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PDBsum entry 1ir1

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
1ir1
Jmol
Contents
Protein chains
464 a.a.
123 a.a.
Ligands
CAP ×4
Metals
_MG ×4
Waters ×2272
HEADER    LYASE                                   31-AUG-01   1IR1
TITLE     CRYSTAL STRUCTURE OF SPINACH RIBULOSE-1,5-BISPHOSPHATE
TITLE    2 CARBOXYLASE/OXYGENASE (RUBISCO) COMPLEXED WITH CO2, MG2+ AND 2-
TITLE    3 CARBOXYARABINITOL-1,5-BISPHOSPHATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: LARGE SUBUNIT OF RUBISCO;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 SYNONYM: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN;
COMPND   5 EC: 4.1.1.39;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: SMALL SUBUNIT OF RUBISCO;
COMPND   8 CHAIN: S, T, U, V;
COMPND   9 SYNONYM: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 2;
COMPND  10 EC: 4.1.1.39
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SPINACIA OLERACEA;
SOURCE   3 ORGANISM_COMMON: SPINACH;
SOURCE   4 ORGANISM_TAXID: 3562;
SOURCE   5 ORGAN: LEAVES;
SOURCE   6 MOL_ID: 2;
SOURCE   7 ORGANISM_SCIENTIFIC: SPINACIA OLERACEA;
SOURCE   8 ORGANISM_COMMON: SPINACH;
SOURCE   9 ORGANISM_TAXID: 3562;
SOURCE  10 ORGAN: LEAVES
KEYWDS    ALPHA/BETA BARREL, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    E.MIZOHATA,H.MATSUMURA,Y.OKANO,M.KUMEI,H.TAKUMA,J.ONODERA,K.KATO,
AUTHOR   2 N.SHIBATA,T.INOUE,A.YOKOTA,Y.KAI
REVDAT   4   13-JUL-11 1IR1    1       VERSN
REVDAT   3   24-FEB-09 1IR1    1       VERSN
REVDAT   2   14-JAN-03 1IR1    1       REMARK
REVDAT   1   13-MAR-02 1IR1    0
SPRSDE     13-MAR-02 1IR1      1BUR
JRNL        AUTH   E.MIZOHATA,H.MATSUMURA,Y.OKANO,M.KUMEI,H.TAKUMA,J.ONODERA,
JRNL        AUTH 2 K.KATO,N.SHIBATA,T.INOUE,A.YOKOTA,Y.KAI
JRNL        TITL   CRYSTAL STRUCTURE OF ACTIVATED RIBULOSE-1,5-BISPHOSPHATE
JRNL        TITL 2 CARBOXYLASE/OXYGENASE FROM GREEN ALGA CHLAMYDOMONAS
JRNL        TITL 3 REINHARDTII COMPLEXED WITH
JRNL        TITL 4 2-CARBOXYARABINITOL-1,5-BISPHOSPHATE.
JRNL        REF    J.MOL.BIOL.                   V. 316   679 2002
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   11866526
JRNL        DOI    10.1006/JMBI.2001.5381
REMARK   2
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.0
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 76.9
REMARK   3   NUMBER OF REFLECTIONS             : 175568
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 SET) : 0.155
REMARK   3   FREE R VALUE                     : 0.179
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 8801
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.86
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 47.50
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2820
REMARK   3   BIN FREE R VALUE                    : 0.3040
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 573
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.013
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 18696
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 88
REMARK   3   SOLVENT ATOMS            : 2272
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.18
REMARK   3   ESD FROM SIGMAA              (A) : 0.24
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.20
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.28
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.005
REMARK   3   BOND ANGLES            (DEGREES) : 1.36
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1IR1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-SEP-01.
REMARK 100 THE RCSB ID CODE IS RCSB005201.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 298
REMARK 200  PH                             : 7.9
REMARK 200  NUMBER OF CRYSTALS USED        : 2
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY
REMARK 200  BEAMLINE                       : BL-6A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : WEISSENBERG
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 175568
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 76.9
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86
REMARK 200  COMPLETENESS FOR SHELL     (%) : 47.5
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: RE-REFINEMENT OF 1BUR
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ID 1BUR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 46.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, MGCL2, NAHCO3, DTT, 2-
REMARK 280  CARBOXYARABINITOL-1,5-BISPHOSPHATE, BICINE, PH 7.9, VAPOR
REMARK 280  DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   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      100.45000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      100.45000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       78.90000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       78.90000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       78.90000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       78.90000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      100.45000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       78.90000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       78.90000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      100.45000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       78.90000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       78.90000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HEXADECAMER COMPRISED OF 8
REMARK 300 LARGE AND 8 SMALL SUBUNITS. A HALF OF THE HEXADECAMER (4 LARGE AND
REMARK 300 4 SMALL SUBUNITS) EXISTS IN THE ASYMMETRIC UNIT. THE REST PART IS
REMARK 300 GENERATED BY -X, Y, -Z+1/2.
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: HEXADECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 110760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 120160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -503.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, S, B, T, C, U, D, V
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      100.45000
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 B 534  LIES ON A SPECIAL POSITION.
REMARK 375      HOH B 714  LIES ON A SPECIAL POSITION.
REMARK 375      HOH B 716  LIES ON A SPECIAL POSITION.
REMARK 375      HOH B 765  LIES ON A SPECIAL POSITION.
REMARK 375      HOH D 518  LIES ON A SPECIAL POSITION.
REMARK 375      HOH D 521  LIES ON A SPECIAL POSITION.
REMARK 375      HOH D 524  LIES ON A SPECIAL POSITION.
REMARK 375      HOH D 716  LIES ON A SPECIAL POSITION.
REMARK 375      HOH D 841  LIES ON A SPECIAL POSITION.
REMARK 375      HOH D 798  LIES ON A SPECIAL POSITION.
REMARK 375      HOH D 800  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     SER A     2
REMARK 465     PRO A     3
REMARK 465     GLN A     4
REMARK 465     THR A     5
REMARK 465     GLU A     6
REMARK 465     THR A     7
REMARK 465     LYS A     8
REMARK 465     ALA A     9
REMARK 465     SER A    10
REMARK 465     VAL A    11
REMARK 465     MET B     1
REMARK 465     SER B     2
REMARK 465     PRO B     3
REMARK 465     GLN B     4
REMARK 465     THR B     5
REMARK 465     GLU B     6
REMARK 465     THR B     7
REMARK 465     LYS B     8
REMARK 465     ALA B     9
REMARK 465     SER B    10
REMARK 465     VAL B    11
REMARK 465     MET C     1
REMARK 465     SER C     2
REMARK 465     PRO C     3
REMARK 465     GLN C     4
REMARK 465     THR C     5
REMARK 465     GLU C     6
REMARK 465     THR C     7
REMARK 465     LYS C     8
REMARK 465     ALA C     9
REMARK 465     SER C    10
REMARK 465     VAL C    11
REMARK 465     MET D     1
REMARK 465     SER D     2
REMARK 465     PRO D     3
REMARK 465     GLN D     4
REMARK 465     THR D     5
REMARK 465     GLU D     6
REMARK 465     THR D     7
REMARK 465     LYS D     8
REMARK 465     ALA D     9
REMARK 465     SER D    10
REMARK 465     VAL D    11
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    HOH C   828     O    HOH C   913              2.12
REMARK 500   OG1  THR V    46     O    HOH V   269              2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    HOH B   840     O    HOH B   840     4565     1.89
REMARK 500   O    HOH A   841     O    HOH C   914     8455     2.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    SER A  62      -76.51   -140.88
REMARK 500    HIS A 153      -58.85   -134.01
REMARK 500    ASN A 207      -89.74   -119.44
REMARK 500    MET A 212      109.45   -167.73
REMARK 500    MET A 297       -0.14     82.72
REMARK 500    VAL A 331      -49.95     77.04
REMARK 500    ASN S   8       54.69     36.94
REMARK 500    GLU S  13     -146.48     65.72
REMARK 500    LEU S  15       -4.31     84.56
REMARK 500    LYS S  71     -122.71     57.09
REMARK 500    SER S 114      113.75   -166.94
REMARK 500    SER B  62      -75.47   -139.13
REMARK 500    HIS B 153      -57.59   -134.35
REMARK 500    ASN B 207      -88.31   -121.09
REMARK 500    MET B 212      110.61   -166.12
REMARK 500    ARG B 295       32.08    -96.89
REMARK 500    MET B 297      -12.02     87.69
REMARK 500    VAL B 331      -51.45     75.62
REMARK 500    VAL B 369       57.06     35.87
REMARK 500    GLU T  13     -153.06     65.17
REMARK 500    THR T  14      120.58    -39.72
REMARK 500    LEU T  15       -8.98     85.97
REMARK 500    LYS T  71     -122.84     59.10
REMARK 500    PRO T 120     -174.11    -67.44
REMARK 500    SER C  62      -74.58   -139.83
REMARK 500    HIS C 153      -56.39   -133.92
REMARK 500    CYS C 172      130.06   -171.50
REMARK 500    ASN C 207      -89.04   -120.70
REMARK 500    MET C 212      110.18   -166.82
REMARK 500    ARG C 295       31.70    -93.16
REMARK 500    VAL C 331      -53.28     77.45
REMARK 500    VAL C 369       57.41     34.52
REMARK 500    GLU U  13     -149.21     66.14
REMARK 500    LEU U  15       -4.70     87.33
REMARK 500    LYS U  71     -122.46     57.18
REMARK 500    SER U 114      112.89   -169.34
REMARK 500    SER D  62      -74.19   -143.15
REMARK 500    HIS D 153      -56.16   -132.13
REMARK 500    CYS D 172      128.80   -170.80
REMARK 500    ASN D 207      -88.16   -119.45
REMARK 500    MET D 212      110.72   -162.28
REMARK 500    ARG D 295       32.11    -94.03
REMARK 500    VAL D 331      -52.56     80.59
REMARK 500    ASP D 357       92.13   -160.73
REMARK 500    VAL D 369       56.67     35.50
REMARK 500    GLU V  13     -145.76     66.99
REMARK 500    LEU V  15       -7.83     83.84
REMARK 500    LYS V  71     -126.85     58.79
REMARK 500    SER V 114      116.26   -172.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 776        DISTANCE =  5.28 ANGSTROMS
REMARK 525    HOH A 779        DISTANCE =  7.30 ANGSTROMS
REMARK 525    HOH A 803        DISTANCE =  5.76 ANGSTROMS
REMARK 525    HOH A 817        DISTANCE =  7.56 ANGSTROMS
REMARK 525    HOH A 843        DISTANCE =  5.84 ANGSTROMS
REMARK 525    HOH A 859        DISTANCE =  5.57 ANGSTROMS
REMARK 525    HOH A 863        DISTANCE =  7.81 ANGSTROMS
REMARK 525    HOH A 867        DISTANCE =  6.37 ANGSTROMS
REMARK 525    HOH A 870        DISTANCE =  5.05 ANGSTROMS
REMARK 525    HOH A 871        DISTANCE =  6.06 ANGSTROMS
REMARK 525    HOH A 905        DISTANCE =  5.45 ANGSTROMS
REMARK 525    HOH A 915        DISTANCE =  6.56 ANGSTROMS
REMARK 525    HOH A 919        DISTANCE =  5.94 ANGSTROMS
REMARK 525    HOH A 920        DISTANCE =  5.24 ANGSTROMS
REMARK 525    HOH B 744        DISTANCE =  5.21 ANGSTROMS
REMARK 525    HOH B 775        DISTANCE =  5.50 ANGSTROMS
REMARK 525    HOH B 821        DISTANCE =  5.75 ANGSTROMS
REMARK 525    HOH B 822        DISTANCE =  5.20 ANGSTROMS
REMARK 525    HOH B 823        DISTANCE =  5.34 ANGSTROMS
REMARK 525    HOH B 827        DISTANCE =  6.85 ANGSTROMS
REMARK 525    HOH B 833        DISTANCE =  5.79 ANGSTROMS
REMARK 525    HOH B 834        DISTANCE =  5.17 ANGSTROMS
REMARK 525    HOH B 848        DISTANCE =  5.30 ANGSTROMS
REMARK 525    HOH B 853        DISTANCE =  9.27 ANGSTROMS
REMARK 525    HOH B 857        DISTANCE =  5.30 ANGSTROMS
REMARK 525    HOH B 872        DISTANCE =  7.52 ANGSTROMS
REMARK 525    HOH B 891        DISTANCE =  5.16 ANGSTROMS
REMARK 525    HOH C 757        DISTANCE =  5.43 ANGSTROMS
REMARK 525    HOH C 759        DISTANCE =  6.21 ANGSTROMS
REMARK 525    HOH C 771        DISTANCE =  8.61 ANGSTROMS
REMARK 525    HOH C 782        DISTANCE =  7.08 ANGSTROMS
REMARK 525    HOH C 804        DISTANCE =  6.86 ANGSTROMS
REMARK 525    HOH C 806        DISTANCE =  5.04 ANGSTROMS
REMARK 525    HOH C 823        DISTANCE =  5.16 ANGSTROMS
REMARK 525    HOH C 841        DISTANCE =  5.23 ANGSTROMS
REMARK 525    HOH C 856        DISTANCE =  8.31 ANGSTROMS
REMARK 525    HOH C 865        DISTANCE =  8.03 ANGSTROMS
REMARK 525    HOH C 877        DISTANCE = 10.13 ANGSTROMS
REMARK 525    HOH C 883        DISTANCE =  7.03 ANGSTROMS
REMARK 525    HOH C 887        DISTANCE =  7.19 ANGSTROMS
REMARK 525    HOH C 889        DISTANCE =  6.74 ANGSTROMS
REMARK 525    HOH C 903        DISTANCE =  5.60 ANGSTROMS
REMARK 525    HOH D 694        DISTANCE =  5.13 ANGSTROMS
REMARK 525    HOH D 771        DISTANCE =  6.29 ANGSTROMS
REMARK 525    HOH D 798        DISTANCE =  5.82 ANGSTROMS
REMARK 525    HOH D 830        DISTANCE =  5.26 ANGSTROMS
REMARK 525    HOH D 840        DISTANCE =  5.02 ANGSTROMS
REMARK 525    HOH D 841        DISTANCE =  7.87 ANGSTROMS
REMARK 525    HOH D 842        DISTANCE =  5.51 ANGSTROMS
REMARK 525    HOH D 845        DISTANCE =  7.44 ANGSTROMS
REMARK 525    HOH D 850        DISTANCE =  6.09 ANGSTROMS
REMARK 525    HOH D 852        DISTANCE =  6.51 ANGSTROMS
REMARK 525    HOH D 853        DISTANCE =  6.07 ANGSTROMS
REMARK 525    HOH D 857        DISTANCE =  6.56 ANGSTROMS
REMARK 525    HOH D 862        DISTANCE =  8.94 ANGSTROMS
REMARK 525    HOH D 867        DISTANCE =  6.11 ANGSTROMS
REMARK 525    HOH D 875        DISTANCE =  6.70 ANGSTROMS
REMARK 525    HOH S 224        DISTANCE =  5.24 ANGSTROMS
REMARK 525    HOH S 234        DISTANCE =  6.55 ANGSTROMS
REMARK 525    HOH S 252        DISTANCE =  7.23 ANGSTROMS
REMARK 525    HOH S 264        DISTANCE =  8.41 ANGSTROMS
REMARK 525    HOH S 288        DISTANCE =  6.56 ANGSTROMS
REMARK 525    HOH S 292        DISTANCE =  5.33 ANGSTROMS
REMARK 525    HOH T 202        DISTANCE =  5.82 ANGSTROMS
REMARK 525    HOH T 224        DISTANCE =  5.56 ANGSTROMS
REMARK 525    HOH T 233        DISTANCE =  5.89 ANGSTROMS
REMARK 525    HOH T 240        DISTANCE =  7.81 ANGSTROMS
REMARK 525    HOH T 241        DISTANCE =  5.33 ANGSTROMS
REMARK 525    HOH T 262        DISTANCE =  5.90 ANGSTROMS
REMARK 525    HOH T 263        DISTANCE =  8.10 ANGSTROMS
REMARK 525    HOH T 265        DISTANCE =  5.40 ANGSTROMS
REMARK 525    HOH U 194        DISTANCE =  5.79 ANGSTROMS
REMARK 525    HOH U 196        DISTANCE =  7.21 ANGSTROMS
REMARK 525    HOH U 200        DISTANCE =  5.91 ANGSTROMS
REMARK 525    HOH U 217        DISTANCE =  5.11 ANGSTROMS
REMARK 525    HOH U 227        DISTANCE =  5.11 ANGSTROMS
REMARK 525    HOH U 233        DISTANCE =  6.32 ANGSTROMS
REMARK 525    HOH U 235        DISTANCE =  6.50 ANGSTROMS
REMARK 525    HOH U 237        DISTANCE =  5.22 ANGSTROMS
REMARK 525    HOH U 238        DISTANCE =  5.50 ANGSTROMS
REMARK 525    HOH U 239        DISTANCE =  5.74 ANGSTROMS
REMARK 525    HOH U 251        DISTANCE =  5.65 ANGSTROMS
REMARK 525    HOH U 253        DISTANCE =  5.61 ANGSTROMS
REMARK 525    HOH U 259        DISTANCE =  9.25 ANGSTROMS
REMARK 525    HOH U 269        DISTANCE =  7.05 ANGSTROMS
REMARK 525    HOH V 203        DISTANCE =  5.19 ANGSTROMS
REMARK 525    HOH V 221        DISTANCE =  5.39 ANGSTROMS
REMARK 525    HOH V 233        DISTANCE =  7.59 ANGSTROMS
REMARK 525    HOH V 260        DISTANCE =  9.28 ANGSTROMS
REMARK 525    HOH V 267        DISTANCE =  5.57 ANGSTROMS
REMARK 525    HOH V 270        DISTANCE =  7.33 ANGSTROMS
REMARK 525    HOH V 274        DISTANCE =  5.41 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX A 201   OQ2
REMARK 620 2 ASP A 203   OD1  87.4
REMARK 620 3 GLU A 204   OE1  99.7  88.8
REMARK 620 4 CAP A 501   O6  164.2  93.4  96.2
REMARK 620 5 CAP A 501   O3   91.6 179.0  91.3  87.6
REMARK 620 6 CAP A 501   O2   90.2 103.5 164.6  74.2  76.6
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG B 476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX B 201   OQ2
REMARK 620 2 ASP B 203   OD1  88.2
REMARK 620 3 GLU B 204   OE1  91.9  94.1
REMARK 620 4 CAP B 501   O6  166.8  97.9  99.3
REMARK 620 5 CAP B 501   O3   86.0 174.0  87.5  87.5
REMARK 620 6 CAP B 501   O2   91.1 103.1 162.7  76.2  75.6
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG C 476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX C 201   OQ2
REMARK 620 2 ASP C 203   OD1  88.1
REMARK 620 3 GLU C 204   OE1  91.6  90.3
REMARK 620 4 CAP C 501   O2   93.7 105.1 163.8
REMARK 620 5 CAP C 501   O6  168.4  94.8  99.6  74.7
REMARK 620 6 CAP C 501   O3   89.4 177.0  88.1  76.8  88.0
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG D 476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX D 201   OQ2
REMARK 620 2 ASP D 203   OD1  88.0
REMARK 620 3 GLU D 204   OE1  90.1  90.1
REMARK 620 4 CAP D 501   O3   87.3 175.0  88.2
REMARK 620 5 CAP D 501   O6  168.7  94.5 100.9  90.4
REMARK 620 6 CAP D 501   O2   93.3 104.9 164.8  77.1  75.4
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 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP D 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IR2   RELATED DB: PDB
REMARK 900 1IR2 CONTAINS CRYSTAL STRUCTURE OF SAME PROTEIN FROM
REMARK 900 CHLAMYDOMONAS REINHARDTII COMPLEXED WITH 2-CABP
DBREF  1IR1 A    1   475  UNP    P00875   RBL_SPIOL        1    475
DBREF  1IR1 B    1   475  UNP    P00875   RBL_SPIOL        1    475
DBREF  1IR1 C    1   475  UNP    P00875   RBL_SPIOL        1    475
DBREF  1IR1 D    1   475  UNP    P00875   RBL_SPIOL        1    475
DBREF  1IR1 S    1   123  UNP    Q43832   RBS2_SPIOL      58    180
DBREF  1IR1 T    1   123  UNP    Q43832   RBS2_SPIOL      58    180
DBREF  1IR1 U    1   123  UNP    Q43832   RBS2_SPIOL      58    180
DBREF  1IR1 V    1   123  UNP    Q43832   RBS2_SPIOL      58    180
SEQADV 1IR1 KCX A  201  UNP  P00875    LYS   201 MODIFIED RESIDUE
SEQADV 1IR1 KCX B  201  UNP  P00875    LYS   201 MODIFIED RESIDUE
SEQADV 1IR1 KCX C  201  UNP  P00875    LYS   201 MODIFIED RESIDUE
SEQADV 1IR1 KCX D  201  UNP  P00875    LYS   201 MODIFIED RESIDUE
SEQADV 1IR1 MME S    1  UNP  Q43832    MET    58 MODIFIED RESIDUE
SEQADV 1IR1 MME T    1  UNP  Q43832    MET    58 MODIFIED RESIDUE
SEQADV 1IR1 MME U    1  UNP  Q43832    MET    58 MODIFIED RESIDUE
SEQADV 1IR1 MME V    1  UNP  Q43832    MET    58 MODIFIED RESIDUE
SEQRES   1 A  475  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLU PHE
SEQRES   2 A  475  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR
SEQRES   3 A  475  PRO GLU TYR GLU THR LEU ASP THR ASP ILE LEU ALA ALA
SEQRES   4 A  475  PHE ARG VAL SER PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 A  475  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 A  475  TRP THR THR VAL TRP THR ASP GLY LEU THR ASN LEU ASP
SEQRES   7 A  475  ARG TYR LYS GLY ARG CYS TYR HIS ILE GLU PRO VAL ALA
SEQRES   8 A  475  GLY GLU GLU ASN GLN TYR ILE CYS TYR VAL ALA TYR PRO
SEQRES   9 A  475  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 A  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 A  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO VAL ALA
SEQRES  12 A  475  TYR VAL LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 A  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU
SEQRES  14 A  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 A  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 A  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 A  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE CYS
SEQRES  18 A  475  ALA GLU ALA LEU TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 A  475  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 A  475  GLU ASP MET MET LYS ARG ALA VAL PHE ALA ARG GLU LEU
SEQRES  21 A  475  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 A  475  PHE THR ALA ASN THR THR LEU SER HIS TYR CYS ARG ASP
SEQRES  23 A  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 A  475  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG
SEQRES  25 A  475  VAL LEU ALA LYS ALA LEU ARG LEU SER GLY GLY ASP HIS
SEQRES  26 A  475  ILE HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 A  475  ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG ASP
SEQRES  28 A  475  ASP TYR THR GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 A  475  THR GLN SER TRP VAL SER THR PRO GLY VAL LEU PRO VAL
SEQRES  30 A  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 A  475  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY
SEQRES  32 A  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 A  475  ALA VAL ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN
SEQRES  34 A  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN
SEQRES  35 A  475  THR ILE ILE ARG GLU ALA THR LYS TRP SER PRO GLU LEU
SEQRES  36 A  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 A  475  PHE PRO ALA MET ASP THR VAL
SEQRES   1 S  123  MME LYS VAL TRP PRO THR GLN ASN MET LYS ARG TYR GLU
SEQRES   2 S  123  THR LEU SER TYR LEU PRO PRO LEU THR THR ASP GLN LEU
SEQRES   3 S  123  ALA ARG GLN VAL ASP TYR LEU LEU ASN ASN LYS TRP VAL
SEQRES   4 S  123  PRO CYS LEU GLU PHE GLU THR ASP HIS GLY PHE VAL TYR
SEQRES   5 S  123  ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG
SEQRES   6 S  123  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR
SEQRES   7 S  123  ASP PRO ALA GLN VAL LEU ASN GLU LEU GLU GLU CYS LYS
SEQRES   8 S  123  LYS GLU TYR PRO ASN ALA PHE ILE ARG ILE ILE GLY PHE
SEQRES   9 S  123  ASP SER ASN ARG GLN VAL GLN CYS VAL SER PHE ILE ALA
SEQRES  10 S  123  TYR LYS PRO ALA GLY TYR
SEQRES   1 B  475  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLU PHE
SEQRES   2 B  475  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR
SEQRES   3 B  475  PRO GLU TYR GLU THR LEU ASP THR ASP ILE LEU ALA ALA
SEQRES   4 B  475  PHE ARG VAL SER PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 B  475  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 B  475  TRP THR THR VAL TRP THR ASP GLY LEU THR ASN LEU ASP
SEQRES   7 B  475  ARG TYR LYS GLY ARG CYS TYR HIS ILE GLU PRO VAL ALA
SEQRES   8 B  475  GLY GLU GLU ASN GLN TYR ILE CYS TYR VAL ALA TYR PRO
SEQRES   9 B  475  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 B  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 B  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO VAL ALA
SEQRES  12 B  475  TYR VAL LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 B  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU
SEQRES  14 B  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 B  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 B  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 B  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE CYS
SEQRES  18 B  475  ALA GLU ALA LEU TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 B  475  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 B  475  GLU ASP MET MET LYS ARG ALA VAL PHE ALA ARG GLU LEU
SEQRES  21 B  475  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 B  475  PHE THR ALA ASN THR THR LEU SER HIS TYR CYS ARG ASP
SEQRES  23 B  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 B  475  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG
SEQRES  25 B  475  VAL LEU ALA LYS ALA LEU ARG LEU SER GLY GLY ASP HIS
SEQRES  26 B  475  ILE HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 B  475  ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG ASP
SEQRES  28 B  475  ASP TYR THR GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 B  475  THR GLN SER TRP VAL SER THR PRO GLY VAL LEU PRO VAL
SEQRES  30 B  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 B  475  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY
SEQRES  32 B  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 B  475  ALA VAL ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN
SEQRES  34 B  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN
SEQRES  35 B  475  THR ILE ILE ARG GLU ALA THR LYS TRP SER PRO GLU LEU
SEQRES  36 B  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 B  475  PHE PRO ALA MET ASP THR VAL
SEQRES   1 T  123  MME LYS VAL TRP PRO THR GLN ASN MET LYS ARG TYR GLU
SEQRES   2 T  123  THR LEU SER TYR LEU PRO PRO LEU THR THR ASP GLN LEU
SEQRES   3 T  123  ALA ARG GLN VAL ASP TYR LEU LEU ASN ASN LYS TRP VAL
SEQRES   4 T  123  PRO CYS LEU GLU PHE GLU THR ASP HIS GLY PHE VAL TYR
SEQRES   5 T  123  ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG
SEQRES   6 T  123  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR
SEQRES   7 T  123  ASP PRO ALA GLN VAL LEU ASN GLU LEU GLU GLU CYS LYS
SEQRES   8 T  123  LYS GLU TYR PRO ASN ALA PHE ILE ARG ILE ILE GLY PHE
SEQRES   9 T  123  ASP SER ASN ARG GLN VAL GLN CYS VAL SER PHE ILE ALA
SEQRES  10 T  123  TYR LYS PRO ALA GLY TYR
SEQRES   1 C  475  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLU PHE
SEQRES   2 C  475  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR
SEQRES   3 C  475  PRO GLU TYR GLU THR LEU ASP THR ASP ILE LEU ALA ALA
SEQRES   4 C  475  PHE ARG VAL SER PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 C  475  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 C  475  TRP THR THR VAL TRP THR ASP GLY LEU THR ASN LEU ASP
SEQRES   7 C  475  ARG TYR LYS GLY ARG CYS TYR HIS ILE GLU PRO VAL ALA
SEQRES   8 C  475  GLY GLU GLU ASN GLN TYR ILE CYS TYR VAL ALA TYR PRO
SEQRES   9 C  475  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 C  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 C  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO VAL ALA
SEQRES  12 C  475  TYR VAL LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 C  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU
SEQRES  14 C  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 C  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 C  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 C  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE CYS
SEQRES  18 C  475  ALA GLU ALA LEU TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 C  475  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 C  475  GLU ASP MET MET LYS ARG ALA VAL PHE ALA ARG GLU LEU
SEQRES  21 C  475  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 C  475  PHE THR ALA ASN THR THR LEU SER HIS TYR CYS ARG ASP
SEQRES  23 C  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 C  475  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG
SEQRES  25 C  475  VAL LEU ALA LYS ALA LEU ARG LEU SER GLY GLY ASP HIS
SEQRES  26 C  475  ILE HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 C  475  ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG ASP
SEQRES  28 C  475  ASP TYR THR GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 C  475  THR GLN SER TRP VAL SER THR PRO GLY VAL LEU PRO VAL
SEQRES  30 C  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 C  475  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY
SEQRES  32 C  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 C  475  ALA VAL ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN
SEQRES  34 C  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN
SEQRES  35 C  475  THR ILE ILE ARG GLU ALA THR LYS TRP SER PRO GLU LEU
SEQRES  36 C  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 C  475  PHE PRO ALA MET ASP THR VAL
SEQRES   1 U  123  MME LYS VAL TRP PRO THR GLN ASN MET LYS ARG TYR GLU
SEQRES   2 U  123  THR LEU SER TYR LEU PRO PRO LEU THR THR ASP GLN LEU
SEQRES   3 U  123  ALA ARG GLN VAL ASP TYR LEU LEU ASN ASN LYS TRP VAL
SEQRES   4 U  123  PRO CYS LEU GLU PHE GLU THR ASP HIS GLY PHE VAL TYR
SEQRES   5 U  123  ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG
SEQRES   6 U  123  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR
SEQRES   7 U  123  ASP PRO ALA GLN VAL LEU ASN GLU LEU GLU GLU CYS LYS
SEQRES   8 U  123  LYS GLU TYR PRO ASN ALA PHE ILE ARG ILE ILE GLY PHE
SEQRES   9 U  123  ASP SER ASN ARG GLN VAL GLN CYS VAL SER PHE ILE ALA
SEQRES  10 U  123  TYR LYS PRO ALA GLY TYR
SEQRES   1 D  475  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLU PHE
SEQRES   2 D  475  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR
SEQRES   3 D  475  PRO GLU TYR GLU THR LEU ASP THR ASP ILE LEU ALA ALA
SEQRES   4 D  475  PHE ARG VAL SER PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 D  475  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 D  475  TRP THR THR VAL TRP THR ASP GLY LEU THR ASN LEU ASP
SEQRES   7 D  475  ARG TYR LYS GLY ARG CYS TYR HIS ILE GLU PRO VAL ALA
SEQRES   8 D  475  GLY GLU GLU ASN GLN TYR ILE CYS TYR VAL ALA TYR PRO
SEQRES   9 D  475  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 D  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 D  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO VAL ALA
SEQRES  12 D  475  TYR VAL LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 D  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU
SEQRES  14 D  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 D  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 D  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 D  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE CYS
SEQRES  18 D  475  ALA GLU ALA LEU TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 D  475  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 D  475  GLU ASP MET MET LYS ARG ALA VAL PHE ALA ARG GLU LEU
SEQRES  21 D  475  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 D  475  PHE THR ALA ASN THR THR LEU SER HIS TYR CYS ARG ASP
SEQRES  23 D  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 D  475  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG
SEQRES  25 D  475  VAL LEU ALA LYS ALA LEU ARG LEU SER GLY GLY ASP HIS
SEQRES  26 D  475  ILE HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 D  475  ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG ASP
SEQRES  28 D  475  ASP TYR THR GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 D  475  THR GLN SER TRP VAL SER THR PRO GLY VAL LEU PRO VAL
SEQRES  30 D  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 D  475  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY
SEQRES  32 D  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 D  475  ALA VAL ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN
SEQRES  34 D  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN
SEQRES  35 D  475  THR ILE ILE ARG GLU ALA THR LYS TRP SER PRO GLU LEU
SEQRES  36 D  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 D  475  PHE PRO ALA MET ASP THR VAL
SEQRES   1 V  123  MME LYS VAL TRP PRO THR GLN ASN MET LYS ARG TYR GLU
SEQRES   2 V  123  THR LEU SER TYR LEU PRO PRO LEU THR THR ASP GLN LEU
SEQRES   3 V  123  ALA ARG GLN VAL ASP TYR LEU LEU ASN ASN LYS TRP VAL
SEQRES   4 V  123  PRO CYS LEU GLU PHE GLU THR ASP HIS GLY PHE VAL TYR
SEQRES   5 V  123  ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG
SEQRES   6 V  123  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR
SEQRES   7 V  123  ASP PRO ALA GLN VAL LEU ASN GLU LEU GLU GLU CYS LYS
SEQRES   8 V  123  LYS GLU TYR PRO ASN ALA PHE ILE ARG ILE ILE GLY PHE
SEQRES   9 V  123  ASP SER ASN ARG GLN VAL GLN CYS VAL SER PHE ILE ALA
SEQRES  10 V  123  TYR LYS PRO ALA GLY TYR
MODRES 1IR1 KCX A  201  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 1IR1 MME S    1  MET  N-METHYL METHIONINE
MODRES 1IR1 KCX B  201  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 1IR1 MME T    1  MET  N-METHYL METHIONINE
MODRES 1IR1 KCX C  201  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 1IR1 MME U    1  MET  N-METHYL METHIONINE
MODRES 1IR1 KCX D  201  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 1IR1 MME V    1  MET  N-METHYL METHIONINE
HET    KCX  A 201      12
HET    MME  S   1       9
HET    KCX  B 201      12
HET    MME  T   1       9
HET    KCX  C 201      12
HET    MME  U   1       9
HET    KCX  D 201      12
HET    MME  V   1       9
HET     MG  A 476       1
HET     MG  B 476       1
HET     MG  C 476       1
HET     MG  D 476       1
HET    CAP  A 501      21
HET    CAP  B 501      21
HET    CAP  C 501      21
HET    CAP  D 501      21
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID
HETNAM     MME N-METHYL METHIONINE
HETNAM      MG MAGNESIUM ION
HETNAM     CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE
FORMUL   1  KCX    4(C7 H14 N2 O4)
FORMUL   2  MME    4(C6 H13 N O2 S)
FORMUL   9   MG    4(MG 2+)
FORMUL  13  CAP    4(C6 H14 O13 P2)
FORMUL  17  HOH   *2272(H2 O)
HELIX    1   1 TYR A   20  TYR A   25  1                                   6
HELIX    2   2 PRO A   49  GLU A   60  1                                  12
HELIX    3   3 VAL A   69  THR A   75  5                                   7
HELIX    4   4 ASN A   76  LYS A   81  1                                   6
HELIX    5   5 PRO A  104  PHE A  108  5                                   5
HELIX    6   6 SER A  112  VAL A  121  1                                  10
HELIX    7   7 ASN A  123  PHE A  127  5                                   5
HELIX    8   8 PRO A  141  LYS A  146  1                                   6
HELIX    9   9 GLY A  154  ASN A  163  1                                  10
HELIX   10  10 SER A  181  GLY A  195  1                                  15
HELIX   11  11 ARG A  213  GLY A  233  1                                  21
HELIX   12  12 THR A  246  GLY A  261  1                                  16
HELIX   13  13 TYR A  269  GLY A  273  1                                   5
HELIX   14  14 GLY A  273  GLY A  288  1                                  16
HELIX   15  15 MET A  297  ARG A  303  1                                   7
HELIX   16  16 HIS A  310  GLY A  322  1                                  13
HELIX   17  17 GLU A  338  ASP A  351  1                                  14
HELIX   18  18 ASP A  357  GLY A  361  5                                   5
HELIX   19  19 HIS A  383  TRP A  385  5                                   3
HELIX   20  20 HIS A  386  GLY A  395  1                                  10
HELIX   21  21 GLY A  403  GLY A  408  1                                   6
HELIX   22  22 GLY A  412  GLU A  433  1                                  22
HELIX   23  23 ASP A  436  LYS A  450  1                                  15
HELIX   24  24 SER A  452  LYS A  463  1                                  12
HELIX   25  25 THR S   22  ASN S   36  1                                  15
HELIX   26  26 ASP S   79  TYR S   94  1                                  16
HELIX   27  27 TYR B   20  TYR B   25  1                                   6
HELIX   28  28 PRO B   49  SER B   61  1                                  13
HELIX   29  29 VAL B   69  THR B   75  5                                   7
HELIX   30  30 ASN B   76  LYS B   81  1                                   6
HELIX   31  31 PRO B  104  PHE B  108  5                                   5
HELIX   32  32 SER B  112  VAL B  121  1                                  10
HELIX   33  33 ASN B  123  PHE B  127  5                                   5
HELIX   34  34 PRO B  141  LYS B  146  1                                   6
HELIX   35  35 GLY B  154  ASN B  163  1                                  10
HELIX   36  36 SER B  181  GLY B  195  1                                  15
HELIX   37  37 ARG B  213  GLY B  233  1                                  21
HELIX   38  38 THR B  246  GLY B  261  1                                  16
HELIX   39  39 TYR B  269  GLY B  273  1                                   5
HELIX   40  40 GLY B  273  GLY B  288  1                                  16
HELIX   41  41 MET B  297  ARG B  303  1                                   7
HELIX   42  42 HIS B  310  GLY B  322  1                                  13
HELIX   43  43 GLU B  338  ASP B  351  1                                  14
HELIX   44  44 ASP B  357  GLY B  361  5                                   5
HELIX   45  45 HIS B  383  TRP B  385  5                                   3
HELIX   46  46 HIS B  386  GLY B  395  1                                  10
HELIX   47  47 GLY B  403  GLY B  408  1                                   6
HELIX   48  48 GLY B  412  GLU B  433  1                                  22
HELIX   49  49 ASP B  436  LYS B  450  1                                  15
HELIX   50  50 SER B  452  LYS B  463  1                                  12
HELIX   51  51 THR T   22  ASN T   36  1                                  15
HELIX   52  52 ASP T   79  TYR T   94  1                                  16
HELIX   53  53 TYR C   20  TYR C   25  1                                   6
HELIX   54  54 PRO C   49  GLU C   60  1                                  12
HELIX   55  55 VAL C   69  THR C   75  5                                   7
HELIX   56  56 ASN C   76  LYS C   81  1                                   6
HELIX   57  57 PRO C  104  PHE C  108  5                                   5
HELIX   58  58 SER C  112  VAL C  121  1                                  10
HELIX   59  59 ASN C  123  PHE C  127  5                                   5
HELIX   60  60 PRO C  141  LYS C  146  1                                   6
HELIX   61  61 GLY C  154  ASN C  163  1                                  10
HELIX   62  62 SER C  181  GLY C  195  1                                  15
HELIX   63  63 ARG C  213  GLY C  233  1                                  21
HELIX   64  64 THR C  246  GLY C  261  1                                  16
HELIX   65  65 TYR C  269  GLY C  273  1                                   5
HELIX   66  66 GLY C  273  GLY C  288  1                                  16
HELIX   67  67 MET C  297  ARG C  303  1                                   7
HELIX   68  68 HIS C  310  GLY C  322  1                                  13
HELIX   69  69 GLU C  338  ASP C  351  1                                  14
HELIX   70  70 ASP C  357  GLY C  361  5                                   5
HELIX   71  71 HIS C  383  TRP C  385  5                                   3
HELIX   72  72 HIS C  386  GLY C  395  1                                  10
HELIX   73  73 GLY C  403  GLY C  408  1                                   6
HELIX   74  74 GLY C  412  GLU C  433  1                                  22
HELIX   75  75 ASP C  436  LYS C  450  1                                  15
HELIX   76  76 SER C  452  LYS C  463  1                                  12
HELIX   77  77 THR U   22  ASN U   36  1                                  15
HELIX   78  78 ASP U   79  TYR U   94  1                                  16
HELIX   79  79 TYR D   20  TYR D   25  1                                   6
HELIX   80  80 PRO D   49  GLU D   60  1                                  12
HELIX   81  81 VAL D   69  THR D   75  5                                   7
HELIX   82  82 ASN D   76  LYS D   81  1                                   6
HELIX   83  83 PRO D  104  PHE D  108  5                                   5
HELIX   84  84 SER D  112  VAL D  121  1                                  10
HELIX   85  85 ASN D  123  PHE D  127  5                                   5
HELIX   86  86 PRO D  141  LYS D  146  1                                   6
HELIX   87  87 GLY D  154  ASN D  163  1                                  10
HELIX   88  88 SER D  181  ARG D  194  1                                  14
HELIX   89  89 ARG D  213  GLY D  233  1                                  21
HELIX   90  90 THR D  246  GLY D  261  1                                  16
HELIX   91  91 TYR D  269  GLY D  273  1                                   5
HELIX   92  92 GLY D  273  GLY D  288  1                                  16
HELIX   93  93 MET D  297  ARG D  303  1                                   7
HELIX   94  94 HIS D  310  GLY D  322  1                                  13
HELIX   95  95 GLU D  338  ASP D  351  1                                  14
HELIX   96  96 ASP D  357  GLY D  361  5                                   5
HELIX   97  97 HIS D  383  TRP D  385  5                                   3
HELIX   98  98 HIS D  386  GLY D  395  1                                  10
HELIX   99  99 GLY D  403  GLY D  408  1                                   6
HELIX  100 100 GLY D  412  GLU D  433  1                                  22
HELIX  101 101 ASP D  436  LYS D  450  1                                  15
HELIX  102 102 SER D  452  LYS D  463  1                                  12
HELIX  103 103 THR V   22  ASN V   36  1                                  15
HELIX  104 104 ASP V   79  TYR V   94  1                                  16
SHEET    1   A 5 ARG A  83  PRO A  89  0
SHEET    2   A 5 TYR A  97  TYR A 103 -1  O  ILE A  98   N  GLU A  88
SHEET    3   A 5 ILE A  36  PRO A  44 -1  N  VAL A  42   O  TYR A  97
SHEET    4   A 5 LEU A 130  ARG A 139 -1  O  ARG A 134   N  ARG A  41
SHEET    5   A 5 GLY A 308  MET A 309  1  O  GLY A 308   N  LEU A 135
SHEET    1   B 8 LEU A 169  GLY A 171  0
SHEET    2   B 8 VAL A 399  GLN A 401  1  O  LEU A 400   N  LEU A 169
SHEET    3   B 8 LEU A 375  SER A 379  1  N  ALA A 378   O  GLN A 401
SHEET    4   B 8 HIS A 325  HIS A 327  1  N  ILE A 326   O  VAL A 377
SHEET    5   B 8 LEU A 290  HIS A 294  1  N  ILE A 293   O  HIS A 325
SHEET    6   B 8 ILE A 264  ASP A 268  1  N  VAL A 265   O  HIS A 292
SHEET    7   B 8 GLY A 237  ASN A 241  1  N  LEU A 240   O  MET A 266
SHEET    8   B 8 PHE A 199  KCX A 201  1  N  THR A 200   O  TYR A 239
SHEET    1   C 2 TYR A 353  THR A 354  0
SHEET    2   C 2 GLN A 366  SER A 367 -1  O  GLN A 366   N  THR A 354
SHEET    1   D 4 THR S  68  TRP S  70  0
SHEET    2   D 4 VAL S  39  GLU S  45 -1  N  LEU S  42   O  TRP S  70
SHEET    3   D 4 PHE S  98  ASP S 105 -1  O  ILE S 102   N  CYS S  41
SHEET    4   D 4 VAL S 110  TYR S 118 -1  O  ALA S 117   N  ILE S  99
SHEET    1   E 5 ARG B  83  PRO B  89  0
SHEET    2   E 5 TYR B  97  TYR B 103 -1  O  ILE B  98   N  GLU B  88
SHEET    3   E 5 ILE B  36  PRO B  44 -1  N  VAL B  42   O  TYR B  97
SHEET    4   E 5 LEU B 130  ARG B 139 -1  O  ARG B 134   N  ARG B  41
SHEET    5   E 5 GLY B 308  MET B 309  1  O  GLY B 308   N  LEU B 135
SHEET    1   F 8 LEU B 169  GLY B 171  0
SHEET    2   F 8 VAL B 399  GLN B 401  1  O  LEU B 400   N  GLY B 171
SHEET    3   F 8 LEU B 375  SER B 379  1  N  ALA B 378   O  GLN B 401
SHEET    4   F 8 HIS B 325  HIS B 327  1  N  ILE B 326   O  VAL B 377
SHEET    5   F 8 LEU B 290  HIS B 294  1  N  ILE B 293   O  HIS B 325
SHEET    6   F 8 ILE B 264  ASP B 268  1  N  VAL B 265   O  HIS B 292
SHEET    7   F 8 GLY B 237  ASN B 241  1  N  LEU B 240   O  MET B 266
SHEET    8   F 8 PHE B 199  KCX B 201  1  N  THR B 200   O  TYR B 239
SHEET    1   G 2 TYR B 353  THR B 354  0
SHEET    2   G 2 GLN B 366  SER B 367 -1  O  GLN B 366   N  THR B 354
SHEET    1   H 4 THR T  68  TRP T  70  0
SHEET    2   H 4 VAL T  39  GLU T  45 -1  N  PHE T  44   O  THR T  68
SHEET    3   H 4 PHE T  98  ASP T 105 -1  O  ARG T 100   N  GLU T  43
SHEET    4   H 4 VAL T 110  TYR T 118 -1  O  ALA T 117   N  ILE T  99
SHEET    1   I 5 ARG C  83  PRO C  89  0
SHEET    2   I 5 TYR C  97  TYR C 103 -1  O  ILE C  98   N  GLU C  88
SHEET    3   I 5 ILE C  36  PRO C  44 -1  N  VAL C  42   O  TYR C  97
SHEET    4   I 5 LEU C 130  ARG C 139 -1  O  ARG C 134   N  ARG C  41
SHEET    5   I 5 GLY C 308  MET C 309  1  O  GLY C 308   N  LEU C 135
SHEET    1   J 8 LEU C 169  GLY C 171  0
SHEET    2   J 8 VAL C 399  GLN C 401  1  O  LEU C 400   N  LEU C 169
SHEET    3   J 8 LEU C 375  SER C 379  1  N  ALA C 378   O  GLN C 401
SHEET    4   J 8 HIS C 325  HIS C 327  1  N  ILE C 326   O  VAL C 377
SHEET    5   J 8 LEU C 290  HIS C 294  1  N  ILE C 293   O  HIS C 325
SHEET    6   J 8 ILE C 264  ASP C 268  1  N  VAL C 265   O  HIS C 292
SHEET    7   J 8 GLY C 237  ASN C 241  1  N  LEU C 240   O  MET C 266
SHEET    8   J 8 PHE C 199  KCX C 201  1  N  THR C 200   O  TYR C 239
SHEET    1   K 2 TYR C 353  THR C 354  0
SHEET    2   K 2 GLN C 366  SER C 367 -1  O  GLN C 366   N  THR C 354
SHEET    1   L 4 THR U  68  TRP U  70  0
SHEET    2   L 4 VAL U  39  GLU U  45 -1  N  LEU U  42   O  TRP U  70
SHEET    3   L 4 PHE U  98  ASP U 105 -1  O  PHE U 104   N  VAL U  39
SHEET    4   L 4 VAL U 110  TYR U 118 -1  O  ALA U 117   N  ILE U  99
SHEET    1   M 5 ARG D  83  PRO D  89  0
SHEET    2   M 5 TYR D  97  TYR D 103 -1  O  ILE D  98   N  GLU D  88
SHEET    3   M 5 ILE D  36  PRO D  44 -1  N  VAL D  42   O  TYR D  97
SHEET    4   M 5 LEU D 130  ARG D 139 -1  O  ARG D 134   N  ARG D  41
SHEET    5   M 5 GLY D 308  MET D 309  1  O  GLY D 308   N  LEU D 135
SHEET    1   N 8 LEU D 169  GLY D 171  0
SHEET    2   N 8 VAL D 399  GLN D 401  1  O  LEU D 400   N  LEU D 169
SHEET    3   N 8 LEU D 375  SER D 379  1  N  ALA D 378   O  GLN D 401
SHEET    4   N 8 HIS D 325  HIS D 327  1  N  ILE D 326   O  VAL D 377
SHEET    5   N 8 LEU D 290  HIS D 294  1  N  ILE D 293   O  HIS D 325
SHEET    6   N 8 ILE D 264  ASP D 268  1  N  VAL D 265   O  HIS D 292
SHEET    7   N 8 GLY D 237  ASN D 241  1  N  LEU D 240   O  MET D 266
SHEET    8   N 8 PHE D 199  KCX D 201  1  N  THR D 200   O  TYR D 239
SHEET    1   O 2 TYR D 353  THR D 354  0
SHEET    2   O 2 GLN D 366  SER D 367 -1  O  GLN D 366   N  THR D 354
SHEET    1   P 4 THR V  68  TRP V  70  0
SHEET    2   P 4 VAL V  39  GLU V  45 -1  N  LEU V  42   O  TRP V  70
SHEET    3   P 4 PHE V  98  ASP V 105 -1  O  ILE V 102   N  CYS V  41
SHEET    4   P 4 VAL V 110  TYR V 118 -1  O  ALA V 117   N  ILE V  99
SSBOND   1 CYS A  247    CYS C  247                          1555   3555  2.55
SSBOND   2 CYS B  247    CYS B  247                          1555   3555  2.06
SSBOND   3 CYS D  247    CYS D  247                          1555   3555  2.09
LINK        MG    MG A 476                 OQ2 KCX A 201     1555   1555  2.08
LINK        MG    MG A 476                 OD1 ASP A 203     1555   1555  2.05
LINK        MG    MG A 476                 OE1 GLU A 204     1555   1555  2.03
LINK        MG    MG B 476                 OQ2 KCX B 201     1555   1555  2.19
LINK        MG    MG B 476                 OD1 ASP B 203     1555   1555  2.04
LINK        MG    MG B 476                 OE1 GLU B 204     1555   1555  2.03
LINK        MG    MG B 476                 O6  CAP B 501     1555   1555  2.15
LINK        MG    MG C 476                 OQ2 KCX C 201     1555   1555  2.10
LINK        MG    MG C 476                 OD1 ASP C 203     1555   1555  2.01
LINK        MG    MG C 476                 OE1 GLU C 204     1555   1555  2.05
LINK        MG    MG D 476                 OQ2 KCX D 201     1555   1555  2.11
LINK        MG    MG D 476                 OD1 ASP D 203     1555   1555  2.06
LINK        MG    MG D 476                 OE1 GLU D 204     1555   1555  2.10
LINK        MG    MG D 476                 O3  CAP D 501     1555   1555  2.19
LINK        MG    MG D 476                 O6  CAP D 501     1555   1555  2.17
LINK         C   THR A 200                 N   KCX A 201     1555   1555  1.33
LINK         C   KCX A 201                 N   ASP A 202     1555   1555  1.33
LINK        MG    MG A 476                 O6  CAP A 501     1555   1555  2.25
LINK        MG    MG A 476                 O3  CAP A 501     1555   1555  2.22
LINK        MG    MG A 476                 O2  CAP A 501     1555   1555  2.34
LINK         C   THR B 200                 N   KCX B 201     1555   1555  1.33
LINK         C   KCX B 201                 N   ASP B 202     1555   1555  1.33
LINK        MG    MG B 476                 O3  CAP B 501     1555   1555  2.26
LINK        MG    MG B 476                 O2  CAP B 501     1555   1555  2.37
LINK         C   THR C 200                 N   KCX C 201     1555   1555  1.33
LINK         C   KCX C 201                 N   ASP C 202     1555   1555  1.33
LINK        MG    MG C 476                 O2  CAP C 501     1555   1555  2.33
LINK        MG    MG C 476                 O6  CAP C 501     1555   1555  2.25
LINK        MG    MG C 476                 O3  CAP C 501     1555   1555  2.24
LINK         C   THR D 200                 N   KCX D 201     1555   1555  1.33
LINK         C   KCX D 201                 N   ASP D 202     1555   1555  1.33
LINK        MG    MG D 476                 O2  CAP D 501     1555   1555  2.34
LINK         C   MME S   1                 N   LYS S   2     1555   1555  1.33
LINK         C   MME T   1                 N   LYS T   2     1555   1555  1.33
LINK         C   MME U   1                 N   LYS U   2     1555   1555  1.33
LINK         C   MME V   1                 N   LYS V   2     1555   1555  1.33
CISPEP   1 LYS A  175    PRO A  176          0        -4.68
CISPEP   2 LYS B  175    PRO B  176          0        -0.25
CISPEP   3 LYS C  175    PRO C  176          0         0.12
CISPEP   4 LYS D  175    PRO D  176          0         0.03
SITE     1 AC1  4 KCX A 201  ASP A 203  GLU A 204  CAP A 501
SITE     1 AC2  4 KCX B 201  ASP B 203  GLU B 204  CAP B 501
SITE     1 AC3  4 KCX C 201  ASP C 203  GLU C 204  CAP C 501
SITE     1 AC4  4 KCX D 201  ASP D 203  GLU D 204  CAP D 501
SITE     1 AC5 29 THR A 173  LYS A 175  LYS A 177  KCX A 201
SITE     2 AC5 29 ASP A 203  GLU A 204  HIS A 294  ARG A 295
SITE     3 AC5 29 HIS A 327  LYS A 334  LEU A 335  SER A 379
SITE     4 AC5 29 GLY A 380  GLY A 381  GLY A 403  GLY A 404
SITE     5 AC5 29  MG A 476  HOH A 503  HOH A 505  HOH A 508
SITE     6 AC5 29 HOH A 520  HOH A 524  HOH A 558  HOH A 580
SITE     7 AC5 29 HOH A 623  GLU C  60  THR C  65  TRP C  66
SITE     8 AC5 29 ASN C 123
SITE     1 AC6 28 GLU B  60  THR B  65  TRP B  66  ASN B 123
SITE     2 AC6 28 THR B 173  LYS B 175  LYS B 177  KCX B 201
SITE     3 AC6 28 ASP B 203  GLU B 204  HIS B 294  ARG B 295
SITE     4 AC6 28 HIS B 327  LYS B 334  LEU B 335  SER B 379
SITE     5 AC6 28 GLY B 380  GLY B 381  GLY B 403  GLY B 404
SITE     6 AC6 28  MG B 476  HOH B 507  HOH B 522  HOH B 547
SITE     7 AC6 28 HOH B 548  HOH B 550  HOH B 602  HOH B 695
SITE     1 AC7 29 GLU A  60  THR A  65  TRP A  66  ASN A 123
SITE     2 AC7 29 THR C 173  LYS C 175  LYS C 177  KCX C 201
SITE     3 AC7 29 ASP C 203  GLU C 204  HIS C 294  ARG C 295
SITE     4 AC7 29 HIS C 327  LYS C 334  LEU C 335  SER C 379
SITE     5 AC7 29 GLY C 380  GLY C 381  GLY C 403  GLY C 404
SITE     6 AC7 29  MG C 476  HOH C 502  HOH C 504  HOH C 548
SITE     7 AC7 29 HOH C 549  HOH C 551  HOH C 554  HOH C 575
SITE     8 AC7 29 HOH C 598
SITE     1 AC8 28 GLU D  60  THR D  65  TRP D  66  ASN D 123
SITE     2 AC8 28 THR D 173  LYS D 175  LYS D 177  KCX D 201
SITE     3 AC8 28 ASP D 203  GLU D 204  HIS D 294  ARG D 295
SITE     4 AC8 28 HIS D 327  LYS D 334  LEU D 335  SER D 379
SITE     5 AC8 28 GLY D 380  GLY D 381  GLY D 403  GLY D 404
SITE     6 AC8 28  MG D 476  HOH D 507  HOH D 526  HOH D 551
SITE     7 AC8 28 HOH D 555  HOH D 559  HOH D 585  HOH D 610
CRYST1  157.800  157.800  200.900  90.00  90.00  90.00 C 2 2 21     32
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      0.006337  0.000000  0.000000        0.00000
SCALE2      0.000000  0.006337  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004978        0.00000
      
PROCHECK
Go to PROCHECK summary
 References