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PDBsum entry 8rub

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Lyase(carbon-carbon) PDB id
8rub
Jmol
Contents
Protein chains
123 a.a.
467 a.a.
Ligands
CAP
Metals
_MG
HEADER    LYASE(CARBON-CARBON)                    13-NOV-90   8RUB
OBSLTE     01-AUG-96 8RUB      8RUC
TITLE     CRYSTALLOGRAPHIC ANALYSIS OF RIBULOSE 1,5-BISPHOSPHATE
TITLE    2 CARBOXYLASE FROM SPINACH AT 2.4 ANGSTROMS RESOLUTION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE:;
COMPND   3 CHAIN: S;
COMPND   4 ENGINEERED: YES;
COMPND   5 MOL_ID: 2;
COMPND   6 MOLECULE:;
COMPND   7 CHAIN: L;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 MOL_ID: 2
KEYWDS    LYASE(CARBON-CARBON)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.KNIGHT,I.ANDERSSON,C.-I.BRANDEN
REVDAT   1   15-JUL-92 8RUB    0
JRNL        AUTH   S.KNIGHT,I.ANDERSSON,C.-I.BRANDEN
JRNL        TITL   CRYSTALLOGRAPHIC ANALYSIS OF RIBULOSE
JRNL        TITL 2 1,5-BISPHOSPHATE CARBOXYLASE FROM SPINACH AT 2.4
JRNL        TITL 3 ANGSTROMS RESOLUTION
JRNL        REF    J.MOL.BIOL.                   V. 215   113 1990
JRNL        REFN   ASTM JMOBAK  UK ISSN 0022-2836
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   S.KNIGHT,I.ANDERSSON,C.-I.BRANDEN
REMARK   1  TITL   REEXAMINATION OF THE THREE-DIMENSIONAL STRUCTURE
REMARK   1  TITL 2 OF THE SMALL SUBUNIT OF RUBISCO FROM HIGHER PLANTS
REMARK   1  REF    SCIENCE                       V. 244   702 1989
REMARK   1  REFN   ASTM SCIEAS  US ISSN 0036-8075
REMARK   1 REFERENCE 2
REMARK   1  AUTH   I.ANDERSSON,S.KNIGHT,G.SCHNEIDER,Y.LINDQVIST,
REMARK   1  AUTH 2 T.LUNDQVIST,C.-I.BRANDEN,G.H.LORIMER
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE ACTIVE SITE OF
REMARK   1  TITL 2 RIBULOSE-BISPHOSPHATE CARBOXYLASE
REMARK   1  REF    NATURE                        V. 337   229 1989
REMARK   1  REFN   ASTM NATUAS  UK ISSN 0028-0836
REMARK   2
REMARK   2 RESOLUTION. NULL ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : NULL
REMARK   3   AUTHORS     : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : NULL
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : NULL
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : NULL
REMARK   3   FREE R VALUE                     : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
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) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4666
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 25
REMARK   3   SOLVENT ATOMS            : 0
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) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL
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  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 8RUB COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK   5
REMARK   5 8RUB RESIDUE L 201 IS A MODIFIED ACTIVATOR LYSINE WHICH IS
REMARK   5 8RUB CARBAMYLATED AT THE EPSILON-AMINO GROUP. THE CARBAMYL
REMARK   5 8RUB ACTIVATOR GROUP IS PRESENTED AS HET GROUP *CBX* AT THE
REMARK   5 8RUB END OF CHAIN *L*. 8RUB
REMARK   6
REMARK   6 8RUB *SITE* RECORD *ACT* BELOW DESCRIBES THE CATALYTIC
REMARK   6 RESIDUES. 8RUB
REMARK   7
REMARK   7 8RUB NO ELECTRON DENSITY IS OBSERVED FOR THE FIRST NINE
REMARK   7 8RUB RESIDUES OF THE LARGE SUBUNIT. THE ELECTRON DENSITY
REMARK   7 FOR 8RUB RESIDUES SER L 10, VAL L 11, GLU L 12 AND PHE L 13
REMARK   7 IS WEAK. 8RUB
REMARK   8
REMARK   8 8RUB THE FOLLOWING DEVIATIONS FROM THE PUBLISHED SEQUENCE
REMARK   8 OF THE 8RUB SMALL SUBUNIT ARE FOUND: 8RUB CHEMICAL: PRO S
REMARK   8 6, PRO S 41, GLY S 77, PHE S 101, 8RUB THIS ENTRY: ILE S 6,
REMARK   8 CYS S 41, CYS S 77, ILE S 101, 8RUB CHEMICAL: ASN S 105 ASP
REMARK   8 S 106, GLU S 109 8RUB THIS ENTRY: ASP S 105 ASN S 106, GLN
REMARK   8 S 109 8RUB
REMARK   9
REMARK   9 8RUB THE SHEET PRESENTED AS *CT* ON SHEET RECORDS BELOW IS
REMARK   9 8RUB ACTUALLY AN EIGHT-STRANDED BETA-BARREL. THIS IS 8RUB
REMARK   9 REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST AND
REMARK   9 8RUB LAST STRANDS ARE IDENTICAL. 8RUB
REMARK  10
REMARK  10 8RUB THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT CONTAINS FOUR
REMARK  10 LARGE 8RUB AND FOUR SMALL SUBUNITS RELATED BY A FOUR-FOLD
REMARK  10 AXIS 8RUB THROUGH THE MOLECULAR CENTER AT X=0, Y=1/4, Z=1/
REMARK  10 4. THE 8RUB TRANSFORMATIONS GIVEN IN THE *MTRIX* RECORDS
REMARK  10 BELOW WILL 8RUB GENERATE AN L4S4 HALF-MOLECULE FROM THE
REMARK  10 COORDINATES IN 8RUB ENTRY TO GENERATE THE FULL L8S8
REMARK  10 MOLECULE FROM L4S4 THE 8RUB FOLLOWING TWO-FOLD ROTATION
REMARK  10 ABOUT THE CRYSTALLOGRAPHIC 8RUB TWOFOLD AXIS ALONG Y HAS TO
REMARK  10 BE APPLIED: 8RUB 8RUB -1.0 0.0 0.0 0.0 8RUB 0.0 1.0 0.0 +
REMARK  10 0.0 8RUB 0.0 0.0 -1.0 100.65 8RUB
REMARK  11
REMARK  11 8RUB CHAINS *A* ... *H* ARE AS DESCRIBED IN THE *JRNL*
REMARK  11 REFERENCE 8RUB CHAIN *S* IN THIS ENTRY CORRESPONDS TO CHAIN
REMARK  11 *S1* IN THE 8RUB *JRNL* REFERENCE AND CHAIN *L* IN THIS
REMARK  11 ENTRY CORRESPONDS TO 8RUB CHAIN *B* IN THE *JRNL*
REMARK  11 REFERENCE. 8RUB THE TRANSFORMATION PRESENTED IN MTRIX 1
REMARK  11 RECORDS GENERATES 8RUB THE LARGE SUBUNIT *D* AS DESCRIBED
REMARK  11 IN THE *JRNL* REFERENCE 8RUB ABOVE WHEN APPLIED TO CHAIN *
REMARK  11 B*. 8RUB THE TRANSFORMATION PRESENTED IN MTRIX 1 RECORDS
REMARK  11 GENERATES 8RUB THE SMALL SUBUNIT *S2* AS DESCRIBED IN THE *
REMARK  11 JRNL* REFERENCE 8RUB ABOVE WHEN APPLIED TO CHAIN *S*. 8RUB
REMARK  11 THE TRANSFORMATION PRESENTED IN MTRIX 2 RECORDS GENERATES
REMARK  11 8RUB THE LARGE SUBUNIT *F* AS DESCRIBED IN THE *JRNL*
REMARK  11 REFERENCE 8RUB ABOVE WHEN APPLIED TO CHAIN *B*. 8RUB THE
REMARK  11 TRANSFORMATION PRESENTED IN MTRIX 2 RECORDS GENERATES 8RUB
REMARK  11 THE SMALL SUBUNIT *S3* AS DESCRIBED IN THE *JRNL* REFERENCE
REMARK  11 8RUB ABOVE WHEN APPLIED TO CHAIN *S*. 8RUB THE
REMARK  11 TRANSFORMATION PRESENTED IN MTRIX 3 RECORDS GENERATES 8RUB
REMARK  11 THE LARGE SUBUNIT *H* AS DESCRIBED IN THE *JRNL* REFERENCE
REMARK  11 8RUB ABOVE WHEN APPLIED TO CHAIN *B*. 8RUB THE
REMARK  11 TRANSFORMATION PRESENTED IN MTRIX 3 RECORDS GENERATES 8RUB
REMARK  11 THE SMALL SUBUNIT *S4* AS DESCRIBED IN THE *JRNL* REFERENCE
REMARK  11 8RUB ABOVE WHEN APPLIED TO CHAIN *S*. 8RUB
REMARK  12
REMARK  12 8RUB IN THE CATALYTICALLY COMPETENT MOLECULE, DIMERS OF THE
REMARK  12 LARG 8RUB SUBUNITS FORM FUNCTIONAL UNITS. IN THE *JRNL*
REMARK  12 REFERENCE 8RUB THESE DIMERS ARE DESIGNATED *AB*, *CD*, *EF*
REMARK  12 AND *GH*. 8RUB
REMARK  13
REMARK  13 8RUB THESE DIMERS CAN BE GENERATED BY APPLICATION OF THE
REMARK  13 8RUB *MTRIX* TRANSFORMATIONS TO THE COORDINATES FOR THE *L*
REMARK  13 8RUB CHAIN, FOLLOWED BY THE CRYSTALLOGRAPHIC TWO-FOLD
REMARK  13 ROTATION 8RUB DESCRIBED IN REMARK 10. 8RUB
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : NULL
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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,1/2+Z
REMARK 290       3555   -X,Y,1/2-Z
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   1/2+X,1/2+Y,Z
REMARK 290       6555   1/2-X,1/2-Y,1/2+Z
REMARK 290       7555   1/2-X,1/2+Y,1/2-Z
REMARK 290       8555   1/2+X,1/2-Y,-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      100.65000
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      100.65000
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       78.60000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       78.60000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       78.60000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       78.60000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      100.65000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       78.60000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       78.60000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      100.65000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       78.60000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       78.60000
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 APPLY THE FOLLOWING TO CHAINS: S, L
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 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 L     1
REMARK 465     SER L     2
REMARK 465     PRO L     3
REMARK 465     GLN L     4
REMARK 465     THR L     5
REMARK 465     GLU L     6
REMARK 465     THR L     7
REMARK 465     LYS L     8
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     GLU L  12    CB    CG    CD    OE1   OE2
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
REMARK 500   NZ   LYS L   201     C    CBX L   201              1.31
REMARK 500   NZ   LYS L   201     O2   CBX L   201              2.17
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    PHE S  12   CA  -  C   -  N   ANGL. DEV. = 20.9 DEGREES
REMARK 500    LYS L 356   CB  -  CG  -  CD  ANGL. DEV. =-21.8 DEGREES
REMARK 500    ARG L 358   CB  -  CG  -  CD  ANGL. DEV. = 24.0 DEGREES
REMARK 500    ARG L 358   CG  -  CD  -  NE  ANGL. DEV. =-29.3 DEGREES
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  M RES CSSEQI        PSI       PHI
REMARK 500    LYS S  71     -117.68     52.81
SEQRES   1 S  123  MET GLN VAL TRP PRO ILE LEU GLY LEU LYS LYS PHE GLU
SEQRES   2 S  123  THR LEU SER TYR LEU PRO PRO LEU THR THR GLU GLN LEU
SEQRES   3 S  123  LEU ALA GLU VAL ASN TYR LEU LEU VAL LYS GLY TRP ILE
SEQRES   4 S  123  PRO CYS LEU GLU PHE GLU VAL LYS ASP GLY PHE VAL TYR
SEQRES   5 S  123  ARG GLU HIS ASP LYS 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 VAL ASN GLU VAL GLU GLU VAL LYS
SEQRES   8 S  123  LYS ALA TYR PRO ASP ALA PHE VAL ARG ILE ILE GLY PHE
SEQRES   9 S  123  ASP ASN LYS ARG GLN VAL GLN CYS ILE SER PHE ILE ALA
SEQRES  10 S  123  TYR LYS PRO ALA GLY TYR
SEQRES   1 L  475  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLU PHE
SEQRES   2 L  475  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR
SEQRES   3 L  475  PRO GLU TYR GLU THR LEU ASP THR ASP ILE LEU ALA ALA
SEQRES   4 L  475  PHE ARG VAL SER PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 L  475  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 L  475  TRP THR THR VAL TRP THR ASP GLY LEU THR ASN LEU ASP
SEQRES   7 L  475  ARG TYR LYS GLY ARG CYS TYR HIS ILE GLU PRO VAL ALA
SEQRES   8 L  475  GLY GLU GLU ASN GLN TYR ILE CYS TYR VAL ALA TYR PRO
SEQRES   9 L  475  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 L  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 L  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO VAL ALA
SEQRES  12 L  475  TYR VAL LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 L  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU
SEQRES  14 L  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 L  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 L  475  GLY LEU ASP PHE THR LYS ASP ASP GLU ASN VAL ASN SER
SEQRES  17 L  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE CYS
SEQRES  18 L  475  ALA GLU ALA LEU TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 L  475  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 L  475  GLU ASP MET MET LYS ARG ALA VAL PHE ALA ARG GLU LEU
SEQRES  21 L  475  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 L  475  PHE THR ALA ASN THR THR LEU SER HIS TYR CYS ARG ASP
SEQRES  23 L  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 L  475  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG
SEQRES  25 L  475  VAL LEU ALA LYS ALA LEU ARG LEU SER GLY GLY ASP HIS
SEQRES  26 L  475  ILE HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 L  475  ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG ASP
SEQRES  28 L  475  ASP TYR THR GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 L  475  THR GLN SER TRP VAL SER THR PRO GLY VAL LEU PRO VAL
SEQRES  30 L  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 L  475  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY
SEQRES  32 L  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 L  475  ALA VAL ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN
SEQRES  34 L  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN
SEQRES  35 L  475  THR ILE ILE ARG GLU ALA THR LYS TRP SER PRO GLU LEU
SEQRES  36 L  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 L  475  PHE PRO ALA MET ASP THR VAL
FTNOTE   1 PROLINE L 176 IS A CIS PROLINE.
FTNOTE   2 LYS L 201 IS CARBAMYLATED AT THE NZ POSITION.
FTNOTE   3 THE ELECTRON DENSITY MAP DOES NOT ALLOW ONE TO DEDUCE IF
FTNOTE   3  THE C3 HYDROXYL GROUP OF CAP IS CIS OR TRANS TO THE C2
FTNOTE   3  HYDROXYL GROUP. IN THIS ENTRY C3 HYDROXYL GROUP IS TRANS
FTNOTE   3  WITH RESPECT TO THE C2 HYDROXYL GROUP.
HET     MG  L 476       1
HET    CBX  L 201       3
HET    CAP      1      21
HETNAM      MG MAGNESIUM ION
HETNAM     CBX CARBOXY GROUP
HETNAM     CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE
FORMUL   3   MG    MG 2+
FORMUL   4  CBX    C H2 O2
FORMUL   5  CAP    C6 H14 O13 P2
HELIX    1   A THR S   23  VAL S   35  1SMALL SUBUNIT                     13
HELIX    2   B PRO S   80  ALA S   93  1SMALL SUBUNIT                     14
HELIX    3   B PRO L   50  GLU L   60  1LARGE SUBUNIT,N-TERM DOMAIN       11
HELIX    4   C VAL L  113  VAL L  121  1LARGE SUBUNIT,N-TERM DOMAIN        9
HELIX    5   D VAL L  142  VAL L  145  1LARGE SUBUNIT,N-TERM DOMAIN        4
HELIX    6   E ILE L  155  LEU L  162  1LARGE SUBUNIT,C-TERM DOMAIN        8
HELIX    7   1 ALA L  182  ARG L  194  1LARGE SUBUNIT,C-TERM DOMAIN       13
HELIX    8   2 TRP L  214  THR L  232  1LARGE SUBUNIT,C-TERM DOMAIN       19
HELIX    9   3 CYS L  247  LEU L  260  1LARGE SUBUNIT,C-TERM DOMAIN       14
HELIX   10   4 PHE L  274  ASN L  287  1LARGE SUBUNIT,C-TERM DOMAIN       14
HELIX   11   F HIS L  298  ASP L  302  1LARGE SUBUNIT,C-TERM DOMAIN        5
HELIX   12   5 PHE L  311  SER L  321  1LARGE SUBUNIT,C-TERM DOMAIN       11
HELIX   13   6 ARG L  339  ARG L  350  1LARGE SUBUNIT,C-TERM DOMAIN       12
HELIX   14   7 MET L  387  PHE L  394  1LARGE SUBUNIT,C-TERM DOMAIN        8
HELIX   15   P GLY L  404  LEU L  407  1LARGE SUBUNIT,C-TERM DOMAIN        4
HELIX   16   8 ASN L  413  ASN L  432  1LARGE SUBUNIT,C-TERM DOMAIN       20
HELIX   17   G LEU L  437  TRP L  451  1LARGE SUBUNIT,C-TERM DOMAIN       15
HELIX   18   H PRO L  453  TRP L  462  1LARGE SUBUNIT,C-TERM DOMAIN       10
SHEET    1  NT 5 TYR L  24  THR L  26  0
SHEET    2  NT 5 ARG L  83  PRO L  89  1
SHEET    3  NT 5 TYR L  97  TYR L 103 -1
SHEET    4  NT 5 ILE L  36  PRO L  44 -1
SHEET    5  NT 5 LEU L 130  ARG L 139 -1
SHEET    1  CT 9 LEU L 169  GLY L 171  0
SHEET    2  CT 9 PHE L 199  LYS L 201  1
SHEET    3  CT 9 GLY L 237  ASN L 241  1
SHEET    4  CT 9 ILE L 264  ASP L 268  1
SHEET    5  CT 9 LEU L 290  HIS L 294  1
SHEET    6  CT 9 HIS L 325  HIS L 327  1
SHEET    7  CT 9 LEU L 375  SER L 379  1
SHEET    8  CT 9 VAL L 399  GLN L 401  1
SHEET    9  CT 9 LEU L 169  GLY L 171  1
SHEET    1   S 4 THR S  68  MET S  74  0
SHEET    2   S 4 LEU S  34  GLU S  45 -1
SHEET    3   S 4 PHE S  98  ASP S 105 -1
SHEET    4   S 4 VAL S 110  TYR S 118 -1
CISPEP   1 LYS L  175    PRO L  176          0         2.15
SITE     1 ACT  5 CBX L 201  LYS L 201  ASP L 203  GLU L 204
SITE     2 ACT  5  MG L 476
CRYST1  157.200  157.200  201.300  90.00  90.00  90.00 C 2 2 21      4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.006361  0.000000  0.000000        0.00000
SCALE2      0.000000  0.006361  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004968        0.00000
MTRIX1   1  0.000987  0.999507 -0.031395      -37.70065
MTRIX2   1 -0.999507  0.000000 -0.031411       40.88076
MTRIX3   1 -0.031395  0.031411  0.999013       -1.18479
MTRIX1   2 -0.998027  0.000000 -0.062790        3.15992
MTRIX2   2  0.000000 -1.000000  0.000000       78.60000
MTRIX3   2 -0.062790  0.000000  0.998027        0.09930
MTRIX1   3  0.000987 -0.999507 -0.031395       40.86057
MTRIX2   3  0.999507  0.000000  0.031411       37.71924
MTRIX3   3 -0.031395 -0.031411  0.999013        1.28409
      
PROCHECK
Go to PROCHECK summary
 References