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PDBsum entry 1upp

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
1upp
Jmol
Contents
Protein chains
467 a.a. *
123 a.a. *
Ligands
CAP ×4
Metals
_CA ×4
Waters ×664
* Residue conservation analysis
HEADER    LYASE                                   09-OCT-03   1UPP
TITLE     SPINACH RUBISCO IN COMPLEX WITH 2-CARBOXYARABINITOL 2
TITLE    2 BISPHOSPHATE AND CALCIUM.
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN;
COMPND   3 CHAIN: A, C, E, G;
COMPND   4 SYNONYM: RIBULOSE BISPHOSPHATE CARBOXYLASE/OXYGENASE,
COMPND   5  RUBISCO LARGE SUBUNIT;
COMPND   6 EC: 4.1.1.39;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN;
COMPND   9 CHAIN: I, J, K, L;
COMPND  10 SYNONYM: RIBULOSE BISPHOSPHATE CARBOXYLASE/OXYGENASE,
COMPND  11  RUBISCO SMALL SUBUNIT;
COMPND  12 EC: 4.1.1.39;
COMPND  13 OTHER_DETAILS: THIS IS THE SECOND STRUCTURE OF THIS
COMPND  14  COMPLEX THAT IS BEING SUBMITTED. THE PREVOUS STRUCTURE,
COMPND  15  PDB ID CODE 1UPM, WAS OBTAINED FROM A CRYSTAL OF
COMPND  16  RUBISCO-CA COOCRYSTALLIZED WITH 2-CABP WHERAS THIS
COMPND  17  STRUCTURE IS FROM A RUBISCO-CA/3PGA CRYSTAL WHICH WAS
COMPND  18  SOAKED WITH 2-CABP
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SPINACIA OLERACEA;
SOURCE   3 ORGANISM_COMMON: SPINACH;
SOURCE   4 ORGANISM_TAXID: 3562;
SOURCE   5 ORGAN: LEAF;
SOURCE   6 MOL_ID: 2;
SOURCE   7 ORGANISM_SCIENTIFIC: SPINACIA OLERACEA;
SOURCE   8 ORGANISM_COMMON: SPINACH;
SOURCE   9 ORGANISM_TAXID: 3562;
SOURCE  10 ORGAN: LEAF
KEYWDS    LYASE, CARBON-CARBON, OXIDOREDUCTASE, PHOTOSYNTHESIS,
KEYWDS   2 CARBON-DIOXIDE FIXATION
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.KARKEHABADI,T.C.TAYLOR,I.ANDERSSON
REVDAT   3   24-FEB-09 1UPP    1       VERSN
REVDAT   2   26-MAY-05 1UPP    1       JRNL
REVDAT   1   14-OCT-03 1UPP    0
JRNL        AUTH   S.KAREHABADI,T.C.TAYLOR,I.ANDERSSON
JRNL        TITL   CALCIUM SUPPORTS LOOP CLOSURE BUT NOT CATALYSIS IN
JRNL        TITL 2 RUBISCO
JRNL        REF    J.MOL.BIOL.                   V. 334    65 2003
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   14596800
JRNL        DOI    10.1016/J.JMB.2003.09.025
REMARK   2
REMARK   2 RESOLUTION.    2.3  ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.3
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 100
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 4
REMARK   3   COMPLETENESS FOR RANGE        (%) : 76.1
REMARK   3   NUMBER OF REFLECTIONS             : 102132
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 + TEST SET) : 0.25862
REMARK   3   R VALUE            (WORKING SET) : 0.25598
REMARK   3   FREE R VALUE                     : 0.30710
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1
REMARK   3   FREE R VALUE TEST SET COUNT      : 5500
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 18704
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 136
REMARK   3   SOLVENT ATOMS            : 664
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.364
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.10
REMARK   3    B22 (A**2) : -0.44
REMARK   3    B33 (A**2) : 0.54
REMARK   3    B12 (A**2) : 0.00
REMARK   3    B13 (A**2) : 0.00
REMARK   3    B23 (A**2) : 0.00
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.539
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.314
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.254
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.449
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL
REMARK   3
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: THE DATA IS FROM A MEROHEDRALLY
REMARK   3  TWINNED CRYSTAL
REMARK   4
REMARK   4 1UPP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  09-OCT-03.
