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PDBsum entry 1bur

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
1bur
Jmol
Contents
Protein chains
464 a.a.
123 a.a.
Ligands
CAP ×4
Metals
_MG ×4
Waters ×1875
HEADER    LYASE                                   09-APR-96   1BUR
OBSLTE     13-MAR-02 1BUR      1IR1
TITLE     RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE COMPLEXED
TITLE    2 WITH CARBON DIOXIDE, MG2+ AND 2-CARBOXYARABINITOL-1,5-
TITLE    3 BISPHOSPHATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 SYNONYM: RUBISCO;
COMPND   5 EC: 4.1.1.39;
COMPND   6 OTHER_DETAILS: PURIFIED BY POLYETHYLENE GLYCOL;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE;
COMPND   9 CHAIN: S, U;
COMPND  10 SYNONYM: RUBISCO;
COMPND  11 EC: 4.1.1.39;
COMPND  12 OTHER_DETAILS: PURIFIED BY POLYETHYLENE GLYCOL;
COMPND  13 MOL_ID: 3;
COMPND  14 MOLECULE: RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE;
COMPND  15 CHAIN: T, V;
COMPND  16 SYNONYM: RUBISCO;
COMPND  17 EC: 4.1.1.39;
COMPND  18 OTHER_DETAILS: PURIFIED BY POLYETHYLENE GLYCOL
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SPINACIA OLERACEA;
SOURCE   3 ORGANISM_COMMON: SPINACH;
SOURCE   4 ORGAN: LEAF;
SOURCE   5 ORGANELLE: CHLOROPLAST;
SOURCE   6 MOL_ID: 2;
SOURCE   7 ORGANISM_SCIENTIFIC: SPINACIA OLERACEA;
SOURCE   8 ORGANISM_COMMON: SPINACH;
SOURCE   9 ORGAN: LEAF;
SOURCE  10 ORGANELLE: CHLOROPLAST;
SOURCE  11 MOL_ID: 3;
SOURCE  12 ORGANISM_SCIENTIFIC: SPINACIA OLERACEA;
SOURCE  13 ORGANISM_COMMON: SPINACH;
SOURCE  14 ORGAN: LEAF;
SOURCE  15 ORGANELLE: CHLOROPLAST
KEYWDS    CARBON DIOXIDE FIXING ENZYME, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    N.SHIBATA,T.INOUE,K.FUKUHARA,Y.NAGARA,R.KITAGAWA,S.HARADA,
AUTHOR   2 N.KASAI,K.UEMURA,K.KATO,A.YOKOTA,Y.KAI
REVDAT   1   11-JAN-97 1BUR    0
JRNL        AUTH   N.SHIBATA,T.INOUE,K.FUKUHARA,Y.NAGARA,R.KITAGAWA,
JRNL        AUTH 2 S.HARADA,N.KASAI,K.UEMURA,K.KATO,A.YOKOTA,Y.KAI
JRNL        TITL   ORDERLY DISPOSITION OF HETEROGENEOUS SMALL
JRNL        TITL 2 SUBUNITS IN D-RIBULOSE-1,5-BISPHOSPHATE
JRNL        TITL 3 CARBOXYLASE/OXYGENASE FROM SPINACH.
JRNL        REF    J.BIOL.CHEM.                  V. 271 26449 1996
JRNL        REFN   ASTM JBCHA3  US ISSN 0021-9258
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   S.KNIGHT,I.ANDERSSON,C.I.BRANDEN
REMARK   1  TITL   CRYSTALLOGRAPHIC ANALYSIS OF RIBULOSE
REMARK   1  TITL 2 1,5-BISPHOSPHATE CARBOXYLASE FROM SPINACH AT 2.4 A
REMARK   1  TITL 3 RESOLUTION. SUBUNIT INTERACTIONS AND ACTIVE SITE
REMARK   1  REF    J.MOL.BIOL.                   V. 215   113 1990
REMARK   1  REFN   ASTM JMOBAK  UK ISSN 0022-2836
REMARK   1 REFERENCE 2
REMARK   1  AUTH   S.KNIGHT,I.ANDERSSON,C.-I.BRANDEN
REMARK   1  TITL   LARGE SINGLE CRYSTALS OF SPINACH 1,5-BISPHOSPHATE
REMARK   1  TITL 2 CARBOXYLASE/OXYGENASE SUITABLE FOR X-RAY STUDIES
REMARK   1  REF    J.MOL.BIOL.                   V. 172   363 1984
REMARK   1  REFN   ASTM JMOBAK  UK ISSN 0022-2836
REMARK   2
REMARK   2 RESOLUTION. 1.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.0
REMARK   3   AUTHORS     : BRUNGER
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)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 73.6
REMARK   3   NUMBER OF REFLECTIONS             : 175568
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) : 0.159
REMARK   3   FREE R VALUE                     : 0.188
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            : 18632
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 88
REMARK   3   SOLVENT ATOMS            : 1875
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.19
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) : 0.20
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) : 0.010
REMARK   3   BOND ANGLES            (DEGREES) : 2.38
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.02
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.92
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 1BUR COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006
REMARK   4
REMARK   4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY.
REMARK   4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-19)
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 17-MAR-1994
REMARK 200  TEMPERATURE           (KELVIN) : 293.0
REMARK 200  PH                             : 7.90
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-2A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : SAKABE CAMERA
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : WEIS
REMARK 200  DATA SCALING SOFTWARE          : PROTEIN
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 216085
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 66.9
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.08700
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 2.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.65
REMARK 200  COMPLETENESS FOR SHELL     (%) : 30.5
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.0
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 46.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.9
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      100.45000
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 8 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: 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    81   LIES ON A SPECIAL POSITION.
REMARK 375      HOH    95   LIES ON A SPECIAL POSITION.
REMARK 375      HOH   106   LIES ON A SPECIAL POSITION.
REMARK 375      HOH   169   LIES ON A SPECIAL POSITION.
REMARK 375      HOH  1125   LIES ON A SPECIAL POSITION.
REMARK 375      HOH  1175   LIES ON A SPECIAL POSITION.
REMARK 375      HOH  1166   LIES ON A SPECIAL POSITION.
REMARK 375      HOH  1891   LIES ON A SPECIAL POSITION.
REMARK 375      HOH  1833   LIES ON A SPECIAL POSITION.
REMARK 375      HOH  1835   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 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 A  12    CB    CG    CD    OE1   OE2
REMARK 470     GLU B  12    CB    CG    CD    OE1   OE2
REMARK 470     GLU C  12    CB    CG    CD    OE1   OE2
REMARK 470     GLU D  12    CB    CG    CD    OE1   OE2
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    1075     O    HOH    1896     3555     2.06
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    ILE A 445   CB    ILE A 445   CG1   -0.098
REMARK 500    ILE S  39   CA    ILE S  39   CB     0.089
REMARK 500    VAL S  83   CA    VAL S  83   CB     0.096
REMARK 500    ILE B 301   CA    ILE B 301   CB     0.083
REMARK 500    VAL B 475   CA    VAL B 475   CB     0.105
REMARK 500    ILE T  39   CA    ILE T  39   CB     0.090
REMARK 500    ILE U  39   CA    ILE U  39   CB     0.085
REMARK 500    HIS D 238   NE2   HIS D 238   CD2   -0.085
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    ILE A 445   CB  -  CG1 -  CD1 ANGL. DEV. =-15.7 DEGREES
REMARK 500    ILE S  39   CB  -  CG1 -  CD1 ANGL. DEV. =-13.6 DEGREES
REMARK 500    LEU B 225   CA  -  CB  -  CG  ANGL. DEV. = 16.8 DEGREES
REMARK 500    ARG C 285   CA  -  CB  -  CG  ANGL. DEV. =-15.4 DEGREES
REMARK 500    LEU U  33   CA  -  CB  -  CG  ANGL. DEV. = 15.3 DEGREES
REMARK 500    MET D 297   CA  -  CB  -  CG  ANGL. DEV. = 14.4 DEGREES
REMARK 500    THR D 474   N   -  CA  -  C   ANGL. DEV. = 13.4 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    VAL A 331      -51.78     73.76
REMARK 500    VAL B 331      -51.63     72.48
REMARK 500    VAL C 331      -51.74     71.88
REMARK 500    LYS U  71     -118.69     51.27
REMARK 500    VAL D 331      -52.05     73.30
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 GLU B   12    PHE B   13                  144.49
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACA
REMARK 800 SITE_DESCRIPTION: THE ACTIVE SITE.
REMARK 800 SITE_IDENTIFIER: ACB
REMARK 800 SITE_DESCRIPTION: THE ACTIVE SITE.
REMARK 800 SITE_IDENTIFIER: ACC
REMARK 800 SITE_DESCRIPTION: THE ACTIVE SITE.
REMARK 800 SITE_IDENTIFIER: ACD
REMARK 800 SITE_DESCRIPTION: THE ACTIVE SITE.
DBREF  1BUR A    1   475  UNP    P00875   RBL_SPIOL        1    475
DBREF  1BUR S    1   123  UNP    P00870   RBS1_SPIOL       1    123
DBREF  1BUR B    1   475  UNP    P00875   RBL_SPIOL        1    475
DBREF  1BUR T    1   123  UNP    P00870   RBS1_SPIOL       1    123
DBREF  1BUR C    1   475  UNP    P00875   RBL_SPIOL        1    475
DBREF  1BUR U    1   123  UNP    P00870   RBS1_SPIOL       1    123
DBREF  1BUR D    1   475  UNP    P00875   RBL_SPIOL        1    475
DBREF  1BUR V    1   123  UNP    P00870   RBS1_SPIOL       1    123
SEQADV 1BUR KCX A  201  UNP  P00875    LYS   201 CONFLICT
SEQADV 1BUR ILE S    6  UNP  P00870    PRO     6 CONFLICT
SEQADV 1BUR MET S    9  UNP  P00870    LEU     9 SEE REMARK 999
SEQADV 1BUR TYR S   12  UNP  P00870    PHE    12 SEE REMARK 999
SEQADV 1BUR ASN S   36  UNP  P00870    LYS    36 SEE REMARK 999
SEQADV 1BUR ASN S   37  UNP  P00870    GLY    37 SEE REMARK 999
SEQADV 1BUR CYS S   41  UNP  P00870    PRO    41 CONFLICT
SEQADV 1BUR LEU S   56  UNP  P00870    ASP    56 SEE REMARK 999
SEQADV 1BUR CYS S   77  UNP  P00870    GLY    77 CONFLICT
SEQADV 1BUR LEU S   84  UNP  P00870    VAL    84 SEE REMARK 999
SEQADV 1BUR LEU S   87  UNP  P00870    VAL    87 SEE REMARK 999
SEQADV 1BUR CYS S   90  UNP  P00870    VAL    90 SEE REMARK 999
SEQADV 1BUR TYR S   94  UNP  P00870    PRO    94 CONFLICT
SEQADV 1BUR ILE S   99  UNP  P00870    VAL    99 SEE REMARK 999
SEQADV 1BUR ILE S  101  UNP  P00870    PHE   101 CONFLICT
SEQADV 1BUR ASP S  105  UNP  P00870    ASN   105 CONFLICT
SEQADV 1BUR ASN S  106  UNP  P00870    ASP   106 CONFLICT
SEQADV 1BUR GLN S  109  UNP  P00870    GLU   109 CONFLICT
SEQADV 1BUR KCX B  201  UNP  P00875    LYS   201 CONFLICT
SEQADV 1BUR ILE T    6  UNP  P00870    PRO     6 CONFLICT
SEQADV 1BUR MET T    9  UNP  P00870    LEU     9 SEE REMARK 999
SEQADV 1BUR TYR T   12  UNP  P00870    PHE    12 SEE REMARK 999
SEQADV 1BUR ASN T   36  UNP  P00870    LYS    36 SEE REMARK 999
SEQADV 1BUR ASN T   37  UNP  P00870    GLY    37 SEE REMARK 999
SEQADV 1BUR CYS T   41  UNP  P00870    PRO    41 CONFLICT
SEQADV 1BUR HIS T   56  UNP  P00870    ASP    56 SEE REMARK 999
SEQADV 1BUR CYS T   77  UNP  P00870    GLY    77 CONFLICT
SEQADV 1BUR LEU T   84  UNP  P00870    VAL    84 SEE REMARK 999
SEQADV 1BUR LEU T   87  UNP  P00870    VAL    87 SEE REMARK 999
SEQADV 1BUR CYS T   90  UNP  P00870    VAL    90 SEE REMARK 999
SEQADV 1BUR TYR T   94  UNP  P00870    PRO    94 CONFLICT
SEQADV 1BUR ILE T   99  UNP  P00870    VAL    99 SEE REMARK 999
SEQADV 1BUR ILE T  101  UNP  P00870    PHE   101 CONFLICT
SEQADV 1BUR ASP T  105  UNP  P00870    ASN   105 CONFLICT
SEQADV 1BUR ASN T  106  UNP  P00870    ASP   106 CONFLICT
SEQADV 1BUR GLN T  109  UNP  P00870    GLU   109 CONFLICT
SEQADV 1BUR KCX C  201  UNP  P00875    LYS   201 CONFLICT
SEQADV 1BUR ILE U    6  UNP  P00870    PRO     6 CONFLICT
SEQADV 1BUR MET U    9  UNP  P00870    LEU     9 SEE REMARK 999
SEQADV 1BUR TYR U   12  UNP  P00870    PHE    12 SEE REMARK 999
SEQADV 1BUR ASN U   36  UNP  P00870    LYS    36 SEE REMARK 999
SEQADV 1BUR ASN U   37  UNP  P00870    GLY    37 SEE REMARK 999
SEQADV 1BUR CYS U   41  UNP  P00870    PRO    41 CONFLICT
SEQADV 1BUR LEU U   56  UNP  P00870    ASP    56 SEE REMARK 999
SEQADV 1BUR CYS U   77  UNP  P00870    GLY    77 CONFLICT
SEQADV 1BUR LEU U   84  UNP  P00870    VAL    84 SEE REMARK 999
SEQADV 1BUR LEU U   87  UNP  P00870    VAL    87 SEE REMARK 999
SEQADV 1BUR CYS U   90  UNP  P00870    VAL    90 SEE REMARK 999
SEQADV 1BUR TYR U   94  UNP  P00870    PRO    94 CONFLICT
SEQADV 1BUR ILE U   99  UNP  P00870    VAL    99 SEE REMARK 999
SEQADV 1BUR ILE U  101  UNP  P00870    PHE   101 CONFLICT
SEQADV 1BUR ASP U  105  UNP  P00870    ASN   105 CONFLICT
SEQADV 1BUR ASN U  106  UNP  P00870    ASP   106 CONFLICT
SEQADV 1BUR GLN U  109  UNP  P00870    GLU   109 CONFLICT
SEQADV 1BUR KCX D  201  UNP  P00875    LYS   201 CONFLICT
SEQADV 1BUR ILE V    6  UNP  P00870    PRO     6 CONFLICT
SEQADV 1BUR MET V    9  UNP  P00870    LEU     9 SEE REMARK 999
SEQADV 1BUR TYR V   12  UNP  P00870    PHE    12 SEE REMARK 999
SEQADV 1BUR ASN V   36  UNP  P00870    LYS    36 SEE REMARK 999
SEQADV 1BUR ASN V   37  UNP  P00870    GLY    37 SEE REMARK 999
SEQADV 1BUR CYS V   41  UNP  P00870    PRO    41 CONFLICT
SEQADV 1BUR HIS V   56  UNP  P00870    ASP    56 SEE REMARK 999
SEQADV 1BUR CYS V   77  UNP  P00870    GLY    77 CONFLICT
SEQADV 1BUR LEU V   84  UNP  P00870    VAL    84 SEE REMARK 999
SEQADV 1BUR LEU V   87  UNP  P00870    VAL    87 SEE REMARK 999
SEQADV 1BUR CYS V   90  UNP  P00870    VAL    90 SEE REMARK 999
SEQADV 1BUR TYR V   94  UNP  P00870    PRO    94 CONFLICT
SEQADV 1BUR ILE V   99  UNP  P00870    VAL    99 SEE REMARK 999
SEQADV 1BUR ILE V  101  UNP  P00870    PHE   101 CONFLICT
SEQADV 1BUR ASP V  105  UNP  P00870    ASN   105 CONFLICT
SEQADV 1BUR ASN V  106  UNP  P00870    ASP   106 CONFLICT
SEQADV 1BUR GLN V  109  UNP  P00870    GLU   109 CONFLICT
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  MET GLN VAL TRP PRO ILE LEU GLY MET LYS LYS TYR 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 ASN ASN 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 LEU 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 LEU ASN GLU LEU GLU GLU CYS LYS
SEQRES   8 S  123  LYS ALA TYR PRO ASP ALA PHE ILE 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 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  MET GLN VAL TRP PRO ILE LEU GLY MET LYS LYS TYR GLU
SEQRES   2 T  123  THR LEU SER TYR LEU PRO PRO LEU THR THR GLU GLN LEU
SEQRES   3 T  123  LEU ALA GLU VAL ASN TYR LEU LEU VAL ASN ASN TRP ILE
SEQRES   4 T  123  PRO CYS LEU GLU PHE GLU VAL LYS ASP GLY PHE VAL TYR
SEQRES   5 T  123  ARG GLU HIS HIS LYS 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 ALA TYR PRO ASP ALA PHE ILE ARG ILE ILE GLY PHE
SEQRES   9 T  123  ASP ASN LYS ARG GLN VAL GLN CYS ILE 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  MET GLN VAL TRP PRO ILE LEU GLY MET LYS LYS TYR GLU
SEQRES   2 U  123  THR LEU SER TYR LEU PRO PRO LEU THR THR GLU GLN LEU
SEQRES   3 U  123  LEU ALA GLU VAL ASN TYR LEU LEU VAL ASN ASN TRP ILE
SEQRES   4 U  123  PRO CYS LEU GLU PHE GLU VAL LYS ASP GLY PHE VAL TYR
SEQRES   5 U  123  ARG GLU HIS LEU LYS 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 ALA TYR PRO ASP ALA PHE ILE ARG ILE ILE GLY PHE
SEQRES   9 U  123  ASP ASN LYS ARG GLN VAL GLN CYS ILE 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  MET GLN VAL TRP PRO ILE LEU GLY MET LYS LYS TYR GLU
SEQRES   2 V  123  THR LEU SER TYR LEU PRO PRO LEU THR THR GLU GLN LEU
SEQRES   3 V  123  LEU ALA GLU VAL ASN TYR LEU LEU VAL ASN ASN TRP ILE
SEQRES   4 V  123  PRO CYS LEU GLU PHE GLU VAL LYS ASP GLY PHE VAL TYR
SEQRES   5 V  123  ARG GLU HIS HIS LYS 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 ALA TYR PRO ASP ALA PHE ILE ARG ILE ILE GLY PHE
SEQRES   9 V  123  ASP ASN LYS ARG GLN VAL GLN CYS ILE SER PHE ILE ALA
SEQRES  10 V  123  TYR LYS PRO ALA GLY TYR
MODRES 1BUR KCX A  201  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 1BUR KCX B  201  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 1BUR KCX C  201  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 1BUR KCX D  201  LYS  LYSINE NZ-CARBOXYLIC ACID
