B 157  VAL B 160  0
SHEET    2   E 9 TYR B 187  KCX B 189  1  O  KCX B 189   N  VAL B 160
SHEET    3   E 9 THR B 225  ASN B 229  1  O  PHE B 227   N  MET B 188
SHEET    4   E 9 HIS B 251  ASP B 255  1  O  MET B 253   N  ALA B 228
SHEET    5   E 9 ALA B 277  HIS B 281  1  O  HIS B 279   N  ALA B 252
SHEET    6   E 9 GLN B 312  HIS B 314  1  O  GLN B 312   N  GLY B 280
SHEET    7   E 9 PHE B 363  SER B 367  1  O  THR B 365   N  LEU B 313
SHEET    8   E 9 VAL B 387  GLN B 389  1  O  VAL B 387   N  SER B 366
SHEET    9   E 9 ILE B 157  VAL B 160  1  N  ILE B 157   O  LEU B 388
SHEET    1   F 2 HIS B 341  TYR B 342  0
SHEET    2   F 2 GLN B 354  LYS B 355 -1  O  GLN B 354   N  TYR B 342
SHEET    1   G 5 LYS C  73  ASP C  79  0
SHEET    2   G 5 TRP C  85  PRO C  92 -1  O  ALA C  90   N  LYS C  73
SHEET    3   G 5 ASP C  24  PRO C  33 -1  N  VAL C  31   O  TRP C  85
SHEET    4   G 5 VAL C 118  TYR C 127 -1  O  LYS C 119   N  THR C  32
SHEET    5   G 5 GLY C 295  ILE C 296  1  O  GLY C 295   N  LEU C 121
SHEET    1   H 9 ILE C 157  VAL C 160  0
SHEET    2   H 9 TYR C 187  KCX C 189  1  O  KCX C 189   N  VAL C 160
SHEET    3   H 9 THR C 225  ASN C 229  1  O  PHE C 227   N  MET C 188
SHEET    4   H 9 HIS C 251  ASP C 255  1  O  MET C 253   N  ALA C 228
SHEET    5   H 9 ALA C 277  HIS C 281  1  O  HIS C 279   N  VAL C 254
SHEET    6   H 9 GLN C 312  HIS C 314  1  O  GLN C 312   N  GLY C 280
SHEET    7   H 9 PHE C 363  SER C 367  1  O  THR C 365   N  LEU C 313
SHEET    8   H 9 VAL C 387  GLN C 389  1  O  VAL C 387   N  SER C 366
SHEET    9   H 9 ILE C 157  VAL C 160  1  N  ILE C 157   O  LEU C 388
SHEET    1   I 2 HIS C 341  TYR C 342  0
SHEET    2   I 2 GLN C 354  LYS C 355 -1  O  GLN C 354   N  TYR C 342
SHEET    1   J 5 LYS D  73  ASP D  79  0
SHEET    2   J 5 TRP D  85  PRO D  92 -1  O  ILE D  86   N  HIS D  78
SHEET    3   J 5 ASP D  24  PRO D  33 -1  N  ILE D  25   O  TYR D  91
SHEET    4   J 5 VAL D 118  TYR D 127 -1  O  LYS D 119   N  THR D  32
SHEET    5   J 5 GLY D 295  ILE D 296  1  O  GLY D 295   N  LEU D 123
SHEET    1   K 9 ILE D 157  VAL D 160  0
SHEET    2   K 9 TYR D 187  KCX D 189  1  O  KCX D 189   N  VAL D 160
SHEET    3   K 9 THR D 225  ASN D 229  1  O  PHE D 227   N  MET D 188
SHEET    4   K 9 HIS D 251  ASP D 255  1  O  MET D 253   N  ALA D 228
SHEET    5   K 9 ALA D 277  HIS D 281  1  O  ALA D 277   N  ALA D 252
SHEET    6   K 9 GLN D 312  HIS D 314  1  O  GLN D 312   N  GLY D 280
SHEET    7   K 9 PHE D 363  SER D 367  1  O  THR D 365   N  LEU D 313
SHEET    8   K 9 VAL D 387  GLN D 389  1  O  VAL D 387   N  SER D 366
SHEET    9   K 9 ILE D 157  VAL D 160  1  N  ILE D 157   O  LEU D 388
SHEET    1   L 2 HIS D 341  TYR D 342  0
SHEET    2   L 2 GLN D 354  LYS D 355 -1  O  GLN D 354   N  TYR D 342
SHEET    1   M 5 LYS E  73  ASP E  79  0
SHEET    2   M 5 TRP E  85  PRO E  92 -1  O  ILE E  86   N  HIS E  78
SHEET    3   M 5 ASP E  24  PRO E  33 -1  N  ILE E  25   O  TYR E  91
SHEET    4   M 5 VAL E 118  TYR E 127 -1  O  TYR E 127   N  ILE E  26