REMARK 100 THE PDBE ID CODE IS EBI-13677.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-MAY-00
REMARK 200  TEMPERATURE           (KELVIN) : 279.0
REMARK 200  PH                             : 7.80
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-4
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9386
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 108187
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 76.1
REMARK 200  DATA REDUNDANCY                : 17.400
REMARK 200  R MERGE                    (I) : 0.07600
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 13.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.12
REMARK 200  COMPLETENESS FOR SHELL     (%) : 70.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.26000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS  (%): 40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.1
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 4000, 0.1M HEPES PH
REMARK 280  7.8, 10 MM CACL2, 0.2 M NACL, 50 MM NAHCO3, 0.1 M 3PGA
REMARK 280  THEN SOAKED IN 2-CABP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       99.87500
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       99.87500
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       77.94000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       78.12500
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       77.94000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       78.12500
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       99.87500
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       77.94000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       78.12500
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       99.87500
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       77.94000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       78.12500
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXADECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, G, I, L, E, J, K
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       99.87500
REMARK 400
REMARK 400 COMPOUND
REMARK 400  RUBISCO CATALYZES THE CARBOXYLATION OF D-RIBULOSE 1,5-
REMARK 400  BISPHOSPHATE AS WELL AS THE OXIDATIVE FRAGMENTATION OF
REMARK 400  PENTOSE SUBSTRATE IN PHOTORESPIRATION. THE PROTEIN IS A
REMARK 400  COMPLEX OF 8 LARGE AND 8 SMALL CHAINS.
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     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     MET E     1
REMARK 465     SER E     2
REMARK 465     PRO E     3
REMARK 465     GLN E     4
REMARK 465     THR E     5
REMARK 465     GLU E     6
REMARK 465     THR E     7
REMARK 465     LYS E     8
REMARK 465     MET G     1
REMARK 465     SER G     2
REMARK 465     PRO G     3
REMARK 465     GLN G     4
REMARK 465     THR G     5
REMARK 465     GLU G     6
REMARK 465     THR G     7
REMARK 465     LYS G     8
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   CD   LYS A   177  -  O    HOH A  2040              2.10
REMARK 500   NZ   LYS A   177  -  O    HOH A  2040              2.19
REMARK 500   N    ALA C   276  -  O    HOH C  2077              2.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500
REMARK 500   OD1  ASP L    24     NH2  ARG L    28     4555      2.05
REMARK 500   NH2  ARG L    28     OD1  ASP L    24     4555      2.05
REMARK 500   O    HOH G  2077     O    HOH G  2077     3555      1.65
REMARK 500   O    HOH G  2081     O    HOH G  2081     3555      1.89
REMARK 500   O    HOH G  2086     O    HOH G  2086     3555      2.12
REMARK 500
REMARK 500 REMARK: NULL
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    PRO C 176   N     PRO C 176   CD      0.106
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    TYR A 100   CB  -  CG  -  CD1 ANGL. DEV. =   4.0 DEGREES
REMARK 500    TYR A 100   CB  -  CG  -  CD2 ANGL. DEV. =  -3.9 DEGREES
REMARK 500    GLU A 109   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.7 DEGREES
REMARK 500    SER A 119   O   -  C   -  N   ANGL. DEV. = -11.5 DEGREES
REMARK 500    ARG A 131   CD  -  NE  -  CZ  ANGL. DEV. =  17.1 DEGREES
REMARK 500    ARG A 134   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES
REMARK 500    ARG A 134   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES
REMARK 500    ALA A 143   CB  -  CA  -  C   ANGL. DEV. =   9.7 DEGREES
REMARK 500    TYR A 144   CB  -  CG  -  CD1 ANGL. DEV. =   3.7 DEGREES
REMARK 500    ARG A 167   CD  -  NE  -  CZ  ANGL. DEV. =  14.5 DEGREES
REMARK 500    PRO A 176   C   -  N   -  CA  ANGL. DEV. =  11.0 DEGREES
REMARK 500    LYS A 177   CB  -  CG  -  CD  ANGL. DEV. = -24.5 DEGREES