HET    KCX  A 201      12
HET    KCX  B 201      12
HET    KCX  C 201      12
HET    KCX  D 201      12
HET     MG  A 476       1
HET     MG  B 476       1
HET     MG  C 476       1
HET     MG  D 476       1
HET    CAP  A   1      26
HET    CAP  B   1      26
HET    CAP  C   1      26
HET    CAP  D   1      26
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID
HETNAM      MG MAGNESIUM ION
HETNAM     CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE
FORMUL   1  KCX    4(C7 H14 N2 O4)
FORMUL   9   MG    4(MG 2+)
FORMUL  13  CAP    4(C6 H14 O13 P2)
FORMUL  17  HOH   *1875(H2 O)
HELIX    1   1 TYR A   20  TYR A   24  5                                   5
HELIX    2   2 PRO A   50  GLU A   60  1                                  11
HELIX    3   3 TRP A   70  LEU A   74  5                                   5
HELIX    4   4 LEU A   77  TYR A   80  1                                   4
HELIX    5   5 LEU A  105  LEU A  107  5                                   3
HELIX    6   6 VAL A  113  ILE A  120  1                                   8
HELIX    7   7 VAL A  124  GLY A  126  5                                   3
HELIX    8   8 VAL A  142  THR A  147  1                                   6
HELIX    9   9 ILE A  155  LEU A  162  1                                   8
HELIX   10  10 ALA A  182  GLY A  195  1                                  14
HELIX   11  11 TRP A  214  THR A  232  1                                  19
HELIX   12  12 CYS A  247  LEU A  260  1                                  14
HELIX   13  13 TYR A  269  GLY A  272  1                                   4
HELIX   14  14 PHE A  274  ASN A  287  1                                  14
HELIX   15  15 HIS A  298  ASP A  302  1                                   5
HELIX   16  16 PHE A  311  SER A  321  1                                  11
HELIX   17  17 ARG A  339  ARG A  350  1                                  12
HELIX   18  18 ARG A  358  ARG A  360  5                                   3
HELIX   19  19 VAL A  384  PHE A  394  5                                  11
HELIX   20  20 GLY A  404  LEU A  407  1                                   4
HELIX   21  21 ASN A  413  GLU A  433  1                                  21
HELIX   22  22 LEU A  437  LYS A  450  1                                  14
HELIX   23  23 PRO A  453  TRP A  462  1                                  10
HELIX   24  24 THR S   23  VAL S   35  1                                  13
HELIX   25  25 PRO S   80  ALA S   93  1                                  14
HELIX   26  26 TYR B   20  TYR B   24  5                                   5
HELIX   27  27 PRO B   50  GLU B   60  1                                  11
HELIX   28  28 TRP B   70  LEU B   74  5                                   5
HELIX   29  29 LEU B   77  TYR B   80  1                                   4
HELIX   30  30 LEU B  105  LEU B  107  5                                   3
HELIX   31  31 VAL B  113  ILE B  120  1                                   8
HELIX   32  32 VAL B  124  GLY B  126  5                                   3
HELIX   33  33 VAL B  142  THR B  147  1                                   6
HELIX   34  34 ILE B  155  LEU B  162  1                                   8
HELIX   35  35 ALA B  182  GLY B  195  1                                  14
HELIX   36  36 TRP B  214  THR B  232  1                                  19
HELIX   37  37 CYS B  247  LEU B  260  1                                  14
HELIX   38  38 TYR B  269  GLY B  272  1                                   4
HELIX   39  39 PHE B  274  ASN B  287  1                                  14
HELIX   40  40 HIS B  298  ASP B  302  1                                   5
HELIX   41  41 PHE B  311  SER B  321  1                                  11
HELIX   42  42 ARG B  339  ARG B  350  1                                  12
HELIX   43  43 ARG B  358  ARG B  360  5                                   3
HELIX   44  44 VAL B  384  PHE B  394  5                                  11
HELIX   45  45 GLY B  404  LEU B  407  1                                   4
HELIX   46  46 ASN B  413  GLU B  433  1                                  21
HELIX   47  47 LEU B  437  LYS B  450  1                                  14
HELIX   48  48 PRO B  453  TRP B  462  1                                  10
HELIX   49  49 THR T   23  VAL T   35  1                                  13
HELIX   50  50 PRO T   80  ALA T   93  1                                  14
HELIX   51  51 TYR C   20  TYR C   24  5                                   5
HELIX   52  52 PRO C   50  GLU C   60  1                                  11
HELIX   53  53 TRP C   70  LEU C   74  5                                   5
HELIX   54  54 LEU C   77  TYR C   80  1                                   4
HELIX   55  55 LEU C  105  LEU C  107  5                                   3
HELIX   56  56 VAL C  113  ILE C  120  1                                   8
HELIX   57  57 VAL C  124  GLY C  126  5                                   3
HELIX   58  58 VAL C  142  THR C  147  1                                   6
HELIX   59  59 ILE C  155  LEU C  162  1                                   8
HELIX   60  60 ALA C  182  GLY C  195  1                                  14
HELIX   61  61 TRP C  214  THR C  232  1                                  19
HELIX   62  62 CYS C  247  LEU C  260  1                                  14
HELIX   63  63 TYR C  269  GLY C  272  1                                   4
HELIX   64  64 PHE C  274  ASN C  287  1                                  14
HELIX   65  65 HIS C  298  ASP C  302  1                                   5
HELIX   66  66 PHE C  311  SER C  321  1                                  11
HELIX   67  67 ARG C  339  ARG C  350  1                                  12
HELIX   68  68 ARG C  358  ARG C  360  5                                   3
HELIX   69  69 VAL C  384  PHE C  394  5                                  11
HELIX   70  70 GLY C  404  LEU C  407  1                                   4
HELIX   71  71 ASN C  413  GLU C  433  1                                  21
HELIX   72  72 LEU C  437  LYS C  450  1                                  14
HELIX   73  73 PRO C  453  TRP C  462  1                                  10
HELIX   74  74 THR U   23  VAL U   35  1                                  13
HELIX   75  75 PRO U   80  ALA U   93  1                                  14
HELIX   76  76 TYR D   20  TYR D   24  5                                   5
HELIX   77  77 PRO D   50  GLU D   60  1                                  11
HELIX   78  78 TRP D   70  LEU D   74  5                                   5
HELIX   79  79 LEU D   77  TYR D   80  1                                   4
HELIX   80  80 LEU D  105  LEU D  107  5                                   3
HELIX   81  81 VAL D  113  ILE D  120  1                                   8
HELIX   82  82 VAL D  124  GLY D  126  5                                   3
HELIX   83  83 VAL D  142  THR D  147  1                                   6
HELIX   84  84 ILE D  155  LEU D  162  1                                   8
HELIX   85  85 ALA D  182  GLY D  195  1                                  14
HELIX   86  86 TRP D  214  THR D  232  1                                  19
HELIX   87  87 CYS D  247  LEU D  260  1                                  14
HELIX   88  88 TYR D  269  GLY D  272  1                                   4
HELIX   89  89 PHE D  274  ASN D  287  1                                  14
HELIX   90  90 HIS D  298  ASP D  302  1                                   5
HELIX   91  91 PHE D  311  SER D  321  1                                  11
HELIX   92  92 ARG D  339  ARG D  350  1                                  12
HELIX   93  93 ARG D  358  ARG D  360  5                                   3
HELIX   94  94 VAL D  384  PHE D  394  5                                  11
HELIX   95  95 GLY D  404  LEU D  407  1                                   4
HELIX   96  96 ASN D  413  ASN D  432  1                                  20
HELIX   97  97 LEU D  437  LYS D  450  1                                  14
HELIX   98  98 PRO D  453  TRP D  462  1                                  10
HELIX   99  99 THR V   23  VAL V   35  1                                  13
HELIX  100 100 PRO V   80  ALA V   93  1                                  14
SHEET    1   A 4 ALA A 132  ARG A 139  0
SHEET    2   A 4 ILE A  36  SER A  43 -1  N  SER A  43   O  ALA A 132
SHEET    3   A 4 TYR A  97  TYR A 103 -1  N  TYR A 103   O  ILE A  36
SHEET    4   A 4 ARG A  83  PRO A  89 -1  N  GLU A  88   O  ILE A  98
SHEET    1   B 4 LEU A 169  GLY A 171  0
SHEET    2   B 4 SER A 398  GLN A 401  1  N  LEU A 400   O  LEU A 169
SHEET    3   B 4 LEU A 375  SER A 379  1  N  PRO A 376   O  VAL A 399
SHEET    4   B 4 HIS A 325  HIS A 327  1  N  ILE A 326   O  LEU A 375
SHEET    1   C 2 PHE A 199  KCX A 201  0
SHEET    2   C 2 GLY A 237  TYR A 239  1  N  GLY A 237   O  THR A 200
SHEET    1   D 2 ILE A 264  ASP A 268  0
SHEET    2   D 2 LEU A 290  HIS A 294  1  N  LEU A 290   O  VAL A 265
SHEET    1   E 4 THR S  68  TRP S  70  0
SHEET    2   E 4 ILE S  39  GLU S  45 -1  N  PHE S  44   O  THR S  68
SHEET    3   E 4 PHE S  98  PHE S 104 -1  N  PHE S 104   O  ILE S  39
SHEET    4   E 4 ILE S 113  TYR S 118 -1  N  TYR S 118   O  ILE S  99
SHEET    1   F 4 ALA B 132  ARG B 139  0
SHEET    2   F 4 ILE B  36  SER B  43 -1  N  SER B  43   O  ALA B 132
SHEET    3   F 4 TYR B  97  TYR B 103 -1  N  TYR B 103   O  ILE B  36
SHEET    4   F 4 ARG B  83  PRO B  89 -1  N  GLU B  88   O  ILE B  98
SHEET    1   G 4 LEU B 169  GLY B 171  0
SHEET    2   G 4 SER B 398  GLN B 401  1  N  LEU B 400   O  LEU B 169
SHEET    3   G 4 LEU B 375  SER B 379  1  N  PRO B 376   O  VAL B 399
SHEET    4   G 4 HIS B 325  HIS B 327  1  N  ILE B 326   O  LEU B 375
SHEET    1   H 2 PHE B 199  KCX B 201  0
SHEET    2   H 2 GLY B 237  TYR B 239  1  N  GLY B 237   O  THR B 200
SHEET    1   I 2 ILE B 264  ASP B 268  0
SHEET    2   I 2 LEU B 290  HIS B 294  1  N  LEU B 290   O  VAL B 265
SHEET    1   J 4 THR T  68  TRP T  70  0
SHEET    2   J 4 ILE T  39  GLU T  45 -1  N  PHE T  44   O  THR T  68
SHEET    3   J 4 PHE T  98  PHE T 104 -1  N  PHE T 104   O  ILE T  39
SHEET    4   J 4 ILE T 113  TYR T 118 -1  N  TYR T 118   O  ILE T  99
SHEET    1   K 4 ALA C 132  ARG C 139  0
SHEET    2   K 4 ILE C  36  SER C  43 -1  N  SER C  43   O  ALA C 132
SHEET    3   K 4 TYR C  97  TYR C 103 -1  N  TYR C 103   O  ILE C  36
SHEET    4   K 4 ARG C  83  PRO C  89 -1  N  GLU C  88   O  ILE C  98
SHEET    1   L 4 LEU C 169  GLY C 171  0
SHEET    2   L 4 SER C 398  GLN C 401  1  N  LEU C 400   O  LEU C 169
SHEET    3   L 4 LEU C 375  SER C 379  1  N  PRO C 376   O  VAL C 399
SHEET    4   L 4 HIS C 325  HIS C 327  1  N  ILE C 326   O  LEU C 375
SHEET    1   M 2 PHE C 199  KCX C 201  0
SHEET    2   M 2 GLY C 237  TYR C 239  1  N  GLY C 237   O  THR C 200
SHEET    1   N 2 ILE C 264  ASP C 268  0
SHEET    2   N 2 LEU C 290  HIS C 294  1  N  LEU C 290   O  VAL C 265
SHEET    1   O 3 ILE U  39  GLU U  45  0
SHEET    2   O 3 PHE U  98  PHE U 104 -1  N  PHE U 104   O  ILE U  39
SHEET    3   O 3 ILE U 113  TYR U 118 -1  N  TYR U 118   O  ILE U  99
SHEET    1   P 4 ALA D 132  ARG D 139  0
SHEET    2   P 4 ILE D  36  SER D  43 -1  N  SER D  43   O  ALA D 132
SHEET    3   P 4 TYR D  97  TYR D 103 -1  N  TYR D 103   O  ILE D  36
SHEET    4   P 4 ARG D  83  PRO D  89 -1  N  GLU D  88   O  ILE D  98
SHEET    1   Q 4 LEU D 169  GLY D 171  0
SHEET    2   Q 4 SER D 398  GLN D 401  1  N  LEU D 400   O  LEU D 169
SHEET    3   Q 4 LEU D 375  SER D 379  1  N  PRO D 376   O  VAL D 399
SHEET    4   Q 4 HIS D 325  HIS D 327  1  N  ILE D 326   O  LEU D 375
SHEET    1   R 2 PHE D 199  KCX D 201  0
SHEET    2   R 2 GLY D 237  TYR D 239  1  N  GLY D 237   O  THR D 200
SHEET    1   S 2 ILE D 264  ASP D 268  0
SHEET    2   S 2 LEU D 290  HIS D 294  1  N  LEU D 290   O  VAL D 265
SHEET    1   T 4 THR V  68  TRP V  70  0
SHEET    2   T 4 ILE V  39  GLU V  45 -1  N  PHE V  44   O  THR V  68
SHEET    3   T 4 PHE V  98  PHE V 104 -1  N  PHE V 104   O  ILE V  39
SHEET    4   T 4 ILE V 113  TYR V 118 -1  N  TYR V 118   O  ILE V  99
LINK         N   KCX A 201                 C   THR A 200
LINK         C   KCX A 201                 N   ASP A 202
LINK         OQ2 KCX A 201                MG    MG A 476
LINK        MG    MG A 476                 OE1 GLU A 204
LINK        MG    MG A 476                 O3  CAP A   1
LINK         N   KCX B 201                 C   THR B 200
LINK         C   KCX B 201                 N   ASP B 202
LINK         OQ2 KCX B 201                MG    MG B 476
LINK         N   KCX C 201                 C   THR C 200
LINK         C   KCX C 201                 N   ASP C 202
LINK         OQ2 KCX C 201                MG    MG C 476
LINK        MG    MG C 476                 OD1 ASP C 203
LINK        MG    MG C 476                 OE1 GLU C 204
LINK         N   KCX D 201                 C   THR D 200
LINK         C   KCX D 201                 N   ASP D 202
LINK         OQ2 KCX D 201                MG    MG D 476
LINK        MG    MG D 476                 OD1 ASP D 203
LINK        MG    MG D 476                 OE1 GLU D 204
LINK        MG    MG D 476                 O3  CAP D   1
CISPEP   1 LYS A  175    PRO A  176          0        -1.44
CISPEP   2 LYS B  175    PRO B  176          0        -2.80
CISPEP   3 LYS C  175    PRO C  176          0        -2.54
CISPEP   4 LYS D  175    PRO D  176          0        -4.09
SITE     1 ACA 12 LYS A 175  LYS A 177  KCX A 201  ASP A 203
SITE     2 ACA 12 GLU A 204  HIS A 294  ARG A 295  HIS A 298
SITE     3 ACA 12 HIS A 327  SER A 379  CAP A   1   MG A 476
SITE     1 ACB 12 LYS B 175  LYS B 177  KCX B 201  ASP B 203
SITE     2 ACB 12 GLU B 204  HIS B 294  ARG B 295  HIS B 298
SITE     3 ACB 12 HIS B 327  SER B 379  CAP B   1   MG B 476
SITE     1 ACC 12 LYS C 175  LYS C 177  KCX C 201  ASP C 203
SITE     2 ACC 12 GLU C 204  HIS C 294  ARG C 295  HIS C 298
SITE     3 ACC 12 HIS C 327  SER C 379  CAP C   1   MG C 476
SITE     1 ACD 12 LYS D 175  LYS D 177  KCX D 201  ASP D 203
SITE     2 ACD 12 GLU D 204  HIS D 294  ARG D 295  HIS D 298
SITE     3 ACD 12 HIS D 327  SER D 379  CAP D   1   MG D 476
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