SHEET    5   M 5 GLY E 295  ILE E 296  1  O  GLY E 295   N  LEU E 121
SHEET    1   N 9 ILE E 157  VAL E 160  0
SHEET    2   N 9 TYR E 187  KCX E 189  1  O  KCX E 189   N  VAL E 160
SHEET    3   N 9 THR E 225  ASN E 229  1  O  PHE E 227   N  MET E 188
SHEET    4   N 9 HIS E 251  ASP E 255  1  O  MET E 253   N  ALA E 228
SHEET    5   N 9 ALA E 277  HIS E 281  1  O  ALA E 277   N  ALA E 252
SHEET    6   N 9 GLN E 312  HIS E 314  1  O  GLN E 312   N  GLY E 280
SHEET    7   N 9 PHE E 363  SER E 367  1  O  PHE E 363   N  LEU E 313
SHEET    8   N 9 VAL E 387  GLN E 389  1  O  VAL E 387   N  SER E 366
SHEET    9   N 9 ILE E 157  VAL E 160  1  N  ILE E 157   O  LEU E 388
SHEET    1   O 2 HIS E 341  TYR E 342  0
SHEET    2   O 2 GLN E 354  LYS E 355 -1  O  GLN E 354   N  TYR E 342
SHEET    1   P 5 LYS F  73  ASP F  76  0
SHEET    2   P 5 TRP F  85  PRO F  92 -1  O  ALA F  90   N  LYS F  73
SHEET    3   P 5 ASP F  24  PRO F  33 -1  N  ILE F  25   O  TYR F  91
SHEET    4   P 5 VAL F 118  TYR F 127 -1  O  TYR F 127   N  ILE F  26
SHEET    5   P 5 GLY F 295  ILE F 296  1  O  GLY F 295   N  LEU F 123
SHEET    1   Q 8 THR F 225  PHE F 227  0
SHEET    2   Q 8 TYR F 187  KCX F 189  1  N  MET F 188   O  PHE F 227
SHEET    3   Q 8 ILE F 157  VAL F 160  1  N  VAL F 160   O  KCX F 189
SHEET    4   Q 8 VAL F 387  GLN F 389  1  O  LEU F 388   N  ILE F 157
SHEET    5   Q 8 PHE F 363  SER F 367  1  N  SER F 366   O  VAL F 387
SHEET    6   Q 8 GLN F 312  HIS F 314  1  N  LEU F 313   O  THR F 365
SHEET    7   Q 8 ALA F 277  HIS F 281  1  N  GLY F 280   O  GLN F 312
SHEET    8   Q 8 HIS F 251  ASP F 255  1  N  VAL F 254   O  HIS F 281
SHEET    1   R 2 HIS F 341  TYR F 342  0
SHEET    2   R 2 GLN F 354  LYS F 355 -1  O  GLN F 354   N  TYR F 342
SHEET    1   S 5 LYS G  73  ASP G  79  0
SHEET    2   S 5 TRP G  85  PRO G  92 -1  O  ILE G  86   N  HIS G  78
SHEET    3   S 5 ASP G  24  PRO G  33 -1  N  ILE G  25   O  TYR G  91
SHEET    4   S 5 VAL G 118  TYR G 127 -1  O  LYS G 119   N  THR G  32
SHEET    5   S 5 GLY G 295  ILE G 296  1  O  GLY G 295   N  LEU G 121
SHEET    1   T 9 ILE G 157  VAL G 160  0
SHEET    2   T 9 TYR G 187  KCX G 189  1  O  KCX G 189   N  VAL G 160
SHEET    3   T 9 THR G 225  ASN G 229  1  O  PHE G 227   N  MET G 188
SHEET    4   T 9 HIS G 251  ASP G 255  1  O  MET G 253   N  ALA G 228
SHEET    5   T 9 ALA G 277  HIS G 281  1  O  HIS G 279   N  ALA G 252
SHEET    6   T 9 GLN G 312  HIS G 314  1  O  GLN G 312   N  GLY G 280
SHEET    7   T 9 PHE G 363  SER G 367  1  O  THR G 365   N  LEU G 313
SHEET    8   T 9 VAL G 387  GLN G 389  1  O  VAL G 387   N  SER G 366
SHEET    9   T 9 ILE G 157  VAL G 160  1  N  ILE G 157   O  LEU G 388
SHEET    1   U 2 HIS G 341  TYR G 342  0
SHEET    2   U 2 GLN G 354  LYS G 355 -1  O  GLN G 354   N  TYR G 342
SHEET    1   V 5 LYS H  73  ASP H  79  0
SHEET    2   V 5 TRP H  85  PRO H  92 -1  O  ILE H  86   N  HIS H  78
SHEET    3   V 5 ASP H  24  PRO H  33 -1  N  PHE H  29   O  VAL H  87
SHEET    4   V 5 VAL H 118  TYR H 127 -1  O  LYS H 119   N  THR H  32