REMARK 500    ARG A 187   CD  -  NE  -  CZ  ANGL. DEV. =  11.2 DEGREES
REMARK 500    ARG A 187   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES
REMARK 500    ARG A 194   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.9 DEGREES
REMARK 500    ASP A 203   CB  -  CG  -  OD1 ANGL. DEV. = -10.1 DEGREES
REMARK 500    ASP A 203   CB  -  CG  -  OD2 ANGL. DEV. =  12.5 DEGREES
REMARK 500    GLU A 204   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.1 DEGREES
REMARK 500    ARG A 215   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ASP A 216   CB  -  CG  -  OD1 ANGL. DEV. =   7.0 DEGREES
REMARK 500    ARG A 217   CG  -  CD  -  NE  ANGL. DEV. =  18.6 DEGREES
REMARK 500    ARG A 217   NE  -  CZ  -  NH2 ANGL. DEV. =   3.0 DEGREES
REMARK 500    GLU A 231   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.3 DEGREES
REMARK 500    HIS A 238   CG  -  ND1 -  CE1 ANGL. DEV. =   9.1 DEGREES
REMARK 500    HIS A 238   ND1 -  CE1 -  NE2 ANGL. DEV. =  -7.9 DEGREES
REMARK 500    CYS A 247   CA  -  CB  -  SG  ANGL. DEV. = -10.7 DEGREES
REMARK 500    ASP A 249   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES
REMARK 500    TYR A 269   CA  -  CB  -  CG  ANGL. DEV. =  11.7 DEGREES
REMARK 500    TYR A 283   CB  -  CG  -  CD2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    ARG A 285   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES
REMARK 500    ARG A 295   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES
REMARK 500    VAL A 300   CA  -  CB  -  CG1 ANGL. DEV. =  11.6 DEGREES
REMARK 500    ARG A 303   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES
REMARK 500    ARG A 303   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.7 DEGREES
REMARK 500    ARG A 312   NE  -  CZ  -  NH1 ANGL. DEV. =   6.5 DEGREES
REMARK 500    ARG A 312   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES
REMARK 500    ASP A 324   CB  -  CG  -  OD1 ANGL. DEV. =  -7.1 DEGREES
REMARK 500    ARG A 350   NE  -  CZ  -  NH1 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ARG A 350   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES
REMARK 500    ASP A 357   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ARG A 360   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ASP A 396   CB  -  CG  -  OD1 ANGL. DEV. =   6.6 DEGREES
REMARK 500    ASP A 397   CB  -  CG  -  OD1 ANGL. DEV. =   9.2 DEGREES
REMARK 500    ASP A 397   CB  -  CG  -  OD2 ANGL. DEV. =   7.2 DEGREES
REMARK 500    ASP A 397   OD1 -  CG  -  OD2 ANGL. DEV. = -16.3 DEGREES
REMARK 500    TYR C  25   CB  -  CG  -  CD2 ANGL. DEV. =   4.1 DEGREES
REMARK 500    ASP C  35   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES
REMARK 500    ASP C  35   CB  -  CG  -  OD2 ANGL. DEV. =  -7.4 DEGREES
REMARK 500    ARG C  41   NE  -  CZ  -  NH2 ANGL. DEV. =   4.1 DEGREES
REMARK 500    TYR C 103   CB  -  CG  -  CD2 ANGL. DEV. =   4.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS     221 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 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    SER A  62      -79.69   -146.42
REMARK 500    ASN A 163       41.12     71.81
REMARK 500    CYS A 172      118.99   -173.58
REMARK 500    PRO A 176      120.96      8.46
REMARK 500    ASN A 207      -96.83   -118.42
REMARK 500    MET A 212      107.78   -169.34
REMARK 500    MET A 297      -13.48     92.72
REMARK 500    VAL A 331      -54.68     86.93
REMARK 500    LYS A 356      138.99    -36.07
REMARK 500    ASP A 357       88.78   -166.59
REMARK 500    VAL A 369       51.79     34.69
REMARK 500    HIS A 409      129.60    -37.97
REMARK 500    SER C  62      -84.35   -143.34
REMARK 500    THR C  65     -158.55   -131.75
REMARK 500    CYS C 172      114.87   -169.40
REMARK 500    ASN C 207      -90.81   -118.25
REMARK 500    MET C 212      115.05   -161.98
REMARK 500    MET C 297       -9.98     87.78
REMARK 500    VAL C 331      -48.43     76.71
REMARK 500    LYS C 356      138.89    -37.06
REMARK 500    ASP C 357       86.89   -164.37
REMARK 500    VAL C 369       54.18     38.94
REMARK 500    SER C 370       16.06     55.09
REMARK 500    SER E  62      -80.83   -148.70
REMARK 500    THR E  75     -169.40   -110.42
REMARK 500    PRO E 176      115.28      5.61
REMARK 500    ASN E 207      -90.40   -121.64
REMARK 500    MET E 212      107.62   -162.58
REMARK 500    MET E 297      -19.22     90.92
REMARK 500    VAL E 331      -51.39     85.71
REMARK 500    LYS E 356      137.40    -39.27
REMARK 500    VAL E 369       62.83     26.48
REMARK 500    SER E 370       14.03     59.88
REMARK 500    SER G  62      -80.04   -139.04
REMARK 500    THR G  65     -156.64   -130.22
REMARK 500    ASN G 163       39.68     74.37
REMARK 500    CYS G 172      115.86   -167.78
REMARK 500    PRO G 176      115.39     17.82
REMARK 500    ASN G 207      -99.15   -116.09
REMARK 500    MET G 212      110.90   -161.05
REMARK 500    MET G 297      -10.88     88.30
REMARK 500    VAL G 331      -56.12     79.98
REMARK 500    ASP G 357       92.48   -162.99
REMARK 500    THR G 406      -66.01    -97.48
REMARK 500    GLU I  13     -154.50     61.23
REMARK 500    LEU I  15       -9.58     97.84
REMARK 500    ASP I  47      -69.60    -94.50
REMARK 500    LYS I  71     -133.66     54.86
REMARK 500    GLU J  13     -155.02     73.38
REMARK 500    LEU J  15      -11.57    102.82
REMARK 500    PRO J  20      141.45    -37.40
REMARK 500    ASP J  47      -70.80    -92.51
REMARK 500    LYS J  71     -135.82     62.83
REMARK 500    SER J 114      118.79   -170.53
REMARK 500    GLU K  13     -153.76     69.97
REMARK 500    LEU K  15      -12.56     97.58
REMARK 500    ASP K  47      -68.06    -96.35
REMARK 500    LYS K  71     -136.95     50.00
REMARK 500    SER K 114      115.96   -167.76
REMARK 500    TYR K 118      128.11   -172.39
REMARK 500    GLU L  13     -149.59     64.00
REMARK 500    LEU L  15      -13.80    102.40
REMARK 500    ASP L  47      -68.31    -91.43
REMARK 500    TRP L  67     -167.57   -105.18
REMARK 500    LYS L  71     -143.32     58.52
REMARK 500    SER L 114      115.68   -172.19
REMARK 500
REMARK 500 REMARK: NULL
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 LYS A  175     PRO A  176                  -79.09
REMARK 500 LYS E  175     PRO E  176                  -80.07
REMARK 500 LYS G  175     PRO G  176                  -85.52
REMARK 500 KCX G  201     ASP G  202                  146.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    THR A 330         10.30
REMARK 500    LYS C 175         25.40
REMARK 500    THR E 243        -10.19
REMARK 500    PRO G 152         10.63
REMARK 500    LYS I  11         10.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    SER A 370        24.9      L          L   OUTSIDE RANGE
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 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                              CA A 476  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP A 477   O2
REMARK 620 2 CAP A 477   O6   69.4
REMARK 620 3 GLU A 204   OE1 150.2  96.2
REMARK 620 4 CAP A 477   O3   62.9  81.9  90.0
REMARK 620 5 KCX A 201   OQ2  95.7 163.1  93.3  84.2
REMARK 620 6 ASP A 203   OD1 128.9 103.6  78.9 168.0  91.9
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA C 476  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP C 477   O2
REMARK 620 2 CAP C 477   O6   67.0
REMARK 620 3 KCX C 201   OQ2  95.0 158.5
REMARK 620 4 ASP C 203   OD1 123.1  99.6 100.2
REMARK 620 5 GLU C 204   OE1 149.0  95.2  95.3  83.6
REMARK 620 6 CAP C 477   O3   59.3  80.5  80.0 177.5  93.9
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA E 476  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP E 477   O2
REMARK 620 2 KCX E 201   OQ2  94.6
REMARK 620 3 ASP E 203   OD1 126.8  91.2
REMARK 620 4 GLU E 204   OE1 147.8  95.9  83.3
REMARK 620 5 CAP E 477   O3   58.6  84.7 173.6  92.2
REMARK 620 6 CAP E 477   O6   67.8 161.6 103.6  96.7  81.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA G 476  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP G 477   O2
REMARK 620 2 CAP G 477   O6   66.2
REMARK 620 3 GLU G 204   OE1 151.2 103.4
REMARK 620 4 CAP G 477   O3   61.4  84.0  91.7
REMARK 620 5 KCX G 201   OQ2  93.8 160.0  94.3  86.1
REMARK 620 6 ASP G 203   OD1 125.6 102.2  82.2 172.1  89.4
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA E 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA G 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP C 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP G 477
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AA1   RELATED DB: PDB
REMARK 900  ACTIVATED SPINACH RUBISCO IN COMPLEX WITH
REMARK 900  THE PRODUCT 3-PHOSPHOGLYCERATE
REMARK 900 RELATED ID: 1AUS   RELATED DB: PDB
REMARK 900  ACTIVATED UNLIGANDED SPINACH RUBISCO
REMARK 900 RELATED ID: 1IR1   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF SPINACH RIBULOSE-1,5-
REMARK 900  BISPHOSPHATECARBOXYLASE/OXYGENASE (RUBISCO)
REMARK 900  COMPLEXED WITH CO2, MG2+AND 2-
REMARK 900  CARBOXYARABINITOL-1,5-BISPHOSPHATE
REMARK 900 RELATED ID: 1RBO   RELATED DB: PDB
REMARK 900  SPINACH RUBISCO IN COMPLEX WITH THE
REMARK 900  INHIBITOR 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE
REMARK 900 RELATED ID: 1RCO   RELATED DB: PDB
REMARK 900  SPINACH RUBISCO IN COMPLEX WITH THE
REMARK 900  INHIBITOR D-XYLULOSE-2,2-DIOL-1,5-
REMARK 900  BