spacer
spacer

PDBsum entry 3a13

Go to PDB code: 
Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
3a13
Jmol
Contents
Protein chains
(+ 4 more) 436 a.a.
Ligands
CAP ×10
Metals
_MG ×8
_CA ×2
Waters ×1951
HEADER    LYASE                                   25-MAR-09   3A13
TITLE     CRYSTAL STRUCTURE OF TYPE III RUBISCO SP4 MUTANT COMPLEXED
TITLE    2 WITH 2-CABP AND ACTIVATED WITH CA
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;
COMPND   7 MUTATION: 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, 2-BISPHOSPHATE CARBOXYLASE/OXYGENASE, RUBISCO,
KEYWDS   2 LYASE, CARBON DIOXIDE FIXATION, MAGNESIUM, METAL-BINDING,
KEYWDS   3 MONOOXYGENASE, OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Y.NISHITANI,M.FUJIHASHI,T.DOI,S.YOSHIDA,H.ATOMI,T.IMANAKA,
AUTHOR   2 K.MIKI
REVDAT   1   07-APR-10 3A13    0
JRNL        AUTH   Y.NISHITANI,M.FUJIHASHI,T.DOI,S.YOSHIDA,H.ATOMI,
JRNL        AUTH 2 T.IMANAKA,K.MIKI
JRNL        TITL   STURCTURE-BASED OPTIMIZATION OF A TYPE III RUBISCO
JRNL        TITL 2 FROM A HYPERTHERMOPHILE
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.34 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) : 2.34
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.22
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3
REMARK   3   NUMBER OF REFLECTIONS             : 248212
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) : 0.207
REMARK   3   R VALUE            (WORKING SET) : 0.205
REMARK   3   FREE R VALUE                     : 0.250
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 13142
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) : 2.34
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.40
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 17756
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.67
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2590
REMARK   3   BIN FREE R VALUE SET COUNT          : 916
REMARK   3   BIN FREE R VALUE                    : 0.3280
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 34022
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 220
REMARK   3   SOLVENT ATOMS            : 1951
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 32.20
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.75
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 3.32000
REMARK   3    B22 (A**2) : -0.88000
REMARK   3    B33 (A**2) : -2.44000
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): 0.289
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.228
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.154
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.404
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 35083 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 47621 ; 0.995 ; 1.958
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  4343 ; 5.345 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1611 ;30.561 ;23.476
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  5575 ;14.590 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   230 ;20.248 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  5055 ; 0.067 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 27008 ; 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): 21635 ; 0.453 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 34403 ; 0.867 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 13448 ; 1.231 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 13218 ; 2.074 ; 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
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3A13 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 RCSB028678.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 23-JUL-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          : RAYONIX MX-225
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 262382
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.340
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) : 0.11400
REMARK 200   FOR THE DATA SET  : 12.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.34
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38
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) : 0.39200
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   (%): 60.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M ACETATE, 0.1M CACL2, 5%
REMARK 280  PEG6000, 10% MPD, PH6.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  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       86.83900
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      123.54500
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       86.83900
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      123.54500
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: 61520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 128280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -381.0 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      173.67800
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: 61430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 127780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -376.0 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 545  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     ILE A     8
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     THR B     7
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     PRO C   398
REMARK 465     MET D     1
REMARK 465     VAL D     2
REMARK 465     GLU D     3
REMARK 465     LYS D     4
REMARK 465     THR D    54
REMARK 465     LEU D    58
REMARK 465     TYR D    59
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     THR E     7
REMARK 465     ALA E   318
REMARK 465     GLY E   319
REMARK 465     ALA E   320
REMARK 465     GLY E   321
REMARK 465     GLY E   325
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     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     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     MET I     1
REMARK 465     VAL I     2
REMARK 465     GLU I     3
REMARK 465     LYS I     4
REMARK 465     THR I    54
REMARK 465     LEU I    58
REMARK 465     TYR I    59
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 465     ALA J   318
REMARK 465     GLY J   319
REMARK 465     GLY J   325
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     ASP A  10    CG   OD1  OD2
REMARK 470     GLU A  18    CG   CD   OE1  OE2
REMARK 470     THR A  54    OG1  CG2
REMARK 470     THR A  56    OG1  CG2
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     LYS A 153    CG   CD   CE   NZ
REMARK 470     GLU A 203    CG   CD   OE1  OE2
REMARK 470     GLU A 346    CG   CD   OE1  OE2
REMARK 470     GLU A 380    CG   CD   OE1  OE2
REMARK 470     LYS A 429    CG   CD   CE   NZ
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     TYR B  59    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     LYS B 119    CG   CD   CE   NZ
REMARK 470     GLU B 144    CG   CD   OE1  OE2
REMARK 470     ASP B 328    CG   OD1  OD2
REMARK 470     GLU B 346    CG   CD   OE1  OE2
REMARK 470     GLU B 380    CG   CD   OE1  OE2
REMARK 470     LYS B 426    CG   CD   CE   NZ
REMARK 470     LYS B 429    CG   CD   CE   NZ
REMARK 470     VAL B 441    CG1  CG2
REMARK 470     THR C   7    OG1  CG2
REMARK 470     ILE C   8    CG1  CG2  CD1
REMARK 470     ASP C  10    CG   OD1  OD2
REMARK 470     GLU C  65    CG   CD   OE1  OE2
REMARK 470     GLU C 144    CG   CD   OE1  OE2
REMARK 470     LYS C 148    CG   CD   CE   NZ
REMARK 470     LYS C 153    CG   CD   CE   NZ
REMARK 470     ASP C 328    CG   OD1  OD2
REMARK 470     GLU C 380    CG   CD   OE1  OE2
REMARK 470     GLN C 417    CG   CD   OE1  NE2
REMARK 470     LEU C 421    CG   CD1  CD2
REMARK 470     ASP C 422    CG   OD1  OD2
REMARK 470     GLU C 423    CG   CD   OE1  OE2
REMARK 470     LYS C 426    CG   CD   CE   NZ
REMARK 470     LYS C 429    CG   CD   CE   NZ
REMARK 470     LEU C 431    CG   CD1  CD2
REMARK 470     GLU C 436    CG   CD   OE1  OE2
REMARK 470     PHE D   5    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     ASP D   6    CG   OD1  OD2
REMARK 470     THR D  57    OG1  CG2
REMARK 470     GLU D 144    CG   CD   OE1  OE2
REMARK 470     LYS D 153    CG   CD   CE   NZ
REMARK 470     GLU D 346    CG   CD   OE1  OE2
REMARK 470     LEU D 370    CG   CD1  CD2
REMARK 470     GLN D 376    CG   CD   OE1  NE2
REMARK 470     ILE D 415    CG1  CG2  CD1
REMARK 470     GLN D 417    CG   CD   OE1  NE2
REMARK 470     LEU D 421    CG   CD1  CD2
REMARK 470     GLU D 423    CG   CD   OE1  OE2
REMARK 470     TYR D 424    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     LYS D 426    CG   CD   CE   NZ
REMARK 470     LYS D 429    CG   CD   CE   NZ
REMARK 470     GLU D 430    CG   CD   OE1  OE2
REMARK 470     LEU D 431    CG   CD1  CD2
REMARK 470     ILE E   8    CG1  CG2  CD1
REMARK 470     LEU E  58    CG   CD1  CD2
REMARK 470     TYR E  59    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     GLU E 144    CG   CD   OE1  OE2
REMARK 470     LYS E 322    CG   CD   CE   NZ
REMARK 470     LEU E 323    CG   CD1  CD2
REMARK 470     GLU E 324    CG   CD   OE1  OE2
REMARK 470     ILE E 379    CG1  CG2  CD1
REMARK 470     GLU E 380    CG   CD   OE1  OE2
REMARK 470     LEU E 421    CG   CD1  CD2
REMARK 470     GLU E 423    CG   CD   OE1  OE2
REMARK 470     LYS E 426    CG   CD   CE   NZ
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     VAL E 444    CG1  CG2
REMARK 470     ILE F   8    CG1  CG2  CD1
REMARK 470     ASP F  10    CG   OD1  OD2
REMARK 470     GLU F  18    CG   CD   OE1  OE2
REMARK 470     THR F  54    OG1  CG2
REMARK 470     THR F  57    OG1  CG2
REMARK 470     LEU F  58    CG   CD1  CD2
REMARK 470     TYR F  59    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     LYS F 153    CG   CD   CE   NZ
REMARK 470     GLU F 203    CG   CD   OE1  OE2
REMARK 470     ASN F 218    CG   OD1  ND2
REMARK 470     GLU F 346    CG   CD   OE1  OE2
REMARK 470     GLU F 380    CG   CD   OE1  OE2
REMARK 470     LEU F 421    CG   CD1  CD2
REMARK 470     GLU F 423    CG   CD   OE1  OE2
REMARK 470     LYS F 429    CG   CD   CE   NZ
REMARK 470     ILE G   8    CG1  CG2  CD1
REMARK 470     ASP G  10    CG   OD1  OD2
REMARK 470     THR G  54    OG1  CG2
REMARK 470     THR G  57    OG1  CG2
REMARK 470     LEU G  58    CG   CD1  CD2
REMARK 470     GLU G 144    CG   CD   OE1  OE2
REMARK 470     LYS G 153    CG   CD   CE   NZ
REMARK 470     ASP G 328    CG   OD1  OD2
REMARK 470     GLU G 346    CG   CD   OE1  OE2
REMARK 470     GLN G 376    CG   CD   OE1  NE2
REMARK 470     GLU G 380    CG   CD   OE1  OE2
REMARK 470     LYS G 426    CG   CD   CE   NZ
REMARK 470     LYS G 429    CG   CD   CE   NZ
REMARK 470     VAL G 441    CG1  CG2
REMARK 470     THR H   7    OG1  CG2
REMARK 470     ILE H   8    CG1  CG2  CD1
REMARK 470     ASP H  10    CG   OD1  OD2
REMARK 470     TYR H  59    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     GLU H 144    CG   CD   OE1  OE2
REMARK 470     LYS H 153    CG   CD   CE   NZ
REMARK 470     GLU H 326    CG   CD   OE1  OE2
REMARK 470     ASP H 328    CG   OD1  OD2
REMARK 470     GLU H 380    CG   CD   OE1  OE2
REMARK 470     LEU H 421    CG   CD1  CD2
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     GLU H 436    CG   CD   OE1  OE2
REMARK 470     VAL H 441    CG1  CG2
REMARK 470     PHE I   5    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     ASP I   6    CG   OD1  OD2
REMARK 470     THR I  57    OG1  CG2
REMARK 470     GLU I 326    CG   CD   OE1  OE2
REMARK 470     SER I 340    OG
REMARK 470     GLU I 346    CG   CD   OE1  OE2
REMARK 470     GLN I 376    CG   CD   OE1  NE2
REMARK 470     GLU I 423    CG   CD   OE1  OE2
REMARK 470     LYS I 426    CG   CD   CE   NZ
REMARK 470     LEU I 435    CG   CD1  CD2
REMARK 470     ILE J   8    CG1  CG2  CD1
REMARK 470     LEU J  58    CG   CD1  CD2
REMARK 470     TYR J  59    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     GLU J 144    CG   CD   OE1  OE2
REMARK 470     LEU J 235    CG   CD1  CD2
REMARK 470     LYS J 322    CG   CD   CE   NZ
REMARK 470     LEU J 323    CG   CD1  CD2
REMARK 470     GLU J 324    CG   CD   OE1  OE2
REMARK 470     GLU J 346    CG   CD   OE1  OE2
REMARK 470     VAL J 378    CG1  CG2
REMARK 470     GLU J 380    CG   CD   OE1  OE2
REMARK 470     LEU J 421    CG   CD1  CD2
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     LEU J 431    CG   CD1  CD2
REMARK 470     VAL J 441    CG1  CG2
REMARK 470     THR J 442    OG1  CG2
REMARK 470     VAL J 444    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     -101.77   -139.57
REMARK 500    ASP A  82       13.57   -141.37
REMARK 500    ALA A 109       36.18   -150.11
REMARK 500    THR A 195     -107.88   -121.80
REMARK 500    ASN A 200       83.07   -163.17
REMARK 500    ALA A 232     -173.49    179.35
REMARK 500    MET A 284      -18.41    106.17
REMARK 500    TYR A 357     -111.72     50.26
REMARK 500    ASP B  10       -4.44    -59.82
REMARK 500    SER B  51     -109.86   -134.69
REMARK 500    ALA B 109       40.65   -147.44
REMARK 500    THR B 195     -109.54   -118.25
REMARK 500    ASN B 200       77.71   -166.83
REMARK 500    ALA B 232     -179.23    179.55
REMARK 500    MET B 284      -19.79     98.02
REMARK 500    TYR B 357     -116.13     53.36
REMARK 500    HIS B 428       98.58   -160.93
REMARK 500    ASP C  14       83.71   -155.64
REMARK 500    SER C  51      -99.41   -136.93
REMARK 500    THR C  56     -168.93   -124.28
REMARK 500    ALA C 109       35.83   -146.16
REMARK 500    THR C 195     -112.62   -113.22
REMARK 500    ASN C 200       71.30   -154.84
REMARK 500    ALA C 232     -172.22    177.18
REMARK 500    MET C 284      -18.10     97.32
REMARK 500    ALA C 318       31.83     78.60
REMARK 500    TYR C 357     -111.55     54.03
REMARK 500    PRO C 377        0.93    -69.20
REMARK 500    THR C 394      -52.72   -121.44
REMARK 500    PRO C 420      143.78    -31.73
REMARK 500    ARG C 433        5.81    -63.14
REMARK 500    SER D  51     -128.37   -135.64
REMARK 500    ALA D 109       29.10   -152.23
REMARK 500    ASP D 154      -36.73   -134.73
REMARK 500    THR D 195     -114.10   -115.36
REMARK 500    ASN D 200       77.08   -165.83
REMARK 500    ALA D 232     -168.39   -177.73
REMARK 500    ALA D 283      135.93    -38.03
REMARK 500    MET D 284      -27.10     94.47
REMARK 500    TYR D 357     -120.76     60.41
REMARK 500    THR D 394      -63.86   -126.55
REMARK 500    LEU D 395       12.26    -69.68
REMARK 500    GLN D 410      -71.08    -66.68
REMARK 500    GLN D 417      -72.57    -92.69
REMARK 500    GLU D 423      -81.94    -66.57
REMARK 500    SER E  51      -93.45   -142.32
REMARK 500    ASP E 154      -30.79   -132.76
REMARK 500    THR E 195     -111.28   -108.91
REMARK 500    ASN E 200       75.75   -158.41
REMARK 500    THR E 231      129.55    -39.99
REMARK 500
REMARK 500 THIS ENTRY HAS     108 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   OQ1
REMARK 620 2 ASP A 191   OD1  99.5
REMARK 620 3 GLU A 192   OE1  89.7  78.4
REMARK 620 4 CAP A 446   O3   83.5 160.5  82.5
REMARK 620 5 CAP A 446   O2   95.1 119.2 160.5  79.3
REMARK 620 6 CAP A 446   O7  170.7  86.1  98.7  93.6  75.7
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   OQ1
REMARK 620 2 ASP B 191   OD1  94.1
REMARK 620 3 GLU B 192   OE1  72.8 102.1
REMARK 620 4 CAP B 446   O2   79.5  99.4 145.7
REMARK 620 5 CAP B 446   O3   67.4 161.4  74.8  76.3
REMARK 620 6 CAP B 446   O7  166.2  93.1 117.1  87.7 104.7
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   OQ1
REMARK 620 2 GLU C 192   OE1  77.4
REMARK 620 3 CAP C 446   O7  155.9 112.1
REMARK 620 4 CAP C 446   O2   86.3 156.6  77.2
REMARK 620 5 CAP C 446   O3   68.3  81.2  90.7  77.2
REMARK 620 N                    1     2     3     4
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   OQ1
REMARK 620 2 ASP D 191   OD1 102.6
REMARK 620 3 GLU D 192   OE1  89.9  77.6
REMARK 620 4 CAP D 446   O2   88.5 123.9 158.2
REMARK 620 5 CAP D 446   O3   78.8 155.2  77.6  80.8
REMARK 620 6 CAP D 446   O7  165.2  92.1  92.0  84.3  87.3
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA E 445  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX E 189   OQ1
REMARK 620 2 ASP E 191   OD1  89.3
REMARK 620 3 GLU E 192   OE1  78.0  80.3
REMARK 620 4 CAP E 446   O6   87.0 161.9  81.6
REMARK 620 5 CAP E 446   O4   97.9 132.7 146.9  65.3
REMARK 620 6 HOH E 666   O   166.1 101.9  95.6  79.8  80.6
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 KCX F 189   OQ1
REMARK 620 2 ASP F 191   OD1  91.6
REMARK 620 3 GLU F 192   OE1  86.6  79.0
REMARK 620 4 CAP F 446   O3   84.5 163.4  84.6
REMARK 620 5 CAP F 446   O7  173.8  90.9  99.5  94.7
REMARK 620 6 CAP F 446   O2   94.2 116.9 164.0  79.5  79.6
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   OQ1
REMARK 620 2 ASP G 191   OD1  91.8
REMARK 620 3 GLU G 192   OE1  80.0  99.1
REMARK 620 4 CAP G 446   O2   83.8  98.4 156.4
REMARK 620 5 CAP G 446   O3   74.2 165.8  80.7  78.4
REMARK 620 6 CAP G 446   O7  167.7  88.0 112.1  84.1 105.3
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   OQ1
REMARK 620 2 GLU H 192   OE1  77.2
REMARK 620 3 CAP H 446   O2   81.1 147.8
REMARK 620 4 CAP H 446   O7  151.4 113.5  77.0
REMARK 620 5 CAP H 446   O3   67.1  77.3  72.4  88.7
REMARK 620 N                    1     2     3     4
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   OQ1
REMARK 620 2 ASP I 191   OD1  93.6
REMARK 620 3 GLU I 192   OE1  80.5  71.3
REMARK 620 4 CAP I 446   O3   75.4 144.6  73.8
REMARK 620 5 CAP I 446   O7  166.7  97.0  95.2  91.3
REMARK 620 6 CAP I 446   O2   92.1 135.9 152.6  78.8  86.0
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA J 445  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX J 189   OQ1
REMARK 620 2 ASP J 191   OD2  89.7
REMARK 620 3 GLU J 192   OE1  79.4  80.2
REMARK 620 4 CAP J 446   O6   82.6 161.1  81.4
REMARK 620 5 CAP J 446   O4   96.4 133.7 146.1  64.7
REMARK 620 6 HOH J 678   O   164.3 105.5  99.1  81.8  76.0
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 CA 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 CA 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: 3A12   RELATED DB: PDB
DBREF  3A13 A    1   444  UNP    O93627   RBL_PYRKO        1    444
DBREF  3A13 B    1   444  UNP    O93627   RBL_PYRKO        1    444
DBREF  3A13 C    1   444  UNP    O93627   RBL_PYRKO        1    444
DBREF  3A13 D    1   444  UNP    O93627   RBL_PYRKO        1    444
DBREF  3A13 E    1   444  UNP    O93627   RBL_PYRKO        1    444
DBREF  3A13 F    1   444  UNP    O93627   RBL_PYRKO        1    444
DBREF  3A13 G    1   444  UNP    O93627   RBL_PYRKO        1    444
DBREF  3A13 H    1   444  UNP    O93627   RBL_PYRKO        1    444
DBREF  3A13 I    1   444  UNP    O93627   RBL_PYRKO        1    444
DBREF  3A13 J    1   444  UNP    O93627   RBL_PYRKO        1    444
SEQADV 3A13 GLU A  326  UNP  O93627    GLY   326 ENGINEERED
SEQADV 3A13 ARG A  327  UNP  O93627    LYS   327 ENGINEERED
SEQADV 3A13 ASP A  328  UNP  O93627    TRP   328 ENGINEERED
SEQADV 3A13 ILE A  329  UNP  O93627    ASP   329 ENGINEERED
SEQADV 3A13 THR A  330  UNP  O93627    VAL   330 ENGINEERED
SEQADV 3A13 GLU B  326  UNP  O93627    GLY   326 ENGINEERED
SEQADV 3A13 ARG B  327  UNP  O93627    LYS   327 ENGINEERED
SEQADV 3A13 ASP B  328  UNP  O93627    TRP   328 ENGINEERED
SEQADV 3A13 ILE B  329  UNP  O93627    ASP   329 ENGINEERED
SEQADV 3A13 THR B  330  UNP  O93627    VAL   330 ENGINEERED
SEQADV 3A13 GLU C  326  UNP  O93627    GLY   326 ENGINEERED
SEQADV 3A13 ARG C  327  UNP  O93627    LYS   327 ENGINEERED
SEQADV 3A13 ASP C  328  UNP  O93627    TRP   328 ENGINEERED
SEQADV 3A13 ILE C  329  UNP  O93627    ASP   329 ENGINEERED
SEQADV 3A13 THR C  330  UNP  O93627    VAL   330 ENGINEERED
SEQADV 3A13 GLU D  326  UNP  O93627    GLY   326 ENGINEERED
SEQADV 3A13 ARG D  327  UNP  O93627    LYS   327 ENGINEERED
SEQADV 3A13 ASP D  328  UNP  O93627    TRP   328 ENGINEERED
SEQADV 3A13 ILE D  329  UNP  O93627    ASP   329 ENGINEERED
SEQADV 3A13 THR D  330  UNP  O93627    VAL   330 ENGINEERED
SEQADV 3A13 GLU E  326  UNP  O93627    GLY   326 ENGINEERED
SEQADV 3A13 ARG E  327  UNP  O93627    LYS   327 ENGINEERED
SEQADV 3A13 ASP E  328  UNP  O93627    TRP   328 ENGINEERED
SEQADV 3A13 ILE E  329  UNP  O93627    ASP   329 ENGINEERED
SEQADV 3A13 THR E  330  UNP  O93627    VAL   330 ENGINEERED
SEQADV 3A13 GLU F  326  UNP  O93627    GLY   326 ENGINEERED
SEQADV 3A13 ARG F  327  UNP  O93627    LYS   327 ENGINEERED
SEQADV 3A13 ASP F  328  UNP  O93627    TRP   328 ENGINEERED
SEQADV 3A13 ILE F  329  UNP  O93627    ASP   329 ENGINEERED
SEQADV 3A13 THR F  330  UNP  O93627    VAL   330 ENGINEERED
SEQADV 3A13 GLU G  326  UNP  O93627    GLY   326 ENGINEERED
SEQADV 3A13 ARG G  327  UNP  O93627    LYS   327 ENGINEERED
SEQADV 3A13 ASP G  328  UNP  O93627    TRP   328 ENGINEERED
SEQADV 3A13 ILE G  329  UNP  O93627    ASP   329 ENGINEERED
SEQADV 3A13 THR G  330  UNP  O93627    VAL   330 ENGINEERED
SEQADV 3A13 GLU H  326  UNP  O93627    GLY   326 ENGINEERED
SEQADV 3A13 ARG H  327  UNP  O93627    LYS   327 ENGINEERED
SEQADV 3A13 ASP H  328  UNP  O93627    TRP   328 ENGINEERED
SEQADV 3A13 ILE H  329  UNP  O93627    ASP   329 ENGINEERED
SEQADV 3A13 THR H  330  UNP  O93627    VAL   330 ENGINEERED
SEQADV 3A13 GLU I  326  UNP  O93627    GLY   326 ENGINEERED
SEQADV 3A13 ARG I  327  UNP  O93627    LYS   327 ENGINEERED
SEQADV 3A13 ASP I  328  UNP  O93627    TRP   328 ENGINEERED
SEQADV 3A13 ILE I  329  UNP  O93627    ASP   329 ENGINEERED
SEQADV 3A13 THR I  330  UNP  O93627    VAL   330 ENGINEERED
SEQADV 3A13 GLU J  326  UNP  O93627    GLY   326 ENGINEERED
SEQADV 3A13 ARG J  327  UNP  O93627    LYS   327 ENGINEERED
SEQADV 3A13 ASP J  328  UNP  O93627    TRP   328 ENGINEERED
SEQADV 3A13 ILE J  329  UNP  O93627    ASP   329 ENGINEERED
SEQADV 3A13 THR J  330  UNP  O93627    VAL   330 ENGINEERED
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  GLU ARG ASP ILE THR 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  GLU ARG ASP ILE THR 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  GLU ARG ASP ILE THR 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  GLU ARG ASP ILE THR 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  GLU ARG ASP ILE THR 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  GLU ARG ASP ILE THR 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  GLU ARG ASP ILE THR 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  GLU ARG ASP ILE THR 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  GLU ARG ASP ILE THR 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  GLU ARG ASP ILE THR 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 3A13 KCX A  189  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 3A13 KCX B  189  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 3A13 KCX C  189  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 3A13 KCX D  189  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 3A13 KCX E  189  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 3A13 KCX F  189  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 3A13 KCX G  189  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 3A13 KCX H  189  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 3A13 KCX I  189  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 3A13 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     CA  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     CA  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
HETNAM      CA CALCIUM ION
FORMUL   1  KCX    10(C7 H14 N2 O4)
FORMUL  11   MG    8(MG 2+)
FORMUL  12  CAP    10(C6 H14 O13 P2)
FORMUL  19   CA    2(CA 2+)
FORMUL  31  HOH   *1951(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 GLU 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  GLN A  417  1                                  18
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 TYR B    9  VAL B   13  5                                   5
HELIX   24  24 THR B   38  SER B   50  1                                  13
HELIX   25  25 GLU B   63  LEU B   70  1                                   8
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 ALA B  263  GLY B  275  1                                  13
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 GLU B  326  GLU B  339  1                                  14
HELIX   39  39 ILE B  375  GLY B  383  1                                   9
HELIX   40  40 GLY B  391  GLY B  396  1                                   6
HELIX   41  41 ASP B  399  GLY B  418  1                                  20
HELIX   42  42 PRO B  420  ALA B  425  1                                   6
HELIX   43  43 HIS B  428  GLY B  439  1                                  12
HELIX   44  44 TYR C    9  VAL C   13  5                                   5
HELIX   45  45 THR C   38  SER C   50  1                                  13
HELIX   46  46 GLU C   63  SER C   71  1                                   9
HELIX   47  47 HIS C   94  PHE C   96  5                                   3
HELIX   48  48 ASN C  100  ALA C  109  1                                  10
HELIX   49  49 GLY C  110  MET C  115  5                                   6
HELIX   50  50 PRO C  129  ARG C  134  1                                   6
HELIX   51  51 PHE C  141  GLU C  151  1                                  11
HELIX   52  52 SER C  169  ASN C  183  1                                  15
HELIX   53  53 ARG C  201  GLY C  221  1                                  21
HELIX   54  54 ASP C  233  LEU C  247  1                                  15
HELIX   55  55 VAL C  256  GLY C  260  1                                   5
HELIX   56  56 GLY C  260  TYR C  274  1                                  15
HELIX   57  57 HIS C  285  ARG C  290  1                                   6
HELIX   58  58 SER C  297  GLY C  309  1                                  13
HELIX   59  59 GLU C  326  GLU C  339  1                                  14
HELIX   60  60 ILE C  375  GLY C  383  1                                   9
HELIX   61  61 GLY C  391  GLY C  396  1                                   6
HELIX   62  62 GLY C  400  MET C  416  1                                  17
HELIX   63  63 PRO C  420  ALA C  425  1                                   6
HELIX   64  64 HIS C  428  GLY C  439  1                                  12
HELIX   65  65 PHE D    5  VAL D   13  1                                   9
HELIX   66  66 THR D   38  SER D   50  1                                  13
HELIX   67  67 GLU D   63  LEU D   70  1                                   8
HELIX   68  68 HIS D   94  PHE D   96  5                                   3
HELIX   69  69 ASN D  100  ALA D  109  1                                  10
HELIX   70  70 GLY D  110  MET D  115  5                                   6
HELIX   71  71 PRO D  129  ARG D  134  1                                   6
HELIX   72  72 PHE D  141  GLU D  151  1                                  11
HELIX   73  73 SER D  169  ASN D  183  1                                  15
HELIX   74  74 ARG D  201  GLY D  221  1                                  21
HELIX   75  75 ASP D  233  LEU D  247  1                                  15
HELIX   76  76 VAL D  256  GLY D  260  1                                   5
HELIX   77  77 GLY D  260  GLY D  275  1                                  16
HELIX   78  78 HIS D  285  ARG D  290  1                                   6
HELIX   79  79 SER D  297  GLY D  309  1                                  13
HELIX   80  80 GLU D  326  GLU D  339  1                                  14
HELIX   81  81 HIS D  371  ASN D  374  5                                   4
HELIX   82  82 ILE D  375  GLY D  383  1                                   9
HELIX   83  83 GLY D  400  GLY D  418  1                                  19
HELIX   84  84 PRO D  420  LYS D  426  1                                   7
HELIX   85  85 HIS D  428  GLY D  439  1                                  12
HELIX   86  86 ILE E    8  VAL E   13  5                                   6
HELIX   87  87 THR E   38  SER E   50  1                                  13
HELIX   88  88 GLU E   63  LEU E   70  1                                   8
HELIX   89  89 HIS E   94  PHE E   96  5                                   3
HELIX   90  90 ASN E  100  ALA E  109  1                                  10
HELIX   91  91 GLY E  110  MET E  115  5                                   6
HELIX   92  92 PRO E  129  ARG E  134  1                                   6
HELIX   93  93 PHE E  141  LEU E  150  1                                  10
HELIX   94  94 SER E  169  ASN E  183  1                                  15
HELIX   95  95 ARG E  201  GLY E  221  1                                  21
HELIX   96  96 ASP E  233  LEU E  247  1                                  15
HELIX   97  97 VAL E  256  GLY E  260  1                                   5
HELIX   98  98 GLY E  260  TYR E  274  1                                  15
HELIX   99  99 MET E  284  PHE E  288  5                                   5
HELIX  100 100 SER E  297  GLY E  309  1                                  13
HELIX  101 101 GLU E  326  GLU E  339  1                                  14
HELIX  102 102 ASN E  374  GLY E  383  1                                  10
HELIX  103 103 GLY E  391  GLY E  396  1                                   6
HELIX  104 104 GLY E  400  GLN E  417  1                                  18
HELIX  105 105 PRO E  420  LYS E  426  1                                   7
HELIX  106 106 HIS E  428  GLY E  439  1                                  12
HELIX  107 107 TYR F    9  VAL F   13  5                                   5
HELIX  108 108 THR F   38  SER F   50  1                                  13
HELIX  109 109 GLU F   63  SER F   71  1                                   9
HELIX  110 110 HIS F   94  PHE F   96  5                                   3
HELIX  111 111 ASN F  100  ALA F  109  1                                  10
HELIX  112 112 GLY F  110  MET F  115  5                                   6
HELIX  113 113 PRO F  129  ARG F  134  1                                   6
HELIX  114 114 PHE F  141  GLU F  151  1                                  11
HELIX  115 115 SER F  169  ASN F  183  1                                  15
HELIX  116 116 ARG F  201  GLY F  221  1                                  21
HELIX  117 117 ASP F  233  LEU F  247  1                                  15
HELIX  118 118 VAL F  256  GLY F  260  1                                   5
HELIX  119 119 GLY F  260  GLY F  275  1                                  16
HELIX  120 120 HIS F  285  ARG F  290  1                                   6
HELIX  121 121 SER F  297  GLY F  309  1                                  13
HELIX  122 122 GLU F  326  GLU F  339  1                                  14
HELIX  123 123 ILE F  375  GLY F  383  1                                   9
HELIX  124 124 GLY F  391  GLY F  396  1                                   6
HELIX  125 125 GLY F  400  MET F  416  1                                  17
HELIX  126 126 PRO F  420  LYS F  426  1                                   7
HELIX  127 127 HIS F  428  GLY F  439  1                                  12
HELIX  128 128 ILE G    8  VAL G   13  5                                   6
HELIX  129 129 THR G   38  SER G   50  1                                  13
HELIX  130 130 GLU G   63  LEU G   70  1                                   8
HELIX  131 131 HIS G   94  PHE G   96  5                                   3
HELIX  132 132 ASN G  100  ALA G  109  1                                  10
HELIX  133 133 GLY G  110  MET G  115  5                                   6
HELIX  134 134 PRO G  129  ARG G  134  1                                   6
HELIX  135 135 PHE G  141  GLU G  151  1                                  11
HELIX  136 136 SER G  169  ASN G  183  1                                  15
HELIX  137 137 ARG G  201  GLY G  221  1                                  21
HELIX  138 138 ASP G  233  LEU G  247  1                                  15
HELIX  139 139 VAL G  256  GLY G  260  1                                   5
HELIX  140 140 GLY G  260  GLY G  275  1                                  16
HELIX  141 141 HIS G  285  ARG G  290  1                                   6
HELIX  142 142 SER G  297  GLY G  309  1                                  13
HELIX  143 143 GLU G  326  GLU G  339  1                                  14
HELIX  144 144 ILE G  375  GLY G  383  1                                   9
HELIX  145 145 GLY G  391  GLY G  396  1                                   6
HELIX  146 146 GLY G  400  GLY G  418  1                                  19
HELIX  147 147 PRO G  420  LYS G  426  1                                   7
HELIX  148 148 HIS G  428  GLY G  439  1                                  12
HELIX  149 149 TYR H    9  VAL H   13  5                                   5
HELIX  150 150 THR H   38  SER H   50  1                                  13
HELIX  151 151 GLU H   63  SER H   71  1                                   9
HELIX  152 152 HIS H   94  PHE H   96  5                                   3
HELIX  153 153 ASN H  100  ALA H  109  1                                  10
HELIX  154 154 GLY H  110  MET H  115  5                                   6
HELIX  155 155 PRO H  129  ARG H  134  1                                   6
HELIX  156 156 PHE H  141  GLU H  151  1                                  11
HELIX  157 157 SER H  169  ASN H  183  1                                  15
HELIX  158 158 ARG H  201  GLY H  221  1                                  21
HELIX  159 159 ASP H  233  LEU H  247  1                                  15
HELIX  160 160 VAL H  256  GLY H  260  1                                   5
HELIX  161 161 GLY H  260  TYR H  274  1                                  15
HELIX  162 162 HIS H  285  ARG H  290  1                                   6
HELIX  163 163 SER H  297  GLY H  309  1                                  13
HELIX  164 164 GLU H  326  GLU H  339  1                                  14
HELIX  165 165 ILE H  375  GLY H  383  1                                   9
HELIX  166 166 GLY H  391  GLY H  396  1                                   6
HELIX  167 167 GLY H  400  MET H  416  1                                  17
HELIX  168 168 PRO H  420  ALA H  425  1                                   6
HELIX  169 169 HIS H  428  GLY H  439  1                                  12
HELIX  170 170 PHE I    5  VAL I   13  1                                   9
HELIX  171 171 THR I   38  SER I   50  1                                  13
HELIX  172 172 GLU I   63  LEU I   70  1                                   8
HELIX  173 173 HIS I   94  PHE I   96  5                                   3
HELIX  174 174 ASN I  100  ALA I  109  1                                  10
HELIX  175 175 GLY I  110  MET I  115  5                                   6
HELIX  176 176 PRO I  129  ARG I  134  1                                   6
HELIX  177 177 PHE I  141  LEU I  150  1                                  10
HELIX  178 178 SER I  169  ASN I  183  1                                  15
HELIX  179 179 ARG I  201  GLY I  221  1                                  21
HELIX  180 180 ASP I  233  LEU I  247  1                                  15
HELIX  181 181 VAL I  256  GLY I  260  1                                   5
HELIX  182 182 GLY I  260  TYR I  274  1                                  15
HELIX  183 183 HIS I  285  ARG I  290  1                                   6
HELIX  184 184 SER I  297  GLY I  309  1                                  13
HELIX  185 185 GLU I  326  GLU I  339  1                                  14
HELIX  186 186 ILE I  375  GLY I  383  1                                   9
HELIX  187 187 GLY I  391  GLY I  396  1                                   6
HELIX  188 188 GLY I  400  GLY I  418  1                                  19
HELIX  189 189 PRO I  420  THR I  427  1                                   8
HELIX  190 190 HIS I  428  GLY I  439  1                                  12
HELIX  191 191 TYR J    9  VAL J   13  5                                   5
HELIX  192 192 THR J   38  SER J   50  1                                  13
HELIX  193 193 GLU J   63  SER J   71  1                                   9
HELIX  194 194 HIS J   94  PHE J   96  5                                   3
HELIX  195 195 ASN J  100  ALA J  109  1                                  10
HELIX  196 196 GLY J  110  MET J  115  5                                   6
HELIX  197 197 PRO J  129  ARG J  134  1                                   6
HELIX  198 198 PHE J  141  GLU J  151  1                                  11
HELIX  199 199 SER J  169  ASN J  183  1                                  15
HELIX  200 200 ARG J  201  GLY J  221  1                                  21
HELIX  201 201 ASP J  233  LEU J  247  1                                  15
HELIX  202 202 VAL J  256  GLY J  260  1                                   5
HELIX  203 203 GLY J  260  TYR J  274  1                                  15
HELIX  204 204 MET J  284  PHE J  288  5                                   5
HELIX  205 205 SER J  297  GLY J  309  1                                  13
HELIX  206 206 GLU J  326  GLU J  339  1                                  14
HELIX  207 207 ASN J  374  GLY J  383  1                                  10
HELIX  208 208 GLY J  391  GLY J  396  1                                   6
HELIX  209 209 GLY J  400  GLN J  417  1                                  18
HELIX  210 210 PRO J  420  LYS J  426  1                                   7
HELIX  211 211 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  ILE A  25   O  TYR A  91
SHEET    4   A 5 VAL A 118  TYR A 127 -1  O  ARG A 122   N  ARG A  30
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  ALA A 277   N  ALA A 252
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  TYR B 127   N  ILE B  26
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 366  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  PRO B 364
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  ILE C  86   N  HIS C  78
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  GLU C 124   N  VAL C  28
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  ALA C 252
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 121
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  HIS D 281   N  VAL D 254
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  ALA E  90   N  LYS E  73
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  GLU E 124   N  VAL E  28
SHEET    5   M 5 GLY E 295  ILE E 296  1  O  GLY E 295   N  LEU E 123
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  HIS E 279   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  THR E 365   N  LEU E 313
SHEET    8   N 9 VAL E 387  GLN E 389  1  O  VAL E 387   N  PRO E 364
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  79  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 121
SHEET    1   Q 9 ILE F 157  VAL F 160  0
SHEET    2   Q 9 TYR F 187  KCX F 189  1  O  KCX F 189   N  VAL F 160
SHEET    3   Q 9 THR F 225  ASN F 229  1  O  PHE F 227   N  MET F 188
SHEET    4   Q 9 HIS F 251  ASP F 255  1  O  MET F 253   N  ALA F 228
SHEET    5   Q 9 ALA F 277  HIS F 281  1  O  HIS F 281   N  VAL F 254
SHEET    6   Q 9 GLN F 312  HIS F 314  1  O  GLN F 312   N  GLY F 280
SHEET    7   Q 9 PHE F 363  SER F 367  1  O  THR F 365   N  LEU F 313
SHEET    8   Q 9 VAL F 387  GLN F 389  1  O  VAL F 387   N  SER F 366
SHEET    9   Q 9 ILE F 157  VAL F 160  1  N  ILE F 157   O  LEU F 388
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  ALA G  90   N  LYS G  73
SHEET    3   S 5 ASP G  24  PRO G  33 -1  N  VAL G  31   O  TRP G  85
SHEET    4   S 5 VAL G 118  TYR G 127 -1  O  GLU G 124   N  VAL G  28
SHEET    5   S 5 GLY G 295  ILE G 296  1  O  GLY G 295   N  LEU G 123
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 281   N  VAL G 254
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 366  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  VAL H  31   O  TRP H  85
SHEET    4   V 5 VAL H 118  TYR H 127 -1  O  GLU H 124   N  VAL H  28
SHEET    5   V 5 GLY H 295  ILE H 296  1  O  GLY H 295   N  LEU H 121
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  TYR H 187
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  SER H 366   O  VAL H 387
SHEET    6   W 8 GLN H 312  HIS H 314  1  N  LEU H 313   O  THR H 365
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  ALA H 252   O  HIS H 279
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  ILE I  25   O  TYR I  91
SHEET    4   Y 5 VAL I 118  TYR I 127 -1  O  GLU I 124   N  VAL I  28
SHEET    5   Y 5 GLY I 295  ILE I 296  1  O  GLY I 295   N  LEU I 121
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  HIS I 279   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  ALA J  90   N  LYS J  73
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 9 ILE J 157  VAL J 160  0
SHEET    2  AC 9 TYR J 187  KCX J 189  1  O  KCX J 189   N  VAL J 160
SHEET    3  AC 9 THR J 225  ASN J 229  1  O  PHE J 227   N  MET J 188
SHEET    4  AC 9 HIS J 251  ASP J 255  1  O  MET J 253   N  ALA J 228
SHEET    5  AC 9 ALA J 277  HIS J 281  1  O  HIS J 279   N  ALA J 252
SHEET    6  AC 9 GLN J 312  HIS J 314  1  O  GLN J 312   N  GLY J 280
SHEET    7  AC 9 PHE J 363  SER J 367  1  O  THR J 365   N  LEU J 313
SHEET    8  AC 9 VAL J 387  GLN J 389  1  O  VAL J 387   N  SER J 366
SHEET    9  AC 9 ILE J 157  VAL J 160  1  N  ILE J 157   O  LEU J 388
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  1.33
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  1.32
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  1.34
LINK         C   MET G 188                 N   KCX G 189     1555   1555  1.33
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         OQ1 KCX A 189                MG    MG A 445     1555   1555  2.06
LINK         OD1 ASP A 191                MG    MG A 445     1555   1555  2.18
LINK         OE1 GLU A 192                MG    MG A 445     1555   1555  2.06
LINK         OQ1 KCX B 189                MG    MG B 445     1555   1555  2.32
LINK         OD1 ASP B 191                MG    MG B 445     1555   1555  2.38
LINK         OE1 GLU B 192                MG    MG B 445     1555   1555  2.37
LINK         OQ1 KCX C 189                MG    MG C 445     1555   1555  2.32
LINK         OE1 GLU C 192                MG    MG C 445     1555   1555  2.27
LINK         OQ1 KCX D 189                MG    MG D 445     1555   1555  2.22
LINK         OD1 ASP D 191                MG    MG D 445     1555   1555  2.14
LINK         OE1 GLU D 192                MG    MG D 445     1555   1555  2.11
LINK         OQ1 KCX E 189                CA    CA E 445     1555   1555  2.36
LINK         OD1 ASP E 191                CA    CA E 445     1555   1555  2.45
LINK         OE1 GLU E 192                CA    CA E 445     1555   1555  2.32
LINK         OQ1 KCX F 189                MG    MG F 445     1555   1555  2.01
LINK         OD1 ASP F 191                MG    MG F 445     1555   1555  2.02
LINK         OE1 GLU F 192                MG    MG F 445     1555   1555  2.03
LINK         OQ1 KCX G 189                MG    MG G 445     1555   1555  2.14
LINK         OD1 ASP G 191                MG    MG G 445     1555   1555  2.12
LINK         OE1 GLU G 192                MG    MG G 445     1555   1555  2.26
LINK         OQ1 KCX H 189                MG    MG H 445     1555   1555  2.19
LINK         OE1 GLU H 192                MG    MG H 445     1555   1555  2.30
LINK         OQ1 KCX I 189                MG    MG I 445     1555   1555  2.30
LINK         OD1 ASP I 191                MG    MG I 445     1555   1555  2.07
LINK         OE1 GLU I 192                MG    MG I 445     1555   1555  2.19
LINK         OQ1 KCX J 189                CA    CA J 445     1555   1555  2.35
LINK         OD2 ASP J 191                CA    CA J 445     1555   1555  2.39
LINK         OE1 GLU J 192                CA    CA J 445     1555   1555  2.36
LINK        MG    MG A 445                 O3  CAP A 446     1555   1555  2.18
LINK        MG    MG A 445                 O2  CAP A 446     1555   1555  2.29
LINK        MG    MG A 445                 O7  CAP A 446     1555   1555  1.99
LINK        MG    MG B 445                 O2  CAP B 446     1555   1555  2.04
LINK        MG    MG B 445                 O3  CAP B 446     1555   1555  2.23
LINK        MG    MG C 445                 O7  CAP C 446     1555   1555  2.25
LINK        MG    MG C 445                 O2  CAP C 446     1555   1555  2.05
LINK        MG    MG C 445                 O3  CAP C 446     1555   1555  2.25
LINK        MG    MG D 445                 O2  CAP D 446     1555   1555  2.21
LINK        MG    MG D 445                 O3  CAP D 446     1555   1555  2.20
LINK        MG    MG D 445                 O7  CAP D 446     1555   1555  1.84
LINK        CA    CA E 445                 O6  CAP E 446     1555   1555  2.48
LINK        CA    CA E 445                 O4  CAP E 446     1555   1555  2.67
LINK        MG    MG F 445                 O3  CAP F 446     1555   1555  2.23
LINK        MG    MG F 445                 O7  CAP F 446     1555   1555  1.85
LINK        MG    MG F 445                 O2  CAP F 446     1555   1555  2.32
LINK        MG    MG G 445                 O2  CAP G 446     1555   1555  2.10
LINK        MG    MG G 445                 O3  CAP G 446     1555   1555  2.17
LINK        MG    MG H 445                 O2  CAP H 446     1555   1555  2.15
LINK        MG    MG H 445                 O7  CAP H 446     1555   1555  2.17
LINK        MG    MG H 445                 O3  CAP H 446     1555   1555  2.35
LINK        MG    MG I 445                 O3  CAP I 446     1555   1555  2.30
LINK        MG    MG I 445                 O7  CAP I 446     1555   1555  1.85
LINK        MG    MG I 445                 O2  CAP I 446     1555   1555  2.09
LINK        CA    CA J 445                 O6  CAP J 446     1555   1555  2.42
LINK        CA    CA J 445                 O4  CAP J 446     1555   1555  2.77
LINK        CA    CA E 445                 O   HOH E 666     1555   1555  2.28
LINK        CA    CA J 445                 O   HOH J 678     1555   1555  2.30
LINK        MG    MG B 445                 O7  CAP B 446     1555   1555  1.73
LINK        MG    MG G 445                 O7  CAP G 446     1555   1555  1.75
CISPEP   1 LYS A  163    PRO A  164          0         8.51
CISPEP   2 LYS B  163    PRO B  164          0         9.06
CISPEP   3 LYS C  163    PRO C  164          0         5.81
CISPEP   4 LYS D  163    PRO D  164          0         3.17
CISPEP   5 LYS E  163    PRO E  164          0         6.62
CISPEP   6 LYS F  163    PRO F  164          0         9.91
CISPEP   7 LYS G  163    PRO G  164          0        11.01
CISPEP   8 LYS H  163    PRO H  164          0         5.17
CISPEP   9 LYS I  163    PRO I  164          0         7.13
CISPEP  10 LYS J  163    PRO J  164          0         4.16
SITE     1 AC1  4 KCX A 189  ASP A 191  GLU A 192  CAP A 446
SITE     1 AC2 29 LYS A 163  LYS A 165  KCX A 189  ASP A 191
SITE     2 AC2 29 GLU A 192  HIS A 281  ARG A 282  HIS A 314
SITE     3 AC2 29 LYS A 322  LEU A 323  SER A 367  GLY A 368
SITE     4 AC2 29 GLY A 369  GLN A 389  GLY A 391  GLY A 392
SITE     5 AC2 29  MG A 445  HOH A 508  HOH A 523  HOH A 528
SITE     6 AC2 29 HOH A 529  HOH A 535  HOH A 554  HOH A 584
SITE     7 AC2 29 HOH A 625  GLU C  49  THR C  54  TRP C  55
SITE     8 AC2 29 ASN C 111
SITE     1 AC3  7 ASN B 111  LYS B 163  LYS B 165  KCX B 189
SITE     2 AC3  7 ASP B 191  GLU B 192  CAP B 446
SITE     1 AC4 27 GLU B  49  TRP B  55  ASN B 111  LYS B 163
SITE     2 AC4 27 LYS B 165  KCX B 189  ASP B 191  GLU B 192
SITE     3 AC4 27 HIS B 281  ARG B 282  HIS B 314  LYS B 322
SITE     4 AC4 27 LEU B 323  SER B 367  GLY B 368  GLY B 369
SITE     5 AC4 27 GLN B 389  GLY B 391  GLY B 392   MG B 445
SITE     6 AC4 27 HOH B 510  HOH B 516  HOH B 520  HOH B 534
SITE     7 AC4 27 HOH B 554  HOH B 555  HOH B 667
SITE     1 AC5  5 LYS C 163  KCX C 189  ASP C 191  GLU C 192
SITE     2 AC5  5 CAP C 446
SITE     1 AC6 25 GLU A  49  TRP A  55  ASN A 111  LYS C 163
SITE     2 AC6 25 LYS C 165  KCX C 189  GLU C 192  HIS C 281
SITE     3 AC6 25 ARG C 282  HIS C 314  LYS C 322  LEU C 323
SITE     4 AC6 25 SER C 367  GLY C 368  GLY C 369  GLN C 389
SITE     5 AC6 25 GLY C 391  GLY C 392   MG C 445  HOH C 518
SITE     6 AC6 25 HOH C 522  HOH C 536  HOH C 553  HOH C 586
SITE     7 AC6 25 HOH C 661
SITE     1 AC7  4 KCX D 189  ASP D 191  GLU D 192  CAP D 446
SITE     1 AC8 26 LYS D 163  LYS D 165  KCX D 189  ASP D 191
SITE     2 AC8 26 GLU D 192  HIS D 281  ARG D 282  HIS D 314
SITE     3 AC8 26 LYS D 322  SER D 367  GLY D 368  GLY D 369
SITE     4 AC8 26 GLN D 389  GLY D 391  GLY D 392   MG D 445
SITE     5 AC8 26 HOH D 504  HOH D 521  HOH D 532  HOH D 536
SITE     6 AC8 26 HOH D 601  HOH D 710  GLU E  49  THR E  54
SITE     7 AC8 26 TRP E  55  ASN E 111
SITE     1 AC9  5 KCX E 189  ASP E 191  GLU E 192  CAP E 446
SITE     2 AC9  5 HOH E 666
SITE     1 BC1 22 TRP D  55  ASN D 111  KCX E 189  GLU E 192
SITE     2 BC1 22 HIS E 281  ARG E 282  HIS E 314  SER E 367
SITE     3 BC1 22 GLY E 368  GLY E 369  GLN E 389  LEU E 390
SITE     4 BC1 22 GLY E 391  GLY E 392   CA E 445  HOH E 528
SITE     5 BC1 22 HOH E 535  HOH E 556  HOH E 577  HOH E 627
SITE     6 BC1 22 HOH E 666  HOH E 687
SITE     1 BC2  4 KCX F 189  ASP F 191  GLU F 192  CAP F 446
SITE     1 BC3 28 LYS F 163  LYS F 165  KCX F 189  ASP F 191
SITE     2 BC3 28 GLU F 192  HIS F 281  ARG F 282  HIS F 314
SITE     3 BC3 28 LYS F 322  LEU F 323  SER F 367  GLY F 368
SITE     4 BC3 28 GLY F 369  GLN F 389  GLY F 391  GLY F 392
SITE     5 BC3 28  MG F 445  HOH F 520  HOH F 524  HOH F 528
SITE     6 BC3 28 HOH F 541  HOH F 562  HOH F 570  HOH F 623
SITE     7 BC3 28 GLU H  49  THR H  54  TRP H  55  ASN H 111
SITE     1 BC4  6 LYS G 163  LYS G 165  KCX G 189  ASP G 191
SITE     2 BC4  6 GLU G 192  CAP G 446
SITE     1 BC5 27 GLU G  49  TRP G  55  ASN G 111  LYS G 163
SITE     2 BC5 27 LYS G 165  KCX G 189  ASP G 191  GLU G 192
SITE     3 BC5 27 HIS G 281  ARG G 282  HIS G 314  LYS G 322
SITE     4 BC5 27 LEU G 323  SER G 367  GLY G 368  GLY G 369
SITE     5 BC5 27 GLN G 389  GLY G 391  GLY G 392   MG G 445
SITE     6 BC5 27 HOH G 503  HOH G 528  HOH G 536  HOH G 582
SITE     7 BC5 27 HOH G 603  HOH G 669  HOH G 672
SITE     1 BC6  5 LYS H 165  KCX H 189  ASP H 191  GLU H 192
SITE     2 BC6  5 CAP H 446
SITE     1 BC7 23 TRP F  55  ASN F 111  HOH F 519  LYS H 163
SITE     2 BC7 23 LYS H 165  KCX H 189  GLU H 192  HIS H 281
SITE     3 BC7 23 ARG H 282  HIS H 314  LYS H 322  LEU H 323
SITE     4 BC7 23 SER H 367  GLY H 368  GLY H 369  GLN H 389
SITE     5 BC7 23 GLY H 391  GLY H 392   MG H 445  HOH H 535
SITE     6 BC7 23 HOH H 543  HOH H 607  HOH H 652
SITE     1 BC8  5 LYS I 163  KCX I 189  ASP I 191  GLU I 192
SITE     2 BC8  5 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 536  HOH I 537  HOH I 543
SITE     6 BC9 28 HOH I 547  HOH I 575  HOH I 659  HOH I 673
SITE     7 BC9 28 GLU J  49  THR J  54  TRP J  55  ASN J 111
SITE     1 CC1  5 KCX J 189  ASP J 191  GLU J 192  CAP J 446
SITE     2 CC1  5 HOH J 678
SITE     1 CC2 22 TRP I  55  ASN I 111  KCX J 189  GLU J 192
SITE     2 CC2 22 HIS J 281  ARG J 282  HIS J 314  SER J 367
SITE     3 CC2 22 GLY J 368  GLY J 369  GLN J 389  LEU J 390
SITE     4 CC2 22 GLY J 391  GLY J 392   CA J 445  HOH J 526
SITE     5 CC2 22 HOH J 538  HOH J 547  HOH J 549  HOH J 586
SITE     6 CC2 22 HOH J 604  HOH J 678
CRYST1  173.678  247.090  144.940  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      0.005758  0.000000  0.000000        0.00000
SCALE2      0.000000  0.004047  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006899        0.00000
      
PROCHECK
Go to PROCHECK summary
 References