spacer
spacer

PDBsum entry 1bwv

Go to PDB code: 
Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
1bwv
Jmol
Contents
Protein chains
472 a.a. *
138 a.a. *
Ligands
CAP ×4
Metals
_MG ×4
Waters ×542
* Residue conservation analysis
HEADER    LYASE                                   29-SEP-98   1BWV
TITLE     ACTIVATED RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE (RUBISCO)
TITLE    2 COMPLEXED WITH THE REACTION INTERMEDIATE ANALOGUE 2-CARBOXYARABINITOL
TITLE    3 1,5-BISPHOSPHATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN (RIBULOSE BISPHOSPHATE CARBOXYLASE);
COMPND   3 CHAIN: A, C, E, G;
COMPND   4 SYNONYM: RUBISCO;
COMPND   5 EC: 4.1.1.39;
COMPND   6 OTHER_DETAILS: THE ENZYME IS COMPLEXED WITH CARBON DIOXIDE, MG2+ AND
COMPND   7 REACTION INTERMEDIATE ANALOGUE, 2-CARBOXYARABINITOL 1,5-BISPHOSPHATE.
COMPND   8 RESIDUE 201, KCX, OF THE LARGE SUBUNIT IS A LYS CARBAMYLATED AT THE
COMPND   9 EPSILON-AMINO GROUP;
COMPND  10 MOL_ID: 2;
COMPND  11 MOLECULE: PROTEIN (RIBULOSE BISPHOSPHATE CARBOXYLASE);
COMPND  12 CHAIN: S, U, W, Y;
COMPND  13 SYNONYM: RUBISCO;
COMPND  14 EC: 4.1.1.39;
COMPND  15 OTHER_DETAILS: THE ENZYME IS COMPLEXED WITH CARBON DIOXIDE, MG2+ AND
COMPND  16 REACTION INTERMEDIATE ANALOGUE, 2-CARBOXYARABINITOL 1,5-BISPHOSPHATE.
COMPND  17 RESIDUE 201, KXC, OF THE LARGE SUBUNIT IS A LYS CARBAMYLATED AT THE
COMPND  18 EPSILON-AMINO GROUP
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: GALDIERIA PARTITA;
SOURCE   3 ORGANISM_TAXID: 83374;
SOURCE   4 ORGANELLE: CHLOROPLAST;
SOURCE   5 MOL_ID: 2;
SOURCE   6 ORGANISM_SCIENTIFIC: GALDIERIA PARTITA;
SOURCE   7 ORGANISM_TAXID: 83374;
SOURCE   8 ORGANELLE: CHLOROPLAST
KEYWDS    CARBON DIOXIDE FIXATION, COMPLEX (RUBISCO-REACTION INTERMEDIATE),
KEYWDS   2 HIGH SPECIFICITY FACTOR, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    H.SUGAWARA,H.YAMAMOTO,N.SHIBATA,T.INOUE,C.MIYAKE,A.YOKOTA,Y.KAI
REVDAT   3   13-JUL-11 1BWV    1       VERSN
REVDAT   2   24-FEB-09 1BWV    1       VERSN
REVDAT   1   27-SEP-99 1BWV    0
JRNL        AUTH   H.SUGAWARA,H.YAMAMOTO,N.SHIBATA,T.INOUE,S.OKADA,C.MIYAKE,
JRNL        AUTH 2 A.YOKOTA,Y.KAI
JRNL        TITL   CRYSTAL STRUCTURE OF CARBOXYLASE REACTION-ORIENTED RIBULOSE
JRNL        TITL 2 1, 5-BISPHOSPHATE CARBOXYLASE/OXYGENASE FROM A THERMOPHILIC
JRNL        TITL 3 RED ALGA, GALDIERIA PARTITA.
JRNL        REF    J.BIOL.CHEM.                  V. 274 15655 1999
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   10336462
JRNL        DOI    10.1074/JBC.274.22.15655
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   I.ANDERSSON
REMARK   1  TITL   LARGE STRUCTURES AT HIGH RESOLUTION: THE 1.6 A CRYSTAL
REMARK   1  TITL 2 STRUCTURE OF SPINACH RIBULOSE-1,5-BISPHOSPHATE
REMARK   1  TITL 3 CARBOXYLASE/OXYGENASE COMPLEXED WITH 2- CARBOXYARABINITOL
REMARK   1  TITL 4 BISPHOSPHATE
REMARK   1  REF    J.MOL.BIOL.                   V. 259   160 1996
REMARK   1  REFN                   ISSN 0022-2836
REMARK   2
REMARK   2 RESOLUTION.    2.40 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) : 2.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
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)   (%) : 86.0
REMARK   3   NUMBER OF REFLECTIONS             : 82988
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) : 0.163
REMARK   3   FREE R VALUE                     : 0.197
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 4149
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            : 19408
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 88
REMARK   3   SOLVENT ATOMS            : 542
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 20.10
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.25
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 4.00
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) : 2.60
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 : RESTRAINTS
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  : PARAM19X.PRO
REMARK   3  PARAMETER FILE  2  : NULL
REMARK   3  TOPOLOGY FILE  1   : TPPH19X.PRO
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1BWV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-99.
REMARK 100 THE RCSB ID CODE IS RCSB007215.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-MAR-98
REMARK 200  TEMPERATURE           (KELVIN) : 293
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY
REMARK 200  BEAMLINE                       : BL-18B
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : FUJI
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 277331
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.4
REMARK 200  DATA REDUNDANCY                : 3.200
REMARK 200  R MERGE                    (I) : 0.09700
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) : 2.40
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49
REMARK 200  COMPLETENESS FOR SHELL     (%) : 58.1
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.20300
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 1RBL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 51.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 9% PEG8000, 4% MPD, 50 MM HEPES PH7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
REMARK 290       4555   -X,-Y,Z
REMARK 290       5555   Y,-X+Y,Z+1/3
REMARK 290       6555   X-Y,X,Z+2/3
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      106.54333
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      213.08667
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  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      106.54333
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      213.08667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE ENZYME IS HEXADECAMER AND CONSISTS OF EIGHT LARGE AND
REMARK 300 EIGHT SMALL SUBUNITS.  THE CHAINS ID'S OF LARGE SUBUNITS ARE
REMARK 300 A,B,C,D,E,F,G AND H.  THE CHAINS ID'S OF SMALL SUBUNITS ARE
REMARK 300 S,T,U,V,W,X,Y AND Z.  FOUR LARGE SUBUNITS (L) AND FOUR SMALL
REMARK 300 SUBUNITS (S) ARE CONTAINED IN THE ASYMMETRIC UNIT.
REMARK 300 A PAIR OF L4S4 UNITS RELATED BY THE CRYSTALLOGRAPHIC 2-FOLD
REMARK 300 GENERATES THE HEXADECAMER.  CATALYTIC UNITS OF THE ENZYME AR
REMARK 300 L2S2 WHICH IS CONSTITUTED BY CHAINS ABST, CDUV, EFWX AND GHY
REMARK 300 OF THE HEXADECAMER.