SHEET    5   V 5 GLY H 295  ILE H 296  1  O  GLY H 295   N  LEU H 123
SHEET    1   W 8 THR H 225  PHE H 227  0
SHEET    2   W 8 TYR H 187  KCX H 189  1  N  MET H 188   O  PHE H 227
SHEET    3   W 8 ILE H 157  VAL H 160  1  N  VAL H 160   O  KCX H 189
SHEET    4   W 8 VAL H 387  GLN H 389  1  O  LEU H 388   N  ILE H 157
SHEET    5   W 8 PHE H 363  SER H 367  1  N  PRO H 364   O  VAL H 387
SHEET    6   W 8 GLN H 312  HIS H 314  1  N  LEU H 313   O  PHE H 363
SHEET    7   W 8 ALA H 277  HIS H 281  1  N  GLY H 280   O  GLN H 312
SHEET    8   W 8 HIS H 251  ASP H 255  1  N  VAL H 254   O  HIS H 281
SHEET    1   X 2 HIS H 341  TYR H 342  0
SHEET    2   X 2 GLN H 354  LYS H 355 -1  O  GLN H 354   N  TYR H 342
SHEET    1   Y 5 LYS I  73  ASP I  79  0
SHEET    2   Y 5 TRP I  85  PRO I  92 -1  O  ILE I  86   N  HIS I  78
SHEET    3   Y 5 ASP I  24  PRO I  33 -1  N  VAL I  31   O  TRP I  85
SHEET    4   Y 5 VAL I 118  TYR I 127 -1  O  LYS I 119   N  THR I  32
SHEET    5   Y 5 GLY I 295  ILE I 296  1  O  GLY I 295   N  LEU I 123
SHEET    1   Z 9 ILE I 157  VAL I 160  0
SHEET    2   Z 9 TYR I 187  KCX I 189  1  O  KCX I 189   N  VAL I 160
SHEET    3   Z 9 THR I 225  ASN I 229  1  O  PHE I 227   N  MET I 188
SHEET    4   Z 9 HIS I 251  ASP I 255  1  O  MET I 253   N  ALA I 228
SHEET    5   Z 9 ALA I 277  HIS I 281  1  O  ALA I 277   N  ALA I 252
SHEET    6   Z 9 GLN I 312  HIS I 314  1  O  GLN I 312   N  GLY I 280
SHEET    7   Z 9 PHE I 363  SER I 367  1  O  THR I 365   N  LEU I 313
SHEET    8   Z 9 VAL I 387  GLN I 389  1  O  VAL I 387   N  SER I 366
SHEET    9   Z 9 ILE I 157  VAL I 160  1  N  ILE I 157   O  LEU I 388
SHEET    1  AA 2 HIS I 341  TYR I 342  0
SHEET    2  AA 2 GLN I 354  LYS I 355 -1  O  GLN I 354   N  TYR I 342
SHEET    1  AB 5 LYS J  73  ASP J  79  0
SHEET    2  AB 5 TRP J  85  PRO J  92 -1  O  ILE J  86   N  HIS J  78
SHEET    3  AB 5 ASP J  24  PRO J  33 -1  N  ILE J  25   O  TYR J  91
SHEET    4  AB 5 VAL J 118  TYR J 127 -1  O  GLU J 124   N  VAL J  28
SHEET    5  AB 5 GLY J 295  ILE J 296  1  O  GLY J 295   N  LEU J 121
SHEET    1  AC 8 THR J 225  PHE J 227  0
SHEET    2  AC 8 TYR J 187  KCX J 189  1  N  MET J 188   O  PHE J 227
SHEET    3  AC 8 ILE J 157  VAL J 160  1  N  VAL J 160   O  KCX J 189
SHEET    4  AC 8 VAL J 387  GLN J 389  1  O  LEU J 388   N  ILE J 157
SHEET    5  AC 8 PHE J 363  SER J 367  1  N  PRO J 364   O  VAL J 387
SHEET    6  AC 8 GLN J 312  HIS J 314  1  N  LEU J 313   O  PHE J 363
SHEET    7  AC 8 ALA J 277  HIS J 281  1  N  GLY J 280   O  GLN J 312
SHEET    8  AC 8 HIS J 251  ASP J 255  1  N  VAL J 254   O  HIS J 281
SHEET    1  AD 2 HIS J 341  TYR J 342  0
SHEET    2  AD 2 GLN J 354  LYS J 355 -1  O  GLN J 354   N  TYR J 342
LINK         C   MET A 188                 N   KCX A 189     1555   1555  1.33
LINK         C   KCX A 189                 N   ASP A 190     1555   1555  1.33
LINK         C   MET B 188                 N   KCX B 189     1555   1555  1.32
LINK         C   KCX B 189                 N   ASP B 190     1555   1555  1.33
LINK         C   MET C 188                 N   KCX C 189     1555   1555  1.33
LINK         C   KCX C 189                 N   ASP C 190     1555   1555  1.33
LINK         C   MET D 188                 N   KCX D 189     1555   1555  1.33
LINK         C   KCX D 189                 N   ASP D 190     1555   1555  1.33
LINK         C   MET E 188                 N   KCX E 189     1555   1555  1.33
LINK         C   KCX E 189                 N   ASP E 190     1555   1555  1.33
LINK         C   MET F 188                 N   KCX F 189     1555   1555  1.33
LINK         C   KCX F 189                 N   ASP F 190     1555   1555  1.33
LINK         C   MET G 188                 N   KCX G 189     1555   1555  1.32
LINK         C   KCX G 189                 N   ASP G 190     1555   1555  1.33
LINK         C   MET H 188                 N   KCX H 189     1555   1555  1.33
LINK         C   KCX H 189                 N   ASP H 190     1555   1555  1.33
LINK         C   MET I 188                 N   KCX I 189     1555   1555  1.33
LINK         C   KCX I 189                 N   ASP I 190     1555   1555  1.33
LINK         C   MET J 188                 N   KCX J 189     1555   1555  1.33
LINK         C   KCX J 189                 N   ASP J 190     1555   1555  1.33
LINK         OQ2 KCX A 189                MG    MG A 445     1555   1555  2.00
LINK         OD1 ASP A 191                MG    MG A 445     1555   1555  2.01
LINK         OE1 GLU A 192                MG    MG A 445     1555   1555  1.97
LINK         OQ2 KCX B 189                MG    MG B 445     1555   1555  2.01
LINK         OD1 ASP B 191                MG    MG B 445     1555   1555  1.97
LINK         OE1 GLU B 192                MG    MG B 445     1555   1555  2.02
LINK         OQ2 KCX C 189                MG    MG C 445     1555   1555  1.94
LINK         OD1 ASP C 191                MG    MG C 445     1555   1555  1.94
LINK         OE1 GLU C 192                MG    MG C 445     1555   1555  2.08
LINK         OQ2 KCX D 189                MG    MG D 445     1555   1555  1.91
LINK         OD1 ASP D 191                MG    MG D 445     1555   1555  1.90
LINK         OE1 GLU D 192                MG    MG D 445     1555   1555  2.14
LINK         OQ2 KCX E 189                MG    MG E 445     1555   1555  2.06
LINK         OD2 ASP E 191                MG    MG E 445     1555   1555  2.25
LINK         OE1 GLU E 192                MG    MG E 445     1555   1555  2.17
LINK         OD1 ASP F 191                MG    MG F 445     1555   1555  2.01
LINK         OE1 GLU F 192                MG    MG F 445     1555   1555  1.99
LINK         OQ2 KCX G 189                MG    MG G 445     1555   1555  2.07
LINK         OD2 ASP G 191                MG    MG G 445     1555   1555  2.43
LINK         OE1 GLU G 192                MG    MG G 445     1555   1555  2.06
LINK         OQ2 KCX H 189                MG    MG H 445     1555   1555  2.22
LINK         OE1 GLU H 192                MG    MG H 445     1555   1555  2.07
LINK         OQ2 KCX I 189                MG    MG I 445     1555   1555  1.94
LINK         OD1 ASP I 191                MG    MG I 445     1555   1555  1.96
LINK         OE1 GLU I 192                MG    MG I 445     1555   1555  2.00
LINK         OQ2 KCX J 189                MG    MG J 445     1555   1555  2.08
LINK         OD1 ASP J 191                MG    MG J 445     1555   1555  2.18
LINK         OE1 GLU J 192                MG    MG J 445     1555   1555  2.00
LINK        MG    MG A 445                 O3  CAP A 446     1555   1555  2.14
LINK        MG    MG A 445                 O2  CAP A 446     1555   1555  2.38
LINK        MG    MG A 445                 O7  CAP A 446     1555   1555  1.92
LINK        MG    MG B 445                 O7  CAP B 446     1555   1555  2.02
LINK        MG    MG B 445                 O2  CAP B 446     1555   1555  2.19
LINK        MG    MG B 445                 O3  CAP B 446     1555   1555  2.11
LINK        MG    MG C 445                 O2  CAP C 446     1555   1555  2.38
LINK        MG    MG C 445                 O7  CAP C 446     1555   1555  1.84
LINK        MG    MG C 445                 O3  CAP C 446     1555   1555  2.14
LINK        MG    MG D 445                 O2  CAP D 446     1555   1555  2.29
LINK        MG    MG D 445                 O3  CAP D 446     1555   1555  2.11
LINK        MG    MG D 445                 O7  CAP D 446     1555   1555  2.18
LINK        MG    MG E 445                 O3  CAP E 446     1555   1555  2.04
LINK        MG    MG E 445                 O2  CAP E 446     1555   1555  2.20
LINK        MG    MG E 445                 O7  CAP E 446     1555   1555  1.79
LINK        MG    MG F 445                 O3  CAP F 446     1555   1555  2.21
LINK        MG    MG F 445                 O7  CAP F 446     1555   1555  2.19
LINK        MG    MG F 445                 O2  CAP F 446     1555   1555  2.36
LINK        MG    MG G 445                 O7  CAP G 446     1555   1555  2.09
LINK        MG    MG G 445                 O2  CAP G 446     1555   1555  2.32
LINK        MG    MG G 445                 O3  CAP G 446     1555   1555  2.19
LINK        MG    MG H 445                 O7  CAP H 446     1555   1555  1.98
LINK        MG    MG H 445                 O2  CAP H 446     1555   1555  2.36
LINK        MG    MG H 445                 O3  CAP H 446     1555   1555  2.30
LINK        MG    MG I 445                 O2  CAP I 446     1555   1555  2.28
LINK        MG    MG I 445                 O3  CAP I 446     1555   1555  2.13
LINK        MG    MG I 445                 O7  CAP I 446     1555   1555  2.09
LINK        MG    MG J 445                 O3  CAP J 446     1555   1555  2.08
LINK        MG    MG J 445                 O2  CAP J 446     1555   1555  2.32
LINK         OQ2 KCX F 189                MG    MG F 445     1555   1555  1.71
LINK        MG    MG J 445                 O7  CAP J 446     1555   1555  1.72
LINK         OD2 ASP H 191                MG    MG H 445     1555   1555  2.73
LINK         OD1 ASP H 191                MG    MG H 445     1555   1555  2.94
CISPEP   1 LYS A  163    PRO A  164          0         6.12
CISPEP   2 LYS B  163    PRO B  164          0         5.42
CISPEP   3 LYS C  163    PRO C  164          0         5.75
CISPEP   4 LYS D  163    PRO D  164          0         8.10
CISPEP   5 LYS E  163    PRO E  164          0         3.07
CISPEP   6 LYS F  163    PRO F  164          0         8.05
CISPEP   7 LYS G  163    PRO G  164          0         4.80
CISPEP   8 LYS H  163    PRO H  164          0         4.80
CISPEP   9 LYS I  163    PRO I  164          0         5.67
CISPEP  10 LYS J  163    PRO J  164          0         5.36
SITE     1 AC1  5 KCX A 189  ASP A 191  GLU A 192  CAP A 446
SITE     2 AC1  5 ASN C 111
SITE     1 AC2 30 VAL A 161  LYS A 163  LYS A 165  KCX A 189
SITE     2 AC2 30 ASP A 191  GLU A 192  HIS A 281  ARG A 282
SITE     3 AC2 30 HIS A 314  LYS A 322  LEU A 323  SER A 367
SITE     4 AC2 30 GLY A 368  GLY A 369  GLN A 389  GLY A 391
SITE     5 AC2 30 GLY A 392   MG A 445  HOH A 521  HOH A 523
SITE     6 AC2 30 HOH A 528  HOH A 574  HOH A 579  HOH A 615
SITE     7 AC2 30 HOH A 626  HOH A 684  GLU C  49  THR C  54
SITE     8 AC2 30 TRP C  55  ASN C 111
SITE     1 AC3  5 ASN B 111  KCX B 189  ASP B 191  GLU B 192
SITE     2 AC3  5 CAP B 446
SITE     1 AC4 29 GLU B  49  TRP B  55  ASN B 111  LYS B 163
SITE     2 AC4 29 LYS B 165  KCX B 189  ASP B 191  GLU B 192
SITE     3 AC4 29 HIS B 281  ARG B 282  HIS B 314  LYS B 322
SITE     4 AC4 29 LEU B 323  SER B 367  GLY B 368  GLY B 369
SITE     5 AC4 29 GLN B 389  GLY B 391  GLY B 392   MG B 445
SITE     6 AC4 29 HOH B 519  HOH B 521  HOH B 542  HOH B 551
SITE     7 AC4 29 HOH B 556  HOH B 559  HOH B 692  HOH B 712
SITE     8 AC4 29 HOH B 713
SITE     1 AC5  4 KCX C 189  ASP C 191  GLU C 192  CAP C 446
SITE     1 AC6 28 GLU A  49  TRP A  55  ASN A 111  HOH A 611
SITE     2 AC6 28 LYS C 163  LYS C 165  KCX C 189  ASP C 191
SITE     3 AC6 28 GLU C 192  HIS C 281  ARG C 282  HIS C 314
SITE     4 AC6 28 LYS C 322  LEU C 323  SER C 367  GLY C 368
SITE     5 AC6 28 GLY C 369  GLN C 389  GLY C 391  GLY C 392
SITE     6 AC6 28  MG C 445  HOH C 524  HOH C 528  HOH C 557
SITE     7 AC6 28 HOH C 562  HOH C 591  HOH C 658  HOH C 740
SITE     1 AC7  4 KCX D 189  ASP D 191  GLU D 192  CAP D 446
SITE     1 AC8 28 LYS D 163  LYS D 165  KCX D 189  ASP D 191
SITE     2 AC8 28 GLU D 192  HIS D 281  ARG D 282  HIS D 314
SITE     3 AC8 28 LYS D 322  LEU D 323  SER D 367  GLY D 368
SITE     4 AC8 28 GLY D 369  GLN D 389  GLY D 391  GLY D 392
SITE     5 AC8 28  MG D 445  HOH D 515  HOH D 519  HOH D 524
SITE     6 AC8 28 HOH D 537  HOH D 538  HOH D 539  HOH D 665
SITE     7 AC8 28 HOH D 716  GLU E  49  TRP E  55  ASN E 111
SITE     1 AC9  4 KCX E 189  ASP E 191  GLU E 192  CAP E 446
SITE     1 BC1 28 GLU D  49  TRP D  55  ASN D 111  HOH D 682
SITE     2 BC1 28 LYS E 163  LYS E 165  KCX E 189  ASP E 191
SITE     3 BC1 28 GLU E 192  HIS E 281  ARG E 282  HIS E 314
SITE     4 BC1 28 LYS E 322  LEU E 323  SER E 367  GLY E 368
SITE     5 BC1 28 GLY E 369  GLN E 389  GLY E 391  GLY E 392
SITE     6 BC1 28  MG E 445  HOH E 525  HOH E 532  HOH E 543
SITE     7 BC1 28 HOH E 570  HOH E 574  HOH E 580  HOH E 608
SITE     1 BC2  4 KCX F 189  ASP F 191  GLU F 192  CAP F 446
SITE     1 BC3 27 LYS F 163  LYS F 165  KCX F 189  ASP F 191
SITE     2 BC3 27 GLU F 192  HIS F 281  ARG F 282  HIS F 314
SITE     3 BC3 27 LYS F 322  LEU F 323  SER F 367  GLY F 368
SITE     4 BC3 27 GLY F 369  GLN F 389  GLY F 391  GLY F 392
SITE     5 BC3 27  MG F 445  HOH F 519  HOH F 525  HOH F 536
SITE     6 BC3 27 HOH F 537  HOH F 556  GLU H  49  THR H  54
SITE     7 BC3 27 TRP H  55  ASN H 111  HOH H 513
SITE     1 BC4  4 KCX G 189  ASP G 191  GLU G 192  CAP G 446
SITE     1 BC5 29 GLU G  49  TRP G  55  ASN G 111  LYS G 163
SITE     2 BC5 29 LYS G 165  KCX G 189  ASP G 191  GLU G 192
SITE     3 BC5 29 HIS G 281  ARG G 282  HIS G 314  LYS G 322
SITE     4 BC5 29 LEU G 323  SER G 367  GLY G 368  GLY G 369
SITE     5 BC5 29 GLN G 389  GLY G 391  GLY G 392   MG G 445
SITE     6 BC5 29 HOH G 507  HOH G 524  HOH G 529  HOH G 536
SITE     7 BC5 29 HOH G 540  HOH G 561  HOH G 574  HOH G 602
SITE     8 BC5 29 HOH G 607
SITE     1 BC6  7 ASN F 111  LYS H 163  LYS H 165  KCX H 189
SITE     2 BC6  7 ASP H 191  GLU H 192  CAP H 446
SITE     1 BC7 28 GLU F  49  TRP F  55  ASN F 111  LYS H 163
SITE     2 BC7 28 LYS H 165  KCX H 189  ASP H 191  GLU H 192
SITE     3 BC7 28 HIS H 281  ARG H 282  HIS H 314  LYS H 322
SITE     4 BC7 28 LEU H 323  SER H 367  GLY H 368  GLY H 369
SITE     5 BC7 28 GLN H 389  GLY H 391  GLY H 392   MG H 445
SITE     6 BC7 28 HOH H 520  HOH H 547  HOH H 571  HOH H 584
SITE     7 BC7 28 HOH H 595  HOH H 601  HOH H 604  HOH H 613
SITE     1 BC8  4 KCX I 189  ASP I 191  GLU I 192  CAP I 446
SITE     1 BC9 28 LYS I 163  LYS I 165  KCX I 189  ASP I 191
SITE     2 BC9 28 GLU I 192  HIS I 281  ARG I 282  HIS I 314
SITE     3 BC9 28 LYS I 322  LEU I 323  SER I 367  GLY I 368
SITE     4 BC9 28 GLY I 369  GLN I 389  GLY I 391  GLY I 392
SITE     5 BC9 28  MG I 445  HOH I 515  HOH I 518  HOH I 521
SITE     6 BC9 28 HOH I 525  HOH I 531  HOH I 616  HOH I 662
SITE     7 BC9 28 HOH I 744  GLU J  49  TRP J  55  ASN J 111
SITE     1 CC1  6 ASN I 111  LYS J 163  KCX J 189  ASP J 191
SITE     2 CC1  6 GLU J 192  CAP J 446
SITE     1 CC2 28 GLU I  49  TRP I  55  ASN I 111  HOH I 603
SITE     2 CC2 28 LYS J 163  LYS J 165  KCX J 189  ASP J 191
SITE     3 CC2 28 GLU J 192  HIS J 281  ARG J 282  HIS J 314
SITE     4 CC2 28 LYS J 322  LEU J 323  SER J 367  GLY J 368
SITE     5 CC2 28 GLY J 369  GLN J 389  GLY J 391  GLY J 392
SITE     6 CC2 28  MG J 445  HOH J 502  HOH J 546  HOH J 566
SITE     7 CC2 28 HOH J 580  HOH J 586  HOH J 587  HOH J 633
CRYST1  173.287  246.377  144.589  90.00  90.00  90.00 P 21 21 2    40
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      0.005771  0.000000  0.000000        0.00000
SCALE2      0.000000  0.004059  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006916        0.00000
      
PROCHECK
Go to PROCHECK summary
 References