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PDBsum entry 1wdd

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
1wdd
Jmol
Contents
Protein chains
465 a.a.
122 a.a.
Ligands
CAP ×2
GOL ×17
Metals
_MG ×2
Waters ×999
HEADER    LYASE                                   13-MAY-04   1WDD
TITLE     CRYSTAL STRUCTURE OF ACTIVATED RICE RUBISCO COMPLEXED WITH 2-
TITLE    2 CARBOXYARABINITOL-1,5-BISPHOSPHATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN;
COMPND   3 CHAIN: A, E;
COMPND   4 SYNONYM: LARGE SUBUNIT OF RIBULOSE-1,5-BISPHOSPHATE
COMPND   5 CARBOXYLASE/OXYGENASE, RUBISCO LARGE SUBUNIT;
COMPND   6 EC: 4.1.1.39;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN C;
COMPND   9 CHAIN: S, W;
COMPND  10 SYNONYM: SMALL SUBUNIT OF RIBULOSE-1,5-BISPHOSPHATE
COMPND  11 CARBOXYLASE/OXYGENASE, RUBISCO SMALL SUBUNIT C;
COMPND  12 EC: 4.1.1.39
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ORYZA SATIVA JAPONICA GROUP;
SOURCE   3 ORGANISM_COMMON: JAPANESE RICE;
SOURCE   4 ORGANISM_TAXID: 39947;
SOURCE   5 TISSUE: LEAVES;
SOURCE   6 MOL_ID: 2;
SOURCE   7 ORGANISM_SCIENTIFIC: ORYZA SATIVA JAPONICA GROUP;
SOURCE   8 ORGANISM_COMMON: JAPANESE RICE;
SOURCE   9 ORGANISM_TAXID: 39947;
SOURCE  10 TISSUE: LEAVES
KEYWDS    RUBISCO, PHOTOSYNTHESIS, ALPHA/BETA BARREL, N-METHYLMETHIONINE, POST-
KEYWDS   2 TRANSLATIONAL MODIFICATION, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    E.MIZOHATA,H.MATSUMURA,T.UENO,H.ISHIDA,T.INOUE,A.MAKINO,T.MAE,Y.KAI
REVDAT   5   05-JUN-13 1WDD    1       JRNL
REVDAT   4   13-JUN-12 1WDD    1       JRNL
REVDAT   3   13-JUL-11 1WDD    1       VERSN
REVDAT   2   24-FEB-09 1WDD    1       VERSN
REVDAT   1   13-NOV-04 1WDD    0
JRNL        AUTH   H.MATSUMURA,E.MIZOHATA,H.ISHIDA,A.KOGAMI,T.UENO,A.MAKINO,
JRNL        AUTH 2 T.INOUE,A.YOKOTA,T.MAE,Y.KAI
JRNL        TITL   CRYSTAL STRUCTURE OF RICE RUBISCO AND IMPLICATIONS FOR
JRNL        TITL 2 ACTIVATION INDUCED BY POSITIVE EFFECTORS NADPH AND
JRNL        TITL 3 6-PHOSPHOGLUCONATE
JRNL        REF    J.MOL.BIOL.                   V. 422    75 2012
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   22609438
JRNL        DOI    10.1016/J.JMB.2012.05.014
REMARK   2
REMARK   2 RESOLUTION.    1.35 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
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 : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.35
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.32
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 3255293.900
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.3
REMARK   3   NUMBER OF REFLECTIONS             : 255778
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) : 0.160
REMARK   3   FREE R VALUE                     : 0.182
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 12745
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.002
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.35
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.43
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 84.40
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 35111
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3280
REMARK   3   BIN FREE R VALUE                    : 0.3380
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.90
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1825
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.008
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 9303
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 146
REMARK   3   SOLVENT ATOMS            : 999
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 17.70
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.60
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 1.24000
REMARK   3    B22 (A**2) : 1.24000
REMARK   3    B33 (A**2) : -2.47000
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 COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.15
REMARK   3   ESD FROM SIGMAA              (A) : 0.23
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) : 0.17
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.24
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.022
REMARK   3   BOND ANGLES            (DEGREES) : 1.90
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.80
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.43
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
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 : FLAT MODEL
REMARK   3   KSOL        : 0.41
REMARK   3   BSOL        : 88.98
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  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : CARBOHYDRATE.PARAM
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  4  : ION.PARAM
REMARK   3  PARAMETER FILE  5  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : CARBOHYDRATE.TOP
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP
REMARK   3  TOPOLOGY FILE  4   : ION.TOP
REMARK   3  TOPOLOGY FILE  5   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1WDD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-MAY-04.
REMARK 100 THE RCSB ID CODE IS RCSB023455.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-MAR-03
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SPRING-8
REMARK 200  BEAMLINE                       : BL44XU
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.90000
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : BRUKER DIP-6040
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
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) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1IR1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 45.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
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   -Y,X,Z
REMARK 290       4555   Y,-X,Z
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -Y+1/2,X+1/2,Z+1/2
REMARK 290       8555   Y+1/2,-X+1/2,Z+1/2
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  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   4 -1.000000  0.000000  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       55.85650
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       55.85650
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       98.39000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       55.85650
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       55.85650
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       98.39000
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       55.85650
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       55.85650
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       98.39000
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000       55.85650
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       55.85650
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       98.39000
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 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: 131610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 111360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -549.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, S, E, W
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      111.71300
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      111.71300
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000      111.71300
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000      111.71300
REMARK 350   BIOMT3   4  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 S 247  LIES ON A SPECIAL POSITION.
REMARK 375      HOH W 937  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     ASP A   476
REMARK 465     SER A   477
REMARK 465     GLU S   123
REMARK 465     GLU S   124
REMARK 465     SER S   125
REMARK 465     GLY S   126
REMARK 465     GLY S   127
REMARK 465     ASN S   128
REMARK 465     MET E     1
REMARK 465     SER E     2
REMARK 465     PRO E     3
REMARK 465     GLN E     4
REMARK 465     THR E     5
REMARK 465     GLU E     6
REMARK 465     THR E     7
REMARK 465     LYS E     8
REMARK 465     ALA E     9
REMARK 465     SER E    10
REMARK 465     VAL E    11
REMARK 465     ASP E   476
REMARK 465     SER E   477
REMARK 465     GLU W   123
REMARK 465     GLU W   124
REMARK 465     SER W   125
REMARK 465     GLY W   126
REMARK 465     GLY W   127
REMARK 465     ASN W   128
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 A  3299     O    HOH A  3362              1.84
REMARK 500   O    HOH A  3299     O    HOH A  3300              1.87
REMARK 500   O    HOH A  3365     O    HOH S   215              2.02
REMARK 500   O    HOH A  3306     O    HOH A  3409              2.03
REMARK 500   OD2  ASP W    25     O    HOH W   935              2.03
REMARK 500   O    HOH A  3085     O    HOH E  3376              2.05
REMARK 500   NZ   LYS E   356     O    HOH E  3356              2.06
REMARK 500   O    HOH A  3358     O    HOH A  3369              2.07
REMARK 500   O    HOH A  3165     O    HOH A  3407              2.08
REMARK 500   ND2  ASN E    95     O    HOH E  3315              2.09
REMARK 500   O    HOH A  3024     O    HOH A  3402              2.09
REMARK 500   O    HOH A  3282     O    HOH A  3352              2.09
REMARK 500   O    HOH W   753     O    HOH W   972              2.09
REMARK 500   OD2  ASP S    25     O    HOH S   192              2.10
REMARK 500   O1   GOL E  3002     O    HOH E  3375              2.10
REMARK 500   O    HOH A  3375     O    HOH E  3018              2.10
REMARK 500   NZ   LYS W    84     OE1  GLU W    88              2.15
REMARK 500   O    HOH S   223     O    HOH S   232              2.16
REMARK 500   O    HOH E  3205     O    HOH E  3262              2.16
REMARK 500   O    HOH A  3170     O    HOH A  3394              2.17
REMARK 500   O    HOH E  3353     O    HOH E  3354              2.17
REMARK 500   O    HOH W   483     O    HOH W   863              2.17
REMARK 500   O    HOH A  3292     O    HOH A  3361              2.18
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   OE1  GLU W     7     NZ   LYS W    46     4565     1.91
REMARK 500   O    HOH A  3321     O    HOH E  3375     4565     1.94
REMARK 500   O    HOH E  3249     O    HOH E  3352     4565     2.02
REMARK 500   OE2  GLU W    24     O    HOH S   192     6555     2.08
REMARK 500   O    HOH E  3320     O    HOH W   693     4565     2.10
REMARK 500   O    HOH A  3266     O    HOH E  3363     3555     2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ARG A 159   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    ARG A 187   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    ARG A 253   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES
REMARK 500    ARG E 159   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    ARG E 303   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    SER A  62      -74.95   -143.02
REMARK 500    ASN A  95       39.28   -146.11
REMARK 500    HIS A 153      -55.14   -133.17
REMARK 500    CYS A 172      128.19   -177.08
REMARK 500    ASN A 207      -93.72   -125.30
REMARK 500    MET A 212      112.87   -170.73
REMARK 500    MET A 297       -6.48     82.70
REMARK 500    VAL A 331      -53.04     73.23
REMARK 500    ASP A 357       90.12   -162.64
REMARK 500    VAL A 369       53.58     36.12
REMARK 500    GLU S  13     -145.69     63.96
REMARK 500    LEU S  15       -4.60     88.29
REMARK 500    LYS S  37       30.18     73.18
REMARK 500    LYS S  70     -126.49     55.78
REMARK 500    SER E  62      -78.40   -141.05
REMARK 500    THR E  75     -162.82   -128.43
REMARK 500    HIS E 153      -58.37   -132.20
REMARK 500    CYS E 172      125.61   -176.09
REMARK 500    ASN E 207      -91.33   -125.70
REMARK 500    MET E 212      112.40   -170.09
REMARK 500    MET E 297       -4.85     88.22
REMARK 500    VAL E 331      -51.78     70.65
REMARK 500    ASP E 357       94.16   -161.29
REMARK 500    VAL E 369       56.78     34.57
REMARK 500    GLU W  13     -146.64     62.34
REMARK 500    LEU W  15       -8.52     83.68
REMARK 500    LYS W  70     -128.68     56.78
REMARK 500    SER W 113      119.42   -165.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    TYR S  60         0.06    SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A3211        DISTANCE =  9.48 ANGSTROMS
REMARK 525    HOH A3277        DISTANCE =  5.04 ANGSTROMS
REMARK 525    HOH A3281        DISTANCE =  7.90 ANGSTROMS
REMARK 525    HOH A3323        DISTANCE =  8.90 ANGSTROMS
REMARK 525    HOH A3324        DISTANCE = 11.23 ANGSTROMS
REMARK 525    HOH A3329        DISTANCE =  7.64 ANGSTROMS
REMARK 525    HOH A3331        DISTANCE =  5.89 ANGSTROMS
REMARK 525    HOH A3332        DISTANCE =  8.36 ANGSTROMS
REMARK 525    HOH A3338        DISTANCE =  5.09 ANGSTROMS
REMARK 525    HOH A3343        DISTANCE =  7.85 ANGSTROMS
REMARK 525    HOH A3351        DISTANCE = 11.56 ANGSTROMS
REMARK 525    HOH A3359        DISTANCE =  8.56 ANGSTROMS
REMARK 525    HOH A3367        DISTANCE =  5.90 ANGSTROMS
REMARK 525    HOH A3372        DISTANCE =  6.07 ANGSTROMS
REMARK 525    HOH A3405        DISTANCE =  7.23 ANGSTROMS
REMARK 525    HOH A3406        DISTANCE =  8.32 ANGSTROMS
REMARK 525    HOH A3417        DISTANCE =  7.63 ANGSTROMS
REMARK 525    HOH E3258        DISTANCE =  5.38 ANGSTROMS
REMARK 525    HOH E3272        DISTANCE =  9.10 ANGSTROMS
REMARK 525    HOH E3298        DISTANCE = 10.28 ANGSTROMS
REMARK 525    HOH E3299        DISTANCE =  7.55 ANGSTROMS
REMARK 525    HOH E3331        DISTANCE =  5.35 ANGSTROMS
REMARK 525    HOH E3333        DISTANCE =  8.07 ANGSTROMS
REMARK 525    HOH E3336        DISTANCE =  8.07 ANGSTROMS
REMARK 525    HOH E3339        DISTANCE =  9.12 ANGSTROMS
REMARK 525    HOH E3357        DISTANCE =  8.90 ANGSTROMS
REMARK 525    HOH E3359        DISTANCE =  9.12 ANGSTROMS
REMARK 525    HOH E3368        DISTANCE =  6.09 ANGSTROMS
REMARK 525    HOH E3370        DISTANCE =  7.76 ANGSTROMS
REMARK 525    HOH E3371        DISTANCE =  7.79 ANGSTROMS
REMARK 525    HOH S 210        DISTANCE =  9.69 ANGSTROMS
REMARK 525    HOH S 212        DISTANCE = 13.50 ANGSTROMS
REMARK 525    HOH S 213        DISTANCE = 12.90 ANGSTROMS
REMARK 525    HOH S 214        DISTANCE = 15.09 ANGSTROMS
REMARK 525    HOH S 237        DISTANCE =  6.25 ANGSTROMS
REMARK 525    HOH S 245        DISTANCE =  7.45 ANGSTROMS
REMARK 525    HOH S 246        DISTANCE = 12.75 ANGSTROMS
REMARK 525    HOH S 247        DISTANCE = 16.25 ANGSTROMS
REMARK 525    HOH W 551        DISTANCE =  5.67 ANGSTROMS
REMARK 525    HOH W 676        DISTANCE =  6.83 ANGSTROMS
REMARK 525    HOH W 745        DISTANCE =  5.01 ANGSTROMS
REMARK 525    HOH W 771        DISTANCE =  5.65 ANGSTROMS
REMARK 525    HOH W 772        DISTANCE =  5.51 ANGSTROMS
REMARK 525    HOH W 860        DISTANCE =  6.03 ANGSTROMS
REMARK 525    HOH W 933        DISTANCE =  5.69 ANGSTROMS
REMARK 525    HOH W 937        DISTANCE =  6.89 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 A1476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX A 201   OQ2
REMARK 620 2 GLU A 204   OE1  93.7
REMARK 620 3 CAP A1001   O2   92.3 161.2
REMARK 620 4 CAP A1001   O3   86.7  89.0  73.6
REMARK 620 5 CAP A1001   O6  167.0  98.0  74.7  87.8
REMARK 620 6 ASP A 203   OD1  86.6  91.8 106.4 173.4  98.6
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG E2476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX E 201   OQ2
REMARK 620 2 CAP E2001   O6  166.2
REMARK 620 3 GLU E 204   OE1  93.7  98.9
REMARK 620 4 CAP E2001   O2   92.1  74.1 160.9
REMARK 620 5 CAP E2001   O3   85.8  89.0  89.0  73.3
REMARK 620 6 ASP E 203   OD1  85.4  99.0  94.1 104.5 170.9
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 1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 2476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 3003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 3005
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3006
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL W 3007
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL W 3008
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 3009
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3010
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 3011
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3012
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 3013
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 3014
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3015
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 3016
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3017
DBREF  1WDD A    1   477  UNP    P0C512   RBL_ORYSJ        1    477
DBREF  1WDD S    1   128  UNP    Q0INY7   RBS1_ORYSJ      48    175
DBREF  1WDD E    1   477  UNP    P0C512   RBL_ORYSJ        1    477
DBREF  1WDD W    1   128  UNP    Q0INY7   RBS1_ORYSJ      48    175
SEQRES   1 A  477  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLY PHE
SEQRES   2 A  477  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR
SEQRES   3 A  477  PRO GLU TYR GLU THR LYS ASP THR ASP ILE LEU ALA ALA
SEQRES   4 A  477  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 A  477  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 A  477  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 A  477  ARG TYR LYS GLY ARG CYS TYR HIS ILE GLU PRO VAL VAL
SEQRES   8 A  477  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR PRO
SEQRES   9 A  477  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 A  477  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 A  477  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO THR
SEQRES  12 A  477  TYR SER LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 A  477  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU
SEQRES  14 A  477  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 A  477  LYS ASN TYR GLY ARG ALA CYS TYR GLU CYS LEU ARG GLY
SEQRES  16 A  477  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 A  477  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE VAL PHE CYS
SEQRES  18 A  477  ALA GLU ALA ILE TYR LYS SER GLN ALA GLU THR GLY GLU
SEQRES  19 A  477  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 A  477  GLU GLU MET ILE LYS ARG ALA VAL PHE ALA ARG GLU LEU
SEQRES  21 A  477  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 A  477  PHE THR ALA ASN THR SER LEU ALA HIS TYR CYS ARG ASP
SEQRES  23 A  477  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 A  477  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG
SEQRES  25 A  477  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 A  477  ILE HIS ALA GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 A  477  ARG GLU MET THR LEU GLY PHE VAL ASP LEU LEU ARG ASP
SEQRES  28 A  477  ASP PHE ILE GLU LYS ASP ARG ALA ARG GLY ILE PHE PHE
SEQRES  29 A  477  THR GLN ASP TRP VAL SER MET PRO GLY VAL ILE PRO VAL
SEQRES  30 A  477  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 A  477  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY
SEQRES  32 A  477  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 A  477  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN
SEQRES  34 A  477  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN
SEQRES  35 A  477  GLU ILE ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 A  477  ALA ALA ALA CYS GLU ILE TRP LYS ALA ILE LYS PHE GLU
SEQRES  37 A  477  PHE GLU PRO VAL ASP LYS LEU ASP SER
SEQRES   1 S  128  MME GLN VAL TRP PRO ILE GLU GLY ILE LYS LYS PHE GLU
SEQRES   2 S  128  THR LEU SER TYR LEU PRO PRO LEU THR VAL GLU ASP LEU
SEQRES   3 S  128  LEU LYS GLN ILE GLU TYR LEU LEU ARG SER LYS TRP VAL
SEQRES   4 S  128  PRO CYS LEU GLU PHE SER LYS VAL GLY PHE VAL TYR ARG
SEQRES   5 S  128  GLU ASN HIS ARG SER PRO GLY TYR TYR ASP GLY ARG TYR
SEQRES   6 S  128  TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR ASP
SEQRES   7 S  128  ALA THR GLN VAL LEU LYS GLU LEU GLU GLU ALA LYS LYS
SEQRES   8 S  128  ALA TYR PRO ASP ALA PHE VAL ARG ILE ILE GLY PHE ASP
SEQRES   9 S  128  ASN VAL ARG GLN VAL GLN LEU ILE SER PHE ILE ALA TYR
SEQRES  10 S  128  LYS PRO PRO GLY CYS GLU GLU SER GLY GLY ASN
SEQRES   1 E  477  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLY PHE
SEQRES   2 E  477  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR
SEQRES   3 E  477  PRO GLU TYR GLU THR LYS ASP THR ASP ILE LEU ALA ALA
SEQRES   4 E  477  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 E  477  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 E  477  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 E  477  ARG TYR LYS GLY ARG CYS TYR HIS ILE GLU PRO VAL VAL
SEQRES   8 E  477  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR PRO
SEQRES   9 E  477  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 E  477  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 E  477  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO THR
SEQRES  12 E  477  TYR SER LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 E  477  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU
SEQRES  14 E  477  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 E  477  LYS ASN TYR GLY ARG ALA CYS TYR GLU CYS LEU ARG GLY
SEQRES  16 E  477  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 E  477  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE VAL PHE CYS
SEQRES  18 E  477  ALA GLU ALA ILE TYR LYS SER GLN ALA GLU THR GLY GLU
SEQRES  19 E  477  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 E  477  GLU GLU MET ILE LYS ARG ALA VAL PHE ALA ARG GLU LEU
SEQRES  21 E  477  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 E  477  PHE THR ALA ASN THR SER LEU ALA HIS TYR CYS ARG ASP
SEQRES  23 E  477  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 E  477  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG
SEQRES  25 E  477  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 E  477  ILE HIS ALA GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 E  477  ARG GLU MET THR LEU GLY PHE VAL ASP LEU LEU ARG ASP
SEQRES  28 E  477  ASP PHE ILE GLU LYS ASP ARG ALA ARG GLY ILE PHE PHE
SEQRES  29 E  477  THR GLN ASP TRP VAL SER MET PRO GLY VAL ILE PRO VAL
SEQRES  30 E  477  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 E  477  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY
SEQRES  32 E  477  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 E  477  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN
SEQRES  34 E  477  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN
SEQRES  35 E  477  GLU ILE ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 E  477  ALA ALA ALA CYS GLU ILE TRP LYS ALA ILE LYS PHE GLU
SEQRES  37 E  477  PHE GLU PRO VAL ASP LYS LEU ASP SER
SEQRES   1 W  128  MME GLN VAL TRP PRO ILE GLU GLY ILE LYS LYS PHE GLU
SEQRES   2 W  128  THR LEU SER TYR LEU PRO PRO LEU THR VAL GLU ASP LEU
SEQRES   3 W  128  LEU LYS GLN ILE GLU TYR LEU LEU ARG SER LYS TRP VAL
SEQRES   4 W  128  PRO CYS LEU GLU PHE SER LYS VAL GLY PHE VAL TYR ARG
SEQRES   5 W  128  GLU ASN HIS ARG SER PRO GLY TYR TYR ASP GLY ARG TYR
SEQRES   6 W  128  TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR ASP
SEQRES   7 W  128  ALA THR GLN VAL LEU LYS GLU LEU GLU GLU ALA LYS LYS
SEQRES   8 W  128  ALA TYR PRO ASP ALA PHE VAL ARG ILE ILE GLY PHE ASP
SEQRES   9 W  128  ASN VAL ARG GLN VAL GLN LEU ILE SER PHE ILE ALA TYR
SEQRES  10 W  128  LYS PRO PRO GLY CYS GLU GLU SER GLY GLY ASN
MODRES 1WDD KCX A  201  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 1WDD MME S    1  MET  N-METHYL METHIONINE
MODRES 1WDD KCX E  201  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 1WDD MME W    1  MET  N-METHYL METHIONINE
HET    KCX  A 201      12
HET    MME  S   1       9
HET    KCX  E 201      12
HET    MME  W   1       9
HET     MG  A1476       1
HET     MG  E2476       1
HET    CAP  A1001      21
HET    CAP  E2001      21
HET    GOL  A3001       6
HET    GOL  E3002       6
HET    GOL  E3003       6
HET    GOL  A3004       6
HET    GOL  E3005       6
HET    GOL  A3006       6
HET    GOL  W3007       6
HET    GOL  W3008       6
HET    GOL  E3009       6
HET    GOL  A3010       6
HET    GOL  E3011       6
HET    GOL  A3012       6
HET    GOL  E3013       6
HET    GOL  E3014       6
HET    GOL  A3015       6
HET    GOL  E3016       6
HET    GOL  A3017       6
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID
HETNAM     MME N-METHYL METHIONINE
HETNAM      MG MAGNESIUM ION
HETNAM     CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE
HETNAM     GOL GLYCEROL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   1  KCX    2(C7 H14 N2 O4)
FORMUL   2  MME    2(C6 H13 N O2 S)
FORMUL   5   MG    2(MG 2+)
FORMUL   7  CAP    2(C6 H14 O13 P2)
FORMUL   9  GOL    17(C3 H8 O3)
FORMUL  26  HOH   *999(H2 O)
HELIX    1   1 TYR A   20  TYR A   25  1                                   6
HELIX    2   2 PRO A   49  SER A   61  1                                  13
HELIX    3   3 VAL A   69  THR A   75  5                                   7
HELIX    4   4 SER A   76  LYS A   81  1                                   6
HELIX    5   5 PRO A  104  PHE A  108  5                                   5
HELIX    6   6 SER A  112  GLY A  122  1                                  11
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  SER S   36  1                                  15
HELIX   26  26 ASP S   78  TYR S   93  1                                  16
HELIX   27  27 TYR E   20  TYR E   25  1                                   6
HELIX   28  28 PRO E   49  SER E   61  1                                  13
HELIX   29  29 VAL E   69  THR E   75  5                                   7
HELIX   30  30 SER E   76  LYS E   81  1                                   6
HELIX   31  31 PRO E  104  PHE E  108  5                                   5
HELIX   32  32 SER E  112  GLY E  122  1                                  11
HELIX   33  33 ASN E  123  PHE E  127  5                                   5
HELIX   34  34 PRO E  141  LYS E  146  1                                   6
HELIX   35  35 GLY E  154  ASN E  163  1                                  10
HELIX   36  36 SER E  181  GLY E  195  1                                  15
HELIX   37  37 ARG E  213  GLY E  233  1                                  21
HELIX   38  38 THR E  246  GLY E  261  1                                  16
HELIX   39  39 TYR E  269  GLY E  273  1                                   5
HELIX   40  40 GLY E  273  ASN E  287  1                                  15
HELIX   41  41 MET E  297  ARG E  303  1                                   7
HELIX   42  42 HIS E  310  GLY E  322  1                                  13
HELIX   43  43 GLU E  338  ASP E  351  1                                  14
HELIX   44  44 ASP E  357  GLY E  361  5                                   5
HELIX   45  45 HIS E  383  TRP E  385  5                                   3
HELIX   46  46 HIS E  386  GLY E  395  1                                  10
HELIX   47  47 GLY E  403  GLY E  408  1                                   6
HELIX   48  48 GLY E  412  GLY E  434  1                                  23
HELIX   49  49 ASP E  436  LYS E  450  1                                  15
HELIX   50  50 SER E  452  LYS E  463  1                                  12
HELIX   51  51 THR W   22  SER W   36  1                                  15
HELIX   52  52 ASP W   78  TYR W   93  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  PHE A  40   O  ALA A  99
SHEET    4   A 5 LEU A 130  ARG A 139 -1  O  ARG A 131   N  THR A  43
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 ILE 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 PHE A 353  ILE A 354  0
SHEET    2   C 2 GLN A 366  ASP A 367 -1  O  GLN A 366   N  ILE A 354
SHEET    1   D 4 THR S  67  TRP S  69  0
SHEET    2   D 4 VAL S  39  SER S  45 -1  N  LEU S  42   O  TRP S  69
SHEET    3   D 4 PHE S  97  ASP S 104 -1  O  ILE S 101   N  CYS S  41
SHEET    4   D 4 VAL S 109  TYR S 117 -1  O  LEU S 111   N  GLY S 102
SHEET    1   E 5 ARG E  83  PRO E  89  0
SHEET    2   E 5 TYR E  97  TYR E 103 -1  O  TYR E 100   N  HIS E  86
SHEET    3   E 5 ILE E  36  PRO E  44 -1  N  ILE E  36   O  TYR E 103
SHEET    4   E 5 LEU E 130  ARG E 139 -1  O  ARG E 131   N  THR E  43
SHEET    5   E 5 GLY E 308  MET E 309  1  O  GLY E 308   N  LEU E 135
SHEET    1   F 8 LEU E 169  GLY E 171  0
SHEET    2   F 8 VAL E 399  GLN E 401  1  O  LEU E 400   N  LEU E 169
SHEET    3   F 8 ILE E 375  SER E 379  1  N  ALA E 378   O  GLN E 401
SHEET    4   F 8 HIS E 325  HIS E 327  1  N  ILE E 326   O  VAL E 377
SHEET    5   F 8 LEU E 290  HIS E 294  1  N  ILE E 293   O  HIS E 325
SHEET    6   F 8 ILE E 264  ASP E 268  1  N  VAL E 265   O  HIS E 292
SHEET    7   F 8 GLY E 237  ASN E 241  1  N  LEU E 240   O  MET E 266
SHEET    8   F 8 PHE E 199  KCX E 201  1  N  THR E 200   O  TYR E 239
SHEET    1   G 2 PHE E 353  ILE E 354  0
SHEET    2   G 2 GLN E 366  ASP E 367 -1  O  GLN E 366   N  ILE E 354
SHEET    1   H 4 THR W  67  TRP W  69  0
SHEET    2   H 4 VAL W  39  SER W  45 -1  N  LEU W  42   O  TRP W  69
SHEET    3   H 4 PHE W  97  ASP W 104 -1  O  PHE W  97   N  SER W  45
SHEET    4   H 4 VAL W 109  TYR W 117 -1  O  ALA W 116   N  VAL W  98
SSBOND   1 CYS A  247    CYS E  247                          1555   1555  2.53
LINK         C   THR A 200                 N   KCX A 201     1555   1555  1.32
LINK         C   KCX A 201                 N   ASP A 202     1555   1555  1.34
LINK         OQ2 KCX A 201                MG    MG A1476     1555   1555  2.00
LINK        MG    MG A1476                 OE1 GLU A 204     1555   1555  1.99
LINK        MG    MG A1476                 O2  CAP A1001     1555   1555  2.22
LINK        MG    MG A1476                 O3  CAP A1001     1555   1555  2.17
LINK        MG    MG A1476                 O6  CAP A1001     1555   1555  2.09
LINK        MG    MG A1476                 OD1 ASP A 203     1555   1555  1.96
LINK         C   THR E 200                 N   KCX E 201     1555   1555  1.33
LINK         OQ2 KCX E 201                MG    MG E2476     1555   1555  2.00
LINK         C   KCX E 201                 N   ASP E 202     1555   1555  1.34
LINK         O6  CAP E2001                MG    MG E2476     1555   1555  2.05
LINK        MG    MG E2476                 OE1 GLU E 204     1555   1555  2.01
LINK        MG    MG E2476                 O2  CAP E2001     1555   1555  2.25
LINK        MG    MG E2476                 O3  CAP E2001     1555   1555  2.15
LINK        MG    MG E2476                 OD1 ASP E 203     1555   1555  1.89
LINK         C   MME S   1                 N   GLN S   2     1555   1555  1.33
LINK         C   MME W   1                 N   GLN W   2     1555   1555  1.33
CISPEP   1 LYS A  175    PRO A  176          0         0.31
CISPEP   2 LYS E  175    PRO E  176          0         3.75
SITE     1 AC1  5 LYS A 177  KCX A 201  ASP A 203  GLU A 204
SITE     2 AC1  5 CAP A1001
SITE     1 AC2  5 LYS E 177  KCX E 201  ASP E 203  GLU E 204
SITE     2 AC2  5 CAP E2001
SITE     1 AC3 29 THR A 173  LYS A 175  LYS A 177  KCX A 201
SITE     2 AC3 29 ASP A 203  GLU A 204  HIS A 294  ARG A 295
SITE     3 AC3 29 HIS A 327  LYS A 334  LEU A 335  SER A 379
SITE     4 AC3 29 GLY A 380  GLY A 381  GLY A 403  GLY A 404
SITE     5 AC3 29  MG A1476  HOH A3108  HOH A3109  HOH A3115
SITE     6 AC3 29 HOH A3117  HOH A3131  HOH A3132  GLU E  60
SITE     7 AC3 29 THR E  65  TRP E  66  ASN E 123  HOH E3028
SITE     8 AC3 29 HOH E3038
SITE     1 AC4 29 GLU A  60  THR A  65  TRP A  66  ASN A 123
SITE     2 AC4 29 HOH A3032  HOH A3055  THR E 173  LYS E 175
SITE     3 AC4 29 LYS E 177  KCX E 201  ASP E 203  GLU E 204
SITE     4 AC4 29 HIS E 294  ARG E 295  HIS E 327  LYS E 334
SITE     5 AC4 29 LEU E 335  SER E 379  GLY E 380  GLY E 381
SITE     6 AC4 29 GLY E 403  GLY E 404   MG E2476  HOH E3020
SITE     7 AC4 29 HOH E3044  HOH E3045  HOH E3046  HOH E3130
SITE     8 AC4 29 HOH E3131
SITE     1 AC5  9 LYS A  32  PRO A 104  LEU A 105  ASP A 106
SITE     2 AC5  9 HOH A3027  HOH A3166  HOH A3167  HOH A3407
SITE     3 AC5  9 HOH E3142
SITE     1 AC6 10 HOH A3127  HOH A3204  HOH A3205  LYS E  32
SITE     2 AC6 10 PRO E 104  LEU E 105  ASP E 106  HOH E3053
SITE     3 AC6 10 HOH E3362  HOH E3375
SITE     1 AC7  6 LEU A 270  LEU E 270  MET E 297  HOH E3035
SITE     2 AC7  6 HOH E3036  HOH E3037
SITE     1 AC8 10 GLY A  16  VAL A  17  LYS A  18  TYR A  20
SITE     2 AC8 10 THR A  65  THR A  67  THR A  68  GOL A3010
SITE     3 AC8 10 HOH A3021  HOH A3036
SITE     1 AC9  3 GLU E  52  HOH E3042  HOH E3058
SITE     1 BC1  5 GLU A  52  HOH A3029  HOH A3030  HOH A3259
SITE     2 BC1  5 HOH A3360
SITE     1 BC2 10 ASN E 163  ARG E 187  GLU W  43  ARG W  64
SITE     2 BC2 10 TYR W  65  TRP W  66  ARG W  99  GLN W 110
SITE     3 BC2 10 HOH W 536  HOH W 558
SITE     1 BC3  6 GLN W   2  VAL W   3  TRP W  69  ALA W  92
SITE     2 BC3  6 HOH W 312  HOH W 669
SITE     1 BC4  8 TYR E 226  GLN E 229  ALA E 230  HOH E3366
SITE     2 BC4  8 VAL W  50  ASN W  54  ARG W  56  HOH W 555
SITE     1 BC5  9 LYS A  18  THR A  23  THR A  68  ASP A  72
SITE     2 BC5  9 LEU A  77  GOL A3004  GOL A3012  HOH A3038
SITE     3 BC5  9 HOH A3327
SITE     1 BC6 10 GLY E  16  VAL E  17  LYS E  18  TYR E  20
SITE     2 BC6 10 THR E  65  THR E  67  THR E  68  HOH E3026
SITE     3 BC6 10 HOH E3049  HOH E3304
SITE     1 BC7  8 VAL A  11  PHE A  13  THR A  68  VAL A  69
SITE     2 BC7  8 TRP A  70  GLY A  73  GOL A3010  PHE W  74
SITE     1 BC8  4 THR E  68  VAL E  69  TRP E  70  HOH E3183
SITE     1 BC9 10 ARG E 295  HIS E 298  PHE E 311  GLY E 329
SITE     2 BC9 10 GLU E 336  PHE E 345  HOH E3128  HOH E3133
SITE     3 BC9 10 HOH E3172  HOH E3300
SITE     1 CC1 10 ASN A 163  ARG A 187  HOH A3303  GLU S  43
SITE     2 CC1 10 ARG S  64  TYR S  65  TRP S  66  ARG S  99
SITE     3 CC1 10 GLN S 110  HOH S 177
SITE     1 CC2  9 HOH A3263  ILE E 155  GLN E 156  ARG E 350
SITE     2 CC2  9 ASP E 351  ASP E 352  PRO E 372  GLY E 373
SITE     3 CC2  9 HOH E3141
SITE     1 CC3  5 THR A  23  LEU A  77  ASP A  78  LYS A  81
SITE     2 CC3  5 HOH A3161
CRYST1  111.713  111.713  196.780  90.00  90.00  90.00 I 4          16
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      0.008952  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008952  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005082        0.00000
      
PROCHECK
Go to PROCHECK summary
 References