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: 108770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 124270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -458.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, S, C, U, E, W, G, Y
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 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    -7
REMARK 465     SER A    -6
REMARK 465     GLN A    -5
REMARK 465     SER A    -4
REMARK 465     ILE A    -3
REMARK 465     GLU A    -2
REMARK 465     GLU A    -1
REMARK 465     LYS A     0
REMARK 465     SER A     1
REMARK 465     VAL A     2
REMARK 465     GLN A     3
REMARK 465     GLU A     4
REMARK 465     ARG A     5
REMARK 465     THR A     6
REMARK 465     GLU A   479
REMARK 465     THR A   480
REMARK 465     PRO A   481
REMARK 465     THR A   482
REMARK 465     ALA A   483
REMARK 465     ASN A   484
REMARK 465     ILE A   485
REMARK 465     MET C    -7
REMARK 465     SER C    -6
REMARK 465     GLN C    -5
REMARK 465     SER C    -4
REMARK 465     ILE C    -3
REMARK 465     GLU C    -2
REMARK 465     GLU C    -1
REMARK 465     LYS C     0
REMARK 465     SER C     1
REMARK 465     VAL C     2
REMARK 465     GLN C     3
REMARK 465     GLU C     4
REMARK 465     ARG C     5
REMARK 465     THR C     6
REMARK 465     GLU C   479
REMARK 465     THR C   480
REMARK 465     PRO C   481
REMARK 465     THR C   482
REMARK 465     ALA C   483
REMARK 465     ASN C   484
REMARK 465     ILE C   485
REMARK 465     MET E    -7
REMARK 465     SER E    -6
REMARK 465     GLN E    -5
REMARK 465     SER E    -4
REMARK 465     ILE E    -3
REMARK 465     GLU E    -2
REMARK 465     GLU E    -1
REMARK 465     LYS E     0
REMARK 465     SER E     1
REMARK 465     VAL E     2
REMARK 465     GLN E     3
REMARK 465     GLU E     4
REMARK 465     ARG E     5
REMARK 465     THR E     6
REMARK 465     GLU E   479
REMARK 465     THR E   480
REMARK 465     PRO E   481
REMARK 465     THR E   482
REMARK 465     ALA E   483
REMARK 465     ASN E   484
REMARK 465     ILE E   485
REMARK 465     MET G    -7
REMARK 465     SER G    -6
REMARK 465     GLN G    -5
REMARK 465     SER G    -4
REMARK 465     ILE G    -3
REMARK 465     GLU G    -2
REMARK 465     GLU G    -1
REMARK 465     LYS G     0
REMARK 465     SER G     1
REMARK 465     VAL G     2
REMARK 465     GLN G     3
REMARK 465     GLU G     4
REMARK 465     ARG G     5
REMARK 465     THR G     6
REMARK 465     GLU G   479
REMARK 465     THR G   480
REMARK 465     PRO G   481
REMARK 465     THR G   482
REMARK 465     ALA G   483
REMARK 465     ASN G   484
REMARK 465     ILE G   485
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),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500    GLU A 204   CD    GLU A 204   OE1    -0.164
REMARK 500    HIS A 238   NE2   HIS A 238   CD2    -0.075
REMARK 500    HIS A 292   NE2   HIS A 292   CD2    -0.078
REMARK 500    HIS A 307   NE2   HIS A 307   CD2    -0.072
REMARK 500    HIS A 325   NE2   HIS A 325   CD2    -0.074
REMARK 500    HIS A 388   NE2   HIS A 388   CD2    -0.076
REMARK 500    HIS A 392   NE2   HIS A 392   CD2    -0.068
REMARK 500    HIS A 409   NE2   HIS A 409   CD2    -0.070
REMARK 500    HIS S  49   NE2   HIS S  49   CD2    -0.068
REMARK 500    HIS S 122   NE2   HIS S 122   CD2    -0.066
REMARK 500    HIS S 143   NE2   HIS S 143   CD2    -0.071
REMARK 500    GLU C 204   CD    GLU C 204   OE1    -0.149
REMARK 500    HIS C 238   NE2   HIS C 238   CD2    -0.076
REMARK 500    HIS C 292   NE2   HIS C 292   CD2    -0.076
REMARK 500    HIS C 307   NE2   HIS C 307   CD2    -0.073
REMARK 500    HIS C 325   NE2   HIS C 325   CD2    -0.069
REMARK 500    HIS C 327   NE2   HIS C 327   CD2    -0.067
REMARK 500    HIS C 388   NE2   HIS C 388   CD2    -0.077
REMARK 500    HIS C 392   NE2   HIS C 392   CD2    -0.068
REMARK 500    HIS C 409   NE2   HIS C 409   CD2    -0.072
REMARK 500    HIS U  49   NE2   HIS U  49   CD2    -0.068
REMARK 500    HIS U 122   NE2   HIS U 122   CD2    -0.068
REMARK 500    HIS U 143   NE2   HIS U 143   CD2    -0.070
REMARK 500    GLU E 204   CD    GLU E 204   OE1    -0.144
REMARK 500    HIS E 238   NE2   HIS E 238   CD2    -0.077
REMARK 500    HIS E 292   NE2   HIS E 292   CD2    -0.078
REMARK 500    HIS E 307   NE2   HIS E 307   CD2    -0.070
REMARK 500    HIS E 325   NE2   HIS E 325   CD2    -0.074
REMARK 500    HIS E 388   NE2   HIS E 388   CD2    -0.073
REMARK 500    HIS E 392   NE2   HIS E 392   CD2    -0.068
REMARK 500    HIS E 409   NE2   HIS E 409   CD2    -0.072
REMARK 500    HIS W  49   NE2   HIS W  49   CD2    -0.069
REMARK 500    HIS W 143   NE2   HIS W 143   CD2    -0.071
REMARK 500    GLU G 204   CD    GLU G 204   OE1    -0.210
REMARK 500    HIS G 238   NE2   HIS G 238   CD2    -0.075
REMARK 500    HIS G 292   NE2   HIS G 292   CD2    -0.076
REMARK 500    HIS G 307   NE2   HIS G 307   CD2    -0.072
REMARK 500    HIS G 325   NE2   HIS G 325   CD2    -0.071
REMARK 500    HIS G 327   NE2   HIS G 327   CD2    -0.068
REMARK 500    HIS G 388   NE2   HIS G 388   CD2    -0.075
REMARK 500    HIS G 392   NE2   HIS G 392   CD2    -0.068
REMARK 500    HIS G 409   NE2   HIS G 409   CD2    -0.072
REMARK 500    HIS Y  49   NE2   HIS Y  49   CD2    -0.069
REMARK 500    HIS Y 122   NE2   HIS Y 122   CD2    -0.066
REMARK 500    HIS Y 143   NE2   HIS Y 143   CD2    -0.070
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  12   CA  -  CB  -  CG  ANGL. DEV. =  13.8 DEGREES
REMARK 500    TRP A  25   CD1 -  CG  -  CD2 ANGL. DEV. =   6.2 DEGREES
REMARK 500    TRP A  25   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.0 DEGREES
REMARK 500    TRP A  66   CD1 -  CG  -  CD2 ANGL. DEV. =   7.0 DEGREES
REMARK 500    TRP A  66   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.3 DEGREES
REMARK 500    TRP A  70   CD1 -  CG  -  CD2 ANGL. DEV. =   6.1 DEGREES
REMARK 500    TRP A  70   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.8 DEGREES
REMARK 500    ARG A 159   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ARG A 187   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES
REMARK 500    ARG A 187   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    TRP A 214   CD1 -  CG  -  CD2 ANGL. DEV. =   6.2 DEGREES
REMARK 500    TRP A 214   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 DEGREES
REMARK 500    TRP A 283   CD1 -  CG  -  CD2 ANGL. DEV. =   6.4 DEGREES
REMARK 500    TRP A 283   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 DEGREES
REMARK 500    ARG A 295   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES
REMARK 500    TRP A 317   CD1 -  CG  -  CD2 ANGL. DEV. =   6.2 DEGREES
REMARK 500    TRP A 317   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.6 DEGREES
REMARK 500    TRP A 368   CD1 -  CG  -  CD2 ANGL. DEV. =   6.5 DEGREES
REMARK 500    TRP A 368   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.1 DEGREES
REMARK 500    TRP A 462   CD1 -  CG  -  CD2 ANGL. DEV. =   6.3 DEGREES
REMARK 500    TRP A 462   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 DEGREES
REMARK 500    ARG S   9   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    TRP S  67   CD1 -  CG  -  CD2 ANGL. DEV. =   5.9 DEGREES
REMARK 500    TRP S  67   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.6 DEGREES
REMARK 500    TRP S  70   CD1 -  CG  -  CD2 ANGL. DEV. =   6.7 DEGREES
REMARK 500    TRP S  70   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.3 DEGREES
REMARK 500    ARG C  12   CA  -  CB  -  CG  ANGL. DEV. =  13.8 DEGREES
REMARK 500    TRP C  25   CD1 -  CG  -  CD2 ANGL. DEV. =   6.2 DEGREES
REMARK 500    TRP C  25   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.1 DEGREES
REMARK 500    TRP C  66   CD1 -  CG  -  CD2 ANGL. DEV. =   6.8 DEGREES
REMARK 500    TRP C  66   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.1 DEGREES
REMARK 500    TRP C  70   CD1 -  CG  -  CD2 ANGL. DEV. =   6.2 DEGREES
REMARK 500    TRP C  70   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 DEGREES
REMARK 500    ARG C 159   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ARG C 187   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES
REMARK 500    ARG C 187   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    TRP C 214   CD1 -  CG  -  CD2 ANGL. DEV. =   6.2 DEGREES
REMARK 500    TRP C 214   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.8 DEGREES
REMARK 500    TRP C 283   CD1 -  CG  -  CD2 ANGL. DEV. =   6.3 DEGREES
REMARK 500    TRP C 283   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.0 DEGREES
REMARK 500    ARG C 303   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES
REMARK 500    TRP C 317   CD1 -  CG  -  CD2 ANGL. DEV. =   6.3 DEGREES
REMARK 500    TRP C 317   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.7 DEGREES
REMARK 500    TRP C 368   CD1 -  CG  -  CD2 ANGL. DEV. =   6.4 DEGREES
REMARK 500    TRP C 368   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.1 DEGREES
REMARK 500    TRP C 462   CD1 -  CG  -  CD2 ANGL. DEV. =   6.3 DEGREES
REMARK 500    TRP C 462   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.8 DEGREES
REMARK 500    ARG U   9   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500    ARG U   9   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    TRP U  67   CD1 -  CG  -  CD2 ANGL. DEV. =   6.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS     106 ANGLE DEVIATIONS.
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  11     -154.40    173.21
REMARK 500    SER A  62      -70.66   -128.78
REMARK 500    ASN A 207      -82.48   -135.03
REMARK 500    MET A 212      116.01   -166.11
REMARK 500    ILE S  48       46.53    -88.28
REMARK 500    ASN S  96       50.01   -109.38
REMARK 500    ILE S 108      -74.49   -101.93
REMARK 500    ASP S 133     -138.83   -117.99
REMARK 500    SER S 135     -112.31     48.34
REMARK 500    SER C  11     -154.11    173.56
REMARK 500    SER C  62      -70.51   -128.85
REMARK 500    ASN C 207      -82.15   -135.03
REMARK 500    MET C 212      116.88   -166.14
REMARK 500    ILE U  48       46.58    -88.03
REMARK 500    ASN U  96       49.88   -109.58
REMARK 500    ILE U 108      -74.27   -101.60
REMARK 500    ASP U 133     -138.76   -118.71
REMARK 500    SER U 135     -112.32     48.30
REMARK 500    SER E  11     -154.39    173.21
REMARK 500    SER E  62      -70.59   -128.73
REMARK 500    ASN E 207      -82.23   -135.18
REMARK 500    MET E 212      115.91   -165.98
REMARK 500    ILE W  48       46.52    -88.10
REMARK 500    ASN W  96       50.02   -109.40
REMARK 500    ILE W 108      -74.38   -101.99
REMARK 500    ASP W 133     -138.86   -118.03
REMARK 500    SER W 135     -112.63     49.15
REMARK 500    SER G  11     -154.08    173.55
REMARK 500    SER G  62      -70.37   -128.91
REMARK 500    ASN G 207      -81.97   -134.91
REMARK 500    MET G 212      116.76   -166.08
REMARK 500    ILE Y  48       46.54    -88.13
REMARK 500    ASN Y  96       49.84   -109.61
REMARK 500    ILE Y 108      -74.14   -101.69
REMARK 500    ASP Y 133     -138.58   -118.59
REMARK 500    SER Y 135     -112.36     48.37
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 C 563        DISTANCE =  5.97 ANGSTROMS
REMARK 525    HOH C 582        DISTANCE =  5.27 ANGSTROMS
REMARK 525    HOH G 563        DISTANCE =  5.54 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 KCX: THE EPSILON AMINO GROUP OF LYSINE 201 IS CARBAMYLATED.
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 490  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX A 201   OQ1
REMARK 620 2 CAP A 491   O2  112.5
REMARK 620 3 CAP A 491   O3   94.6  80.8
REMARK 620 4 CAP A 491   O7  177.2  69.6  87.6
REMARK 620 5 GLU A 204   OE1  87.5 160.1  97.6  90.6
REMARK 620 6 ASP A 203   OD1  93.8 110.7 161.7  83.5  66.7
REMARK 620 7 KCX A 201   OQ2  44.1  83.7  56.5 138.6 112.1 136.6
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG C 490  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX C 201   OQ1
REMARK 620 2 ASP C 203   OD1  91.6
REMARK 620 3 CAP C 491   O2  110.7 112.7
REMARK 620 4 CAP C 491   O3   98.0 163.9  76.0
REMARK 620 5 CAP C 491   O7  175.7  85.6  67.6  85.5
REMARK 620 6 GLU C 204   OE1  88.5  69.3 160.3  97.8  93.5
REMARK 620 7 KCX C 201   OQ2  44.2 135.0  83.4  57.4 137.9 109.3
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG E 490  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX E 201   OQ1
REMARK 620 2 CAP E 491   O2  114.5
REMARK 620 3 CAP E 491   O3  101.4  78.5
REMARK 620 4 CAP E 491   O7  172.1  67.7  86.5
REMARK 620 5 KCX E 201   OQ2  46.0  87.6  59.1 141.6
REMARK 620 6 GLU E 204   OE1  85.5 159.9  99.8  92.3 108.9
REMARK 620 7 ASP E 203   OD1  88.0 110.8 162.7  84.1 133.5  66.3
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG G 490  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX G 201   OQ1
REMARK 620 2 CAP G 491   O2  116.8
REMARK 620 3 CAP G 491   O3  100.0  82.2
REMARK 620 4 CAP G 491   O7  171.9  68.2  86.8
REMARK 620 5 KCX G 201   OQ2  44.4  89.1  61.4 143.7
REMARK 620 6 GLU G 204   OE1  83.8 159.3  93.4  91.4 106.6
REMARK 620 7 ASP G 203   OD1  88.7 114.0 155.8  83.3 132.8  64.9
REMARK 620 N                    1     2     3     4     5     6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: MGA
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: MG BINDING SITE CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: MGC
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: MG BINDING SITE CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: MGE
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: MG BINDING SITE CHAIN E
REMARK 800
REMARK 800 SITE_IDENTIFIER: MGG
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: MG BINDING SITE CHAIN G
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 490
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 490
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 490
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 490
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A 491
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP C 491
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E 491
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP G 491
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE RESIDUE NUMBERING OF SPINACH RUBISCO HAS BEEN USED IN
REMARK 999 GALDIERIA ENZYME.
DBREF  1BWV A   -7   485  UNP    O98949   O98949_9RHOD     1    493
DBREF  1BWV S    8   155  UNP    O98950   O98950_9RHOD     1    138
DBREF  1BWV C   -7   485  UNP    O98949   O98949_9RHOD     1    493
DBREF  1BWV U    8   155  UNP    O98950   O98950_9RHOD     1    138
DBREF  1BWV E   -7   485  UNP    O98949   O98949_9RHOD     1    493
DBREF  1BWV W    8   155  UNP    O98950   O98950_9RHOD     1    138
DBREF  1BWV G   -7   485  UNP    O98949   O98949_9RHOD     1    493
DBREF  1BWV Y    8   155  UNP    O98950   O98950_9RHOD     1    138
SEQADV 1BWV KCX A  201  UNP  O98949    LYS   210 MODIFIED RESIDUE
SEQADV 1BWV VAL S    8  UNP  O98950    MET     1 CONFLICT
SEQADV 1BWV KCX C  201  UNP  O98949    LYS   210 MODIFIED RESIDUE
SEQADV 1BWV VAL U    8  UNP  O98950    MET     1 CONFLICT
SEQADV 1BWV KCX E  201  UNP  O98949    LYS   210 MODIFIED RESIDUE
SEQADV 1BWV VAL W    8  UNP  O98950    MET     1 CONFLICT
SEQADV 1BWV KCX G  201  UNP  O98949    LYS   210 MODIFIED RESIDUE
SEQADV 1BWV VAL Y    8  UNP  O98950    MET     1 CONFLICT
SEQRES   1 A  493  MET SER GLN SER ILE GLU GLU LYS SER VAL GLN GLU ARG
SEQRES   2 A  493  THR ARG ILE LYS ASN SER ARG TYR GLU SER GLY VAL ILE
SEQRES   3 A  493  PRO TYR ALA LYS MET GLY TYR TRP ASN PRO ASP TYR GLN
SEQRES   4 A  493  VAL LYS ASP THR ASP VAL LEU ALA LEU PHE ARG VAL THR
SEQRES   5 A  493  PRO GLN PRO GLY VAL ASP PRO ILE GLU ALA ALA ALA ALA
SEQRES   6 A  493  VAL ALA GLY GLU SER SER THR ALA THR TRP THR VAL VAL
SEQRES   7 A  493  TRP THR ASP LEU LEU THR ALA ALA ASP LEU TYR ARG ALA
SEQRES   8 A  493  LYS ALA TYR LYS VAL ASP GLN VAL PRO ASN ASN PRO GLU
SEQRES   9 A  493  GLN TYR PHE ALA TYR ILE ALA TYR GLU LEU ASP LEU PHE
SEQRES  10 A  493  GLU GLU GLY SER ILE ALA ASN LEU THR ALA SER ILE ILE
SEQRES  11 A  493  GLY ASN VAL PHE GLY PHE LYS ALA VAL LYS ALA LEU ARG
SEQRES  12 A  493  LEU GLU ASP MET ARG LEU PRO LEU ALA TYR LEU LYS THR
SEQRES  13 A  493  PHE GLN GLY PRO ALA THR GLY VAL ILE LEU GLU ARG GLU
SEQRES  14 A  493  ARG LEU ASP LYS PHE GLY ARG PRO LEU LEU GLY CYS THR
SEQRES  15 A  493  THR LYS PRO LYS LEU GLY LEU SER GLY LYS ASN TYR GLY
SEQRES  16 A  493  ARG VAL VAL TYR GLU ALA LEU LYS GLY GLY LEU ASP PHE
SEQRES  17 A  493  VAL KCX ASP ASP GLU ASN ILE ASN SER GLN PRO PHE MET
SEQRES  18 A  493  ARG TRP ARG GLU ARG TYR LEU PHE THR MET GLU ALA VAL
SEQRES  19 A  493  ASN LYS ALA SER ALA ALA THR GLY GLU VAL LYS GLY HIS
SEQRES  20 A  493  TYR LEU ASN VAL THR ALA ALA THR MET GLU GLU MET TYR
SEQRES  21 A  493  ALA ARG ALA ASN PHE ALA LYS GLU LEU GLY SER VAL ILE
SEQRES  22 A  493  ILE MET ILE ASP LEU VAL ILE GLY TYR THR ALA ILE GLN
SEQRES  23 A  493  THR MET ALA LYS TRP ALA ARG ASP ASN ASP MET ILE LEU
SEQRES  24 A  493  HIS LEU HIS ARG ALA GLY ASN SER THR TYR SER ARG GLN
SEQRES  25 A  493  LYS ASN HIS GLY MET ASN PHE ARG VAL ILE CYS LYS TRP
SEQRES  26 A  493  MET ARG MET ALA GLY VAL ASP HIS ILE HIS ALA GLY THR
SEQRES  27 A  493  VAL VAL GLY LYS LEU GLU GLY ASP PRO ILE ILE THR ARG
SEQRES  28 A  493  GLY PHE TYR LYS THR LEU LEU LEU PRO LYS LEU GLU ARG
SEQRES  29 A  493  ASN LEU GLN GLU GLY LEU PHE PHE ASP MET GLU TRP ALA
SEQRES  30 A  493  SER LEU ARG LYS VAL MET PRO VAL ALA SER GLY GLY ILE
SEQRES  31 A  493  HIS ALA GLY GLN MET HIS GLN LEU ILE HIS TYR LEU GLY
SEQRES  32 A  493  GLU ASP VAL VAL LEU GLN PHE GLY GLY GLY THR ILE GLY
SEQRES  33 A  493  HIS PRO ASP GLY ILE GLN ALA GLY ALA THR ALA ASN ARG
SEQRES  34 A  493  VAL ALA LEU GLU ALA MET ILE LEU ALA ARG ASN GLU ASN
SEQRES  35 A  493  ARG ASP TYR LEU THR GLU GLY PRO GLU ILE LEU ARG GLU
SEQRES  36 A  493  ALA ALA LYS THR CYS GLY ALA LEU ARG THR ALA LEU ASP
SEQRES  37 A  493  LEU TRP LYS ASP ILE THR PHE ASN TYR THR SER THR ASP
SEQRES  38 A  493  THR SER ASP PHE VAL GLU THR PRO THR ALA ASN ILE
SEQRES   1 S  138  VAL ARG ILE THR GLN GLY THR PHE SER PHE LEU PRO ASP
SEQRES   2 S  138  LEU THR ASP GLU GLN ILE LYS LYS GLN ILE ASP TYR MET
SEQRES   3 S  138  ILE SER LYS LYS LEU ALA ILE GLY ILE GLU TYR THR ASN
SEQRES   4 S  138  ASP ILE HIS PRO ARG ASN ALA TYR TRP GLU ILE TRP GLY
SEQRES   5 S  138  LEU PRO LEU PHE ASP VAL THR ASP PRO ALA ALA VAL LEU
SEQRES   6 S  138  PHE GLU ILE ASN ALA CYS ARG LYS ALA ARG SER ASN PHE
SEQRES   7 S  138  TYR ILE LYS VAL VAL GLY PHE SER SER VAL ARG GLY ILE
SEQRES   8 S  138  GLU SER THR ILE ILE SER PHE ILE VAL ASN ARG PRO LYS
SEQRES   9 S  138  HIS GLU PRO GLY PHE ASN LEU MET ARG GLN GLU ASP LYS
SEQRES  10 S  138  SER ARG SER ILE LYS TYR THR ILE HIS SER TYR GLU SER
SEQRES  11 S  138  TYR LYS PRO GLU ASP GLU ARG TYR
SEQRES   1 C  493  MET SER GLN SER ILE GLU GLU LYS SER VAL GLN GLU ARG
SEQRES   2 C  493  THR ARG ILE LYS ASN SER ARG TYR GLU SER GLY VAL ILE
SEQRES   3 C  493  PRO TYR ALA LYS MET GLY TYR TRP ASN PRO ASP TYR GLN
SEQRES   4 C  493  VAL LYS ASP THR ASP VAL LEU ALA LEU PHE ARG VAL THR
SEQRES   5 C  493  PRO GLN PRO GLY VAL ASP PRO ILE GLU ALA ALA ALA ALA
SEQRES   6 C  493  VAL ALA GLY GLU SER SER THR ALA THR TRP THR VAL VAL
SEQRES   7 C  493  TRP THR ASP LEU LEU THR ALA ALA ASP LEU TYR ARG ALA
SEQRES   8 C  493  LYS ALA TYR LYS VAL ASP GLN VAL PRO ASN ASN PRO GLU
SEQRES   9 C  493  GLN TYR PHE ALA TYR ILE ALA TYR GLU LEU ASP LEU PHE
SEQRES  10 C  493  GLU GLU GLY SER ILE ALA ASN LEU THR ALA SER ILE ILE
SEQRES  11 C  493  GLY ASN VAL PHE GLY PHE LYS ALA VAL LYS ALA LEU ARG
SEQRES  12 C  493  LEU GLU ASP MET ARG LEU PRO LEU ALA TYR LEU LYS THR
SEQRES  13 C  493  PHE GLN GLY PRO ALA THR GLY VAL ILE LEU GLU ARG GLU
SEQRES  14 C  493  ARG LEU ASP LYS PHE GLY ARG PRO LEU LEU GLY CYS THR
SEQRES  15 C  493  THR LYS PRO LYS LEU GLY LEU SER GLY LYS ASN TYR GLY
SEQRES  16 C  493  ARG VAL VAL TYR GLU ALA LEU LYS GLY GLY LEU ASP PHE
SEQRES  17 C  493  VAL KCX ASP ASP GLU ASN ILE ASN SER GLN PRO PHE MET
SEQRES  18 C  493  ARG TRP ARG GLU ARG TYR LEU PHE THR MET GLU ALA VAL
SEQRES  19 C  493  ASN LYS ALA SER ALA ALA THR GLY GLU VAL LYS GLY HIS
SEQRES  20 C  493  TYR LEU ASN VAL THR ALA ALA THR MET GLU GLU MET TYR
SEQRES  21 C  493  ALA ARG ALA ASN PHE ALA LYS GLU LEU GLY SER VAL ILE
SEQRES  22 C  493  ILE MET ILE ASP LEU VAL ILE GLY TYR THR ALA ILE GLN
SEQRES  23 C  493  THR MET ALA LYS TRP ALA ARG ASP ASN ASP MET ILE LEU
SEQRES  24 C  493  HIS LEU HIS ARG ALA GLY ASN SER THR TYR SER ARG GLN
SEQRES  25 C  493  LYS ASN HIS GLY MET ASN PHE ARG VAL ILE CYS LYS TRP
SEQRES  26 C  493  MET ARG MET ALA GLY VAL ASP HIS ILE HIS ALA GLY THR
SEQRES  27 C  493  VAL VAL GLY LYS LEU GLU GLY ASP PRO ILE ILE THR ARG
SEQRES  28 C  493  GLY PHE TYR LYS THR LEU LEU LEU PRO LYS LEU GLU ARG
SEQRES  29 C  493  ASN LEU GLN GLU GLY LEU PHE PHE ASP MET GLU TRP ALA
SEQRES  30 C  493  SER LEU ARG LYS VAL MET PRO VAL ALA SER GLY GLY ILE
SEQRES  31 C  493  HIS ALA GLY GLN MET HIS GLN LEU ILE HIS TYR LEU GLY
SEQRES  32 C  493  GLU ASP VAL VAL LEU GLN PHE GLY GLY GLY THR ILE GLY
SEQRES  33 C  493  HIS PRO ASP GLY ILE GLN ALA GLY ALA THR ALA ASN ARG
SEQRES  34 C  493  VAL ALA LEU GLU ALA MET ILE LEU ALA ARG ASN GLU ASN
SEQRES  35 C  493  ARG ASP TYR LEU THR GLU GLY PRO GLU ILE LEU ARG GLU
SEQRES  36 C  493  ALA ALA LYS THR CYS GLY ALA LEU ARG THR ALA LEU ASP
SEQRES  37 C  493  LEU TRP LYS ASP ILE THR PHE ASN TYR THR SER THR ASP
SEQRES  38 C  493  THR SER ASP PHE VAL GLU THR PRO THR ALA ASN ILE
SEQRES   1 U  138  VAL ARG ILE THR GLN GLY THR PHE SER PHE LEU PRO ASP
SEQRES   2 U  138  LEU THR ASP GLU GLN ILE LYS LYS GLN ILE ASP TYR MET
SEQRES   3 U  138  ILE SER LYS LYS LEU ALA ILE GLY ILE GLU TYR THR ASN
SEQRES   4 U  138  ASP ILE HIS PRO ARG ASN ALA TYR TRP GLU ILE TRP GLY
SEQRES   5 U  138  LEU PRO LEU PHE ASP VAL THR ASP PRO ALA ALA VAL LEU
SEQRES   6 U  138  PHE GLU ILE ASN ALA CYS ARG LYS ALA ARG SER ASN PHE
SEQRES   7 U  138  TYR ILE LYS VAL VAL GLY PHE SER SER VAL ARG GLY ILE
SEQRES   8 U  138  GLU SER THR ILE ILE SER PHE ILE VAL ASN ARG PRO LYS
SEQRES   9 U  138  HIS GLU PRO GLY PHE ASN LEU MET ARG GLN GLU ASP LYS
SEQRES  10 U  138  SER ARG SER ILE LYS TYR THR ILE HIS SER TYR GLU SER
SEQRES  11 U  138  TYR LYS PRO GLU ASP GLU ARG TYR
SEQRES   1 E  493  MET SER GLN SER ILE GLU GLU LYS SER VAL GLN GLU ARG
SEQRES   2 E  493  THR ARG ILE LYS ASN SER ARG TYR GLU SER GLY VAL ILE
SEQRES   3 E  493  PRO TYR ALA LYS MET GLY TYR TRP ASN PRO ASP TYR GLN
SEQRES   4 E  493  VAL LYS ASP THR ASP VAL LEU ALA LEU PHE ARG VAL THR
SEQRES   5 E  493  PRO GLN PRO GLY VAL ASP PRO ILE GLU ALA ALA ALA ALA
SEQRES   6 E  493  VAL ALA GLY GLU SER SER THR ALA THR TRP THR VAL VAL
SEQRES   7 E  493  TRP THR ASP LEU LEU THR ALA ALA ASP LEU TYR ARG ALA
SEQRES   8 E  493  LYS ALA TYR LYS VAL ASP GLN VAL PRO ASN ASN PRO GLU
SEQRES   9 E  493  GLN TYR PHE ALA TYR ILE ALA TYR GLU LEU ASP LEU PHE
SEQRES  10 E  493  GLU GLU GLY SER ILE ALA ASN LEU THR ALA SER ILE ILE
SEQRES  11 E  493  GLY ASN VAL PHE GLY PHE LYS ALA VAL LYS ALA LEU ARG
SEQRES  12 E  493  LEU GLU ASP MET ARG LEU PRO LEU ALA TYR LEU LYS THR
SEQRES  13 E  493  PHE GLN GLY PRO ALA THR GLY VAL ILE LEU GLU ARG GLU
SEQRES  14 E  493  ARG LEU ASP LYS PHE GLY ARG PRO LEU LEU GLY CYS THR
SEQRES  15 E  493  THR LYS PRO LYS LEU GLY LEU SER GLY LYS ASN TYR GLY
SEQRES  16 E  493  ARG VAL VAL TYR GLU ALA LEU LYS GLY GLY LEU ASP PHE
SEQRES  17 E  493  VAL KCX ASP ASP GLU ASN ILE ASN SER GLN PRO PHE MET
SEQRES  18 E  493  ARG TRP ARG GLU ARG TYR LEU PHE THR MET GLU ALA VAL
SEQRES  19 E  493  ASN LYS ALA SER ALA ALA THR GLY GLU VAL LYS GLY HIS
SEQRES  20 E  493  TYR LEU ASN VAL THR ALA ALA THR MET GLU GLU MET TYR
SEQRES  21 E  493  ALA ARG ALA ASN PHE ALA LYS GLU LEU GLY SER VAL ILE
SEQRES  22 E  493  ILE MET ILE ASP LEU VAL ILE GLY TYR THR ALA ILE GLN
SEQRES  23 E  493  THR MET ALA LYS TRP ALA ARG ASP ASN ASP MET ILE LEU
SEQRES  24 E  493  HIS LEU HIS ARG ALA GLY ASN SER THR TYR SER ARG GLN
SEQRES  25 E  493  LYS ASN HIS GLY MET ASN PHE ARG VAL ILE CYS LYS TRP
SEQRES  26 E  493  MET ARG MET ALA GLY VAL ASP HIS ILE HIS ALA GLY THR
SEQRES  27 E  493  VAL VAL GLY LYS LEU GLU GLY ASP PRO ILE ILE THR ARG
SEQRES  28 E  493  GLY PHE TYR LYS THR LEU LEU LEU PRO LYS LEU GLU ARG
SEQRES  29 E  493  ASN LEU GLN GLU GLY LEU PHE PHE ASP MET GLU TRP ALA
SEQRES  30 E  493  SER LEU ARG LYS VAL MET PRO VAL ALA SER GLY GLY ILE
SEQRES  31 E  493  HIS ALA GLY GLN MET HIS GLN LEU ILE HIS TYR LEU GLY
SEQRES  32 E  493  GLU ASP VAL VAL LEU GLN PHE GLY GLY GLY THR ILE GLY
SEQRES  33 E  493  HIS PRO ASP GLY ILE GLN ALA GLY ALA THR ALA ASN ARG
SEQRES  34 E  493  VAL ALA LEU GLU ALA MET ILE LEU ALA ARG ASN GLU ASN
SEQRES  35 E  493  ARG ASP TYR LEU THR GLU GLY PRO GLU ILE LEU ARG GLU
SEQRES  36 E  493  ALA ALA LYS THR CYS GLY ALA LEU ARG THR ALA LEU ASP
SEQRES  37 E  493  LEU TRP LYS ASP ILE THR PHE ASN TYR THR SER THR ASP
SEQRES  38 E  493  THR SER ASP PHE VAL GLU THR PRO THR ALA ASN ILE
SEQRES   1 W  138  VAL ARG ILE THR GLN GLY THR PHE SER PHE LEU PRO ASP
SEQRES   2 W  138  LEU THR ASP GLU GLN ILE LYS LYS GLN ILE ASP TYR MET
SEQRES   3 W  138  ILE SER LYS LYS LEU ALA ILE GLY ILE GLU TYR THR ASN
SEQRES   4 W  138  ASP ILE HIS PRO ARG ASN ALA TYR TRP GLU ILE TRP GLY
SEQRES   5 W  138  LEU PRO LEU PHE ASP VAL THR ASP PRO ALA ALA VAL LEU
SEQRES   6 W  138  PHE GLU ILE ASN ALA CYS ARG LYS ALA ARG SER ASN PHE
SEQRES   7 W  138  TYR ILE LYS VAL VAL GLY PHE SER SER VAL ARG GLY ILE
SEQRES   8 W  138  GLU SER THR ILE ILE SER PHE ILE VAL ASN ARG PRO LYS
SEQRES   9 W  138  HIS GLU PRO GLY PHE ASN LEU MET ARG GLN GLU ASP LYS
SEQRES  10 W  138  SER ARG SER ILE LYS TYR THR ILE HIS SER TYR GLU SER
SEQRES  11 W  138  TYR LYS PRO GLU ASP GLU ARG TYR
SEQRES   1 G  493  MET SER GLN SER ILE GLU GLU LYS SER VAL GLN GLU ARG
SEQRES   2 G  493  THR ARG ILE LYS ASN SER ARG TYR GLU SER GLY VAL ILE
SEQRES   3 G  493  PRO TYR ALA LYS MET GLY TYR TRP ASN PRO ASP TYR GLN
SEQRES   4 G  493  VAL LYS ASP THR ASP VAL LEU ALA LEU PHE ARG VAL THR
SEQRES   5 G  493  PRO GLN PRO GLY VAL ASP PRO ILE GLU ALA ALA ALA ALA
SEQRES   6 G  493  VAL ALA GLY GLU SER SER THR ALA THR TRP THR VAL VAL
SEQRES   7 G  493  TRP THR ASP LEU LEU THR ALA ALA ASP LEU TYR ARG ALA
SEQRES   8 G  493  LYS ALA TYR LYS VAL ASP GLN VAL PRO ASN ASN PRO GLU
SEQRES   9 G  493  GLN TYR PHE ALA TYR ILE ALA TYR GLU LEU ASP LEU PHE
SEQRES  10 G  493  GLU GLU GLY SER ILE ALA ASN LEU THR ALA SER ILE ILE
SEQRES  11 G  493  GLY ASN VAL PHE GLY PHE LYS ALA VAL LYS ALA LEU ARG
SEQRES  12 G  493  LEU GLU ASP MET ARG LEU PRO LEU ALA TYR LEU LYS THR
SEQRES  13 G  493  PHE GLN GLY PRO ALA THR GLY VAL ILE LEU GLU ARG GLU
SEQRES  14 G  493  ARG LEU ASP LYS PHE GLY ARG PRO LEU LEU GLY CYS THR
SEQRES  15 G  493  THR LYS PRO LYS LEU GLY LEU SER GLY LYS ASN TYR GLY
SEQRES  16 G  493  ARG VAL VAL TYR GLU ALA LEU LYS GLY GLY LEU ASP PHE
SEQRES  17 G  493  VAL KCX ASP ASP GLU ASN ILE ASN SER GLN PRO PHE MET
SEQRES  18 G  493  ARG TRP ARG GLU ARG TYR LEU PHE THR MET GLU ALA VAL
SEQRES  19 G  493  ASN LYS ALA SER ALA ALA THR GLY GLU VAL LYS GLY HIS
SEQRES  20 G  493  TYR LEU ASN VAL THR ALA ALA THR MET GLU GLU MET TYR
SEQRES  21 G  493  ALA ARG ALA ASN PHE ALA LYS GLU LEU GLY SER VAL ILE
SEQRES  22 G  493  ILE MET ILE ASP LEU VAL ILE GLY TYR THR ALA ILE GLN
SEQRES  23 G  493  THR MET ALA LYS TRP ALA ARG ASP ASN ASP MET ILE LEU
SEQRES  24 G  493  HIS LEU HIS ARG ALA GLY ASN SER THR TYR SER ARG GLN
SEQRES  25 G  493  LYS ASN HIS GLY MET ASN PHE ARG VAL ILE CYS LYS TRP
SEQRES  26 G  493  MET ARG MET ALA GLY VAL ASP HIS ILE HIS ALA GLY THR
SEQRES  27 G  493  VAL VAL GLY LYS LEU GLU GLY ASP PRO ILE ILE THR ARG
SEQRES  28 G  493  GLY PHE TYR LYS THR LEU LEU LEU PRO LYS LEU GLU ARG
SEQRES  29 G  493  ASN LEU GLN GLU GLY LEU PHE PHE ASP MET GLU TRP ALA
SEQRES  30 G  493  SER LEU ARG LYS VAL MET PRO VAL ALA SER GLY GLY ILE
SEQRES  31 G  493  HIS ALA GLY GLN MET HIS GLN LEU ILE HIS TYR LEU GLY
SEQRES  32 G  493  GLU ASP VAL VAL LEU GLN PHE GLY GLY GLY THR ILE GLY
SEQRES  33 G  493  HIS PRO ASP GLY ILE GLN ALA GLY ALA THR ALA ASN ARG
SEQRES  34 G  493  VAL ALA LEU GLU ALA MET ILE LEU ALA ARG ASN GLU ASN
SEQRES  35 G  493  ARG ASP TYR LEU THR GLU GLY PRO GLU ILE LEU ARG GLU
SEQRES  36 G  493  ALA ALA LYS THR CYS GLY ALA LEU ARG THR ALA LEU ASP
SEQRES  37 G  493  LEU TRP LYS ASP ILE THR PHE ASN TYR THR SER THR ASP
SEQRES  38 G  493  THR SER ASP PHE VAL GLU THR PRO THR ALA ASN ILE
SEQRES   1 Y  138  VAL ARG ILE THR GLN GLY THR PHE SER PHE LEU PRO ASP
SEQRES   2 Y  138  LEU THR ASP GLU GLN ILE LYS LYS GLN ILE ASP TYR MET
SEQRES   3 Y  138  ILE SER LYS LYS LEU ALA ILE GLY ILE GLU TYR THR ASN
SEQRES   4 Y  138  ASP ILE HIS PRO ARG ASN ALA TYR TRP GLU ILE TRP GLY
SEQRES   5 Y  138  LEU PRO LEU PHE ASP VAL THR ASP PRO ALA ALA VAL LEU
SEQRES   6 Y  138  PHE GLU ILE ASN ALA CYS ARG LYS ALA ARG SER ASN PHE
SEQRES   7 Y  138  TYR ILE LYS VAL VAL GLY PHE SER SER VAL ARG GLY ILE
SEQRES   8 Y  138  GLU SER THR ILE ILE SER PHE ILE VAL ASN ARG PRO LYS
SEQRES   9 Y  138  HIS GLU PRO GLY PHE ASN LEU MET ARG GLN GLU ASP LYS
SEQRES  10 Y  138  SER ARG SER ILE LYS TYR THR ILE HIS SER TYR GLU SER
SEQRES  11 Y  138  TYR LYS PRO GLU ASP GLU ARG TYR
MODRES 1BWV KCX A  201  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 1BWV KCX C  201  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 1BWV KCX E  201  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 1BWV KCX G  201  LYS  LYSINE NZ-CARBOXYLIC ACID
HET    KCX  A 201      12
HET    KCX  C 201      12
HET    KCX  E 201      12
HET    KCX  G 201      12
HET     MG  A 490       1
HET     MG  C 490       1
HET     MG  E 490       1
HET     MG  G 490       1
HET    CAP  A 491      21
HET    CAP  C 491      21
HET    CAP  E 491      21
HET    CAP  G 491      21
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   *542(H2 O)
HELIX    1   1 PRO A   50  GLU A   60  1                                  11
HELIX    2   2 TRP A   70  LEU A   74  5                                   5
HELIX    3   3 ALA A   77  TYR A   80  1                                   4
HELIX    4   4 LEU A  105  LEU A  107  5                                   3
HELIX    5   5 ILE A  113  ILE A  120  1                                   8
HELIX    6   6 VAL A  124  GLY A  126  5                                   3
HELIX    7   7 LEU A  142  THR A  147  1                                   6
HELIX    8   8 GLY A  154  LEU A  162  1                                   9
HELIX    9   9 GLY A  182  GLY A  195  1                                  14
HELIX   10  10 TRP A  214  THR A  232  1                                  19
HELIX   11  11 MET A  247  GLU A  259  1                                  13
HELIX   12  12 LEU A  270  ILE A  272  5                                   3
HELIX   13  13 TYR A  274  ASN A  287  1                                  14
HELIX   14  14 ASN A  298  SER A  302  5                                   5
HELIX   15  15 PHE A  311  ALA A  321  1                                  11
HELIX   16  16 PRO A  339  LEU A  350  1                                  12
HELIX   17  17 MET A  387  LEU A  394  1                                   8
HELIX   18  18 GLY A  404  ILE A  407  1                                   4
HELIX   19  19 ILE A  413  ASN A  432  1                                  20
HELIX   20  20 TYR A  437  THR A  451  1                                  15
HELIX   21  21 GLY A  453  TRP A  462  1                                  10
HELIX   22  22 ASP S   23  SER S   35  1                                  13
HELIX   23  23 PRO S   80  ALA S   93  1                                  14
HELIX   24  24 TYR S  145  TYR S  148  5                                   4
HELIX   25  25 GLU S  151  GLU S  153  5                                   3
HELIX   26  26 PRO C   50  GLU C   60  1                                  11
HELIX   27  27 TRP C   70  LEU C   74  5                                   5
HELIX   28  28 ALA C   77  TYR C   80  1                                   4
HELIX   29  29 LEU C  105  LEU C  107  5                                   3
HELIX   30  30 ILE C  113  ILE C  120  1                                   8
HELIX   31  31 VAL C  124  GLY C  126  5                                   3
HELIX   32  32 LEU C  142  THR C  147  1                                   6
HELIX   33  33 GLY C  154  LEU C  162  1                                   9
HELIX   34  34 GLY C  182  GLY C  195  1                                  14
HELIX   35  35 TRP C  214  THR C  232  1                                  19
HELIX   36  36 MET C  247  GLU C  259  1                                  13
HELIX   37  37 LEU C  270  ILE C  272  5                                   3
HELIX   38  38 TYR C  274  ASP C  286  1                                  13
HELIX   39  39 ASN C  298  SER C  302  5                                   5
HELIX   40  40 PHE C  311  ALA C  321  1                                  11
HELIX   41  41 PRO C  339  LEU C  350  1                                  12
HELIX   42  42 MET C  387  LEU C  394  1                                   8
HELIX   43  43 GLY C  404  ILE C  407  1                                   4
HELIX   44  44 ILE C  413  ASN C  432  1                                  20
HELIX   45  45 TYR C  437  THR C  451  1                                  15
HELIX   46  46 GLY C  453  TRP C  462  1                                  10
HELIX   47  47 ASP U   23  SER U   35  1                                  13
HELIX   48  48 PRO U   80  ALA U   93  1                                  14
HELIX   49  49 TYR U  145  TYR U  148  5                                   4
HELIX   50  50 GLU U  151  GLU U  153  5                                   3
HELIX   51  51 PRO E   50  GLU E   60  1                                  11
HELIX   52  52 TRP E   70  LEU E   74  5                                   5
HELIX   53  53 ALA E   77  TYR E   80  1                                   4
HELIX   54  54 LEU E  105  LEU E  107  5                                   3
HELIX   55  55 ILE E  113  ILE E  120  1                                   8
HELIX   56  56 VAL E  124  GLY E  126  5                                   3
HELIX   57  57 LEU E  142  THR E  147  1                                   6
HELIX   58  58 GLY E  154  LEU E  162  1                                   9
HELIX   59  59 GLY E  182  GLY E  195  1                                  14
HELIX   60  60 TRP E  214  THR E  232  1                                  19
HELIX   61  61 MET E  247  GLU E  259  1                                  13
HELIX   62  62 LEU E  270  ILE E  272  5                                   3
HELIX   63  63 TYR E  274  ASN E  287  1                                  14
HELIX   64  64 ASN E  298  SER E  302  5                                   5
HELIX   65  65 PHE E  311  ALA E  321  1                                  11
HELIX   66  66 PRO E  339  LEU E  350  1                                  12
HELIX   67  67 MET E  387  LEU E  394  1                                   8
HELIX   68  68 GLY E  404  ILE E  407  1                                   4
HELIX   69  69 ILE E  413  ASN E  432  1                                  20
HELIX   70  70 TYR E  437  THR E  451  1                                  15
HELIX   71  71 GLY E  453  TRP E  462  1                                  10
HELIX   72  72 ASP W   23  SER W   35  1                                  13
HELIX   73  73 PRO W   80  ALA W   93  1                                  14
HELIX   74  74 TYR W  145  TYR W  148  5                                   4
HELIX   75  75 GLU W  151  GLU W  153  5                                   3
HELIX   76  76 PRO G   50  GLU G   60  1                                  11
HELIX   77  77 TRP G   70  LEU G   74  5                                   5
HELIX   78  78 ALA G   77  TYR G   80  1                                   4
HELIX   79  79 LEU G  105  LEU G  107  5                                   3
HELIX   80  80 ILE G  113  ILE G  120  1                                   8
HELIX   81  81 VAL G  124  GLY G  126  5                                   3
HELIX   82  82 LEU G  142  THR G  147  1                                   6
HELIX   83  83 GLY G  154  LEU G  162  1                                   9
HELIX   84  84 GLY G  182  GLY G  195  1                                  14
HELIX   85  85 TRP G  214  THR G  232  1                                  19
HELIX   86  86 MET G  247  GLU G  259  1                                  13
HELIX   87  87 LEU G  270  ILE G  272  5                                   3
HELIX   88  88 TYR G  274  ASP G  286  1                                  13
HELIX   89  89 ASN G  298  SER G  302  5                                   5
HELIX   90  90 PHE G  311  ALA G  321  1                                  11
HELIX   91  91 PRO G  339  LEU G  350  1                                  12
HELIX   92  92 MET G  387  LEU G  394  1                                   8
HELIX   93  93 GLY G  404  ILE G  407  1                                   4
HELIX   94  94 ILE G  413  ASN G  432  1                                  20
HELIX   95  95 TYR G  437  THR G  451  1                                  15
HELIX   96  96 GLY G  453  TRP G  462  1                                  10
HELIX   97  97 ASP Y   23  SER Y   35  1                                  13
HELIX   98  98 PRO Y   80  ALA Y   93  1                                  14
HELIX   99  99 TYR Y  145  TYR Y  148  5                                   4
HELIX  100 100 GLU Y  151  GLU Y  153  5                                   3
SHEET    1   A 4 ALA A 132  ARG A 139  0
SHEET    2   A 4 VAL A  36  THR A  43 -1  N  THR A  43   O  ALA A 132
SHEET    3   A 4 GLN A  96  TYR A 103 -1  N  TYR A 103   O  VAL A  36
SHEET    4   A 4 LYS A  83  GLN A  89 -1  N  ASP A  88   O  PHE A  98
SHEET    1   B 4 LEU A 169  GLY A 171  0
SHEET    2   B 4 VAL A 398  GLN A 401  1  N  LEU A 400   O  LEU A 169
SHEET    3   B 4 MET 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  MET A 375
SHEET    1   C 2 ILE A 264  ASP A 268  0
SHEET    2   C 2 ILE A 290  HIS A 294  1  N  ILE A 290   O  ILE A 265
SHEET    1   D 3 ALA S  39  THR S  45  0
SHEET    2   D 3 TYR S  98  PHE S 104 -1  N  PHE S 104   O  ALA S  39
SHEET    3   D 3 ILE S 113  ASN S 118 -1  N  ASN S 118   O  ILE S  99
SHEET    1   E 2 PHE S 126  GLU S 132  0
SHEET    2   E 2 ILE S 138  SER S 144 -1  N  HIS S 143   O  ASN S 127
SHEET    1   F 4 ALA C 132  ARG C 139  0
SHEET    2   F 4 VAL C  36  THR C  43 -1  N  THR C  43   O  ALA C 132
SHEET    3   F 4 GLN C  96  TYR C 103 -1  N  TYR C 103   O  VAL C  36
SHEET    4   F 4 LYS C  83  GLN C  89 -1  N  ASP C  88   O  PHE C  98
SHEET    1   G 4 LEU C 169  GLY C 171  0
SHEET    2   G 4 VAL C 398  GLN C 401  1  N  LEU C 400   O  LEU C 169
SHEET    3   G 4 MET C 375  SER C 379  1  N  PRO C 376   O  VAL C 399
SHEET    4   G 4 HIS C 325  HIS C 327  1  N  ILE C 326   O  MET C 375
SHEET    1   H 2 ILE C 264  ASP C 268  0
SHEET    2   H 2 ILE C 290  HIS C 294  1  N  ILE C 290   O  ILE C 265
SHEET    1   I 3 ALA U  39  THR U  45  0
SHEET    2   I 3 TYR U  98  PHE U 104 -1  N  PHE U 104   O  ALA U  39
SHEET    3   I 3 ILE U 113  ASN U 118 -1  N  ASN U 118   O  ILE U  99
SHEET    1   J 2 PHE U 126  GLU U 132  0
SHEET    2   J 2 ILE U 138  SER U 144 -1  N  HIS U 143   O  ASN U 127
SHEET    1   K 4 ALA E 132  ARG E 139  0
SHEET    2   K 4 VAL E  36  THR E  43 -1  N  THR E  43   O  ALA E 132
SHEET    3   K 4 GLN E  96  TYR E 103 -1  N  TYR E 103   O  VAL E  36
SHEET    4   K 4 LYS E  83  GLN E  89 -1  N  ASP E  88   O  PHE E  98
SHEET    1   L 4 LEU E 169  GLY E 171  0
SHEET    2   L 4 VAL E 398  GLN E 401  1  N  LEU E 400   O  LEU E 169
SHEET    3   L 4 MET E 375  SER E 379  1  N  PRO E 376   O  VAL E 399
SHEET    4   L 4 HIS E 325  HIS E 327  1  N  ILE E 326   O  MET E 375
SHEET    1   M 2 ILE E 264  ASP E 268  0
SHEET    2   M 2 ILE E 290  HIS E 294  1  N  ILE E 290   O  ILE E 265
SHEET    1   N 3 ALA W  39  THR W  45  0
SHEET    2   N 3 TYR W  98  PHE W 104 -1  N  PHE W 104   O  ALA W  39
SHEET    3   N 3 ILE W 113  ASN W 118 -1  N  ASN W 118   O  ILE W  99
SHEET    1   O 2 PHE W 126  GLU W 132  0
SHEET    2   O 2 ILE W 138  SER W 144 -1  N  HIS W 143   O  ASN W 127
SHEET    1   P 4 ALA G 132  ARG G 139  0
SHEET    2   P 4 VAL G  36  THR G  43 -1  N  THR G  43   O  ALA G 132
SHEET    3   P 4 GLN G  96  TYR G 103 -1  N  TYR G 103   O  VAL G  36
SHEET    4   P 4 LYS G  83  GLN G  89 -1  N  ASP G  88   O  PHE G  98
SHEET    1   Q 4 LEU G 169  GLY G 171  0
SHEET    2   Q 4 VAL G 398  GLN G 401  1  N  LEU G 400   O  LEU G 169
SHEET    3   Q 4 MET G 375  SER G 379  1  N  PRO G 376   O  VAL G 399
SHEET    4   Q 4 HIS G 325  HIS G 327  1  N  ILE G 326   O  MET G 375
SHEET    1   R 2 ILE G 264  ASP G 268  0
SHEET    2   R 2 ILE G 290  HIS G 294  1  N  ILE G 290   O  ILE G 265
SHEET    1   S 3 ALA Y  39  THR Y  45  0
SHEET    2   S 3 TYR Y  98  PHE Y 104 -1  N  PHE Y 104   O  ALA Y  39
SHEET    3   S 3 ILE Y 113  ASN Y 118 -1  N  ASN Y 118   O  ILE Y  99
SHEET    1   T 2 PHE Y 126  GLU Y 132  0
SHEET    2   T 2 ILE Y 138  SER Y 144 -1  N  HIS Y 143   O  ASN Y 127
LINK         OQ1 KCX A 201                MG    MG A 490     1555   1555  2.20
LINK        MG    MG A 490                 O2  CAP A 491     1555   1555  2.24
LINK        MG    MG A 490                 O3  CAP A 491     1555   1555  2.13
LINK        MG    MG A 490                 O7  CAP A 491     1555   1555  2.30
LINK         OQ1 KCX C 201                MG    MG C 490     1555   1555  2.20
LINK        MG    MG C 490                 OD1 ASP C 203     1555   1555  2.39
LINK        MG    MG C 490                 O2  CAP C 491     1555   1555  2.19
LINK        MG    MG C 490                 O3  CAP C 491     1555   1555  2.10
LINK        MG    MG C 490                 O7  CAP C 491     1555   1555  2.33
LINK         OQ1 KCX E 201                MG    MG E 490     1555   1555  2.28
LINK        MG    MG E 490                 O2  CAP E 491     1555   1555  2.27
LINK        MG    MG E 490                 O3  CAP E 491     1555   1555  2.18
LINK        MG    MG E 490                 O7  CAP E 491     1555   1555  2.30
LINK         OQ1 KCX G 201                MG    MG G 490     1555   1555  2.24
LINK        MG    MG G 490                 O2  CAP G 491     1555   1555  2.13
LINK        MG    MG G 490                 O3  CAP G 491     1555   1555  2.09
LINK        MG    MG G 490                 O7  CAP G 491     1555   1555  2.35
LINK         C   VAL A 200                 N   KCX A 201     1555   1555  1.33
LINK         C   KCX A 201                 N   ASP A 202     1555   1555  1.33
LINK        MG    MG A 490                 OE1 GLU A 204     1555   1555  2.50
LINK        MG    MG A 490                 OD1 ASP A 203     1555   1555  2.52
LINK        MG    MG A 490                 OQ2 KCX A 201     1555   1555  2.98
LINK         C   VAL C 200                 N   KCX C 201     1555   1555  1.33
LINK         C   KCX C 201                 N   ASP C 202     1555   1555  1.33
LINK        MG    MG C 490                 OE1 GLU C 204     1555   1555  2.46
LINK        MG    MG C 490                 OQ2 KCX C 201     1555   1555  2.99
LINK         C   VAL E 200                 N   KCX E 201     1555   1555  1.33
LINK         C   KCX E 201                 N   ASP E 202     1555   1555  1.33
LINK        MG    MG E 490                 OQ2 KCX E 201     1555   1555  2.84
LINK        MG    MG E 490                 OE1 GLU E 204     1555   1555  2.44
LINK        MG    MG E 490                 OD1 ASP E 203     1555   1555  2.69
LINK         C   VAL G 200                 N   KCX G 201     1555   1555  1.33
LINK         C   KCX G 201                 N   ASP G 202     1555   1555  1.33
LINK        MG    MG G 490                 OQ2 KCX G 201     1555   1555  2.96
LINK        MG    MG G 490                 OE1 GLU G 204     1555   1555  2.63
LINK        MG    MG G 490                 OD1 ASP G 203     1555   1555  2.47
CISPEP   1 LYS A  175    PRO A  176          0         2.64
CISPEP   2 LYS C  175    PRO C  176          0         1.87
CISPEP   3 LYS E  175    PRO E  176          0         2.56
CISPEP   4 LYS G  175    PRO G  176          0         2.18
SITE     1 MGA  4 KCX A 201  ASP A 203  GLU A 204  CAP A 491
SITE     1 MGC  4 KCX E 201  ASP E 203  GLU E 204  CAP C 491
SITE     1 MGE  4 KCX E 201  ASP E 203  GLU E 204  CAP E 491
SITE     1 MGG  4 KCX G 201  ASP G 203  GLU G 204  CAP G 491
SITE     1 AC1  4 KCX A 201  ASP A 203  GLU A 204  CAP A 491
SITE     1 AC2  4 KCX C 201  ASP C 203  GLU C 204  CAP C 491
SITE     1 AC3  4 KCX E 201  ASP E 203  GLU E 204  CAP E 491
SITE     1 AC4  5 THR G 173  KCX G 201  ASP G 203  GLU G 204
SITE     2 AC4  5 CAP G 491
SITE     1 AC5 27 THR A 173  LYS A 175  LYS A 177  KCX A 201
SITE     2 AC5 27 ASP A 203  GLU A 204  HIS A 294  ARG A 295
SITE     3 AC5 27 HIS A 327  LYS A 334  LEU A 335  SER A 379
SITE     4 AC5 27 GLY A 380  GLY A 381  GLY A 403  GLY A 404
SITE     5 AC5 27  MG A 490  HOH A 518  HOH A 554  HOH A 561
SITE     6 AC5 27 HOH A 565  HOH A 572  HOH A 584  GLU C  60
SITE     7 AC5 27 THR C  65  TRP C  66  ASN C 123
SITE     1 AC6 26 GLU A  60  THR A  65  TRP A  66  ASN A 123
SITE     2 AC6 26 THR C 173  LYS C 175  LYS C 177  KCX C 201
SITE     3 AC6 26 ASP C 203  GLU C 204  HIS C 294  ARG C 295
SITE     4 AC6 26 HIS C 327  LYS C 334  LEU C 335  SER C 379
SITE     5 AC6 26 GLY C 380  GLY C 381  GLY C 403  GLY C 404
SITE     6 AC6 26  MG C 490  HOH C 525  HOH C 555  HOH C 564
SITE     7 AC6 26 HOH C 575  HOH C 580
SITE     1 AC7 27 THR E 173  LYS E 175  LYS E 177  KCX E 201
SITE     2 AC7 27 ASP E 203  GLU E 204  HIS E 294  ARG E 295
SITE     3 AC7 27 HIS E 327  LYS E 334  LEU E 335  SER E 379
SITE     4 AC7 27 GLY E 380  GLY E 381  GLY E 403  GLY E 404
SITE     5 AC7 27  MG E 490  HOH E 520  HOH E 555  HOH E 562
SITE     6 AC7 27 HOH E 566  HOH E 572  HOH E 580  GLU G  60
SITE     7 AC7 27 THR G  65  TRP G  66  ASN G 123
SITE     1 AC8 26 GLU E  60  THR E  65  TRP E  66  ASN E 123
SITE     2 AC8 26 THR G 173  LYS G 175  LYS G 177  KCX G 201
SITE     3 AC8 26 ASP G 203  GLU G 204  HIS G 294  ARG G 295
SITE     4 AC8 26 HIS G 327  LYS G 334  LEU G 335  SER G 379
SITE     5 AC8 26 GLY G 380  GLY G 381  GLY G 403  GLY G 404
SITE     6 AC8 26  MG G 490  HOH G 525  HOH G 555  HOH G 564
SITE     7 AC8 26 HOH G 577  HOH G 581
CRYST1  117.070  117.070  319.630  90.00  90.00 120.00 P 64         24
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      0.008542  0.004932  0.000000        0.00000
SCALE2      0.000000  0.009863  0.000000        0.00000
SCALE3      0.000000  0.000000  0.003129        0.00000
MTRIX1   1 -0.500118  0.865957  0.000014        0.00070    1
MTRIX2   1  0.865957  0.500118  0.000008       -0.00480    1
MTRIX3   1  0.000000  0.000016 -1.000000      -34.62590    1
MTRIX1   2  0.251408  0.432654 -0.865797      -15.02590    1
MTRIX2   2  0.431980  0.750334  0.500392        8.70380    1
MTRIX3   2  0.866134 -0.499809  0.001742      -17.22490    1
MTRIX1   3 -0.500062  0.865990 -0.000004       -0.00340    1
MTRIX2   3  0.865990  0.500062  0.000092        0.00130    1
MTRIX3   3  0.000081  0.000042 -1.000000      -34.62650    1
MTRIX1   4  0.248883  0.434033  0.865836       14.95330    1
MTRIX2   4  0.433806  0.749325 -0.500325       -8.62350    1
MTRIX3   4 -0.865950  0.500127 -0.001792      -17.28890    1
MTRIX1   5 -0.500229  0.865893  0.000498       -0.00480    1
MTRIX2   5  0.865893  0.500228 -0.000548       -0.02520    1
MTRIX3   5 -0.000225 -0.000706 -1.000000      -34.58960    1
MTRIX1   6  0.251848  0.433964 -0.865014      -15.02790    1
MTRIX2   6  0.433250  0.748694  0.501748        8.73400    1
MTRIX3   6  0.865371 -0.501131  0.000542      -17.23000    1
MTRIX1   7 -0.500199  0.865910  0.000072       -0.00050    1
MTRIX2   7  0.865910  0.500199 -0.000070        0.00400    1
MTRIX3   7 -0.000096  0.000027 -1.000000      -34.62190    1
MTRIX1   8  0.249883  0.435122  0.865001       14.92200    1
MTRIX2   8  0.431542  0.749666 -0.501769       -8.63470    1
MTRIX3   8 -0.866793  0.498668 -0.000445      -17.25120    1
      
PROCHECK
Go to PROCHECK summary
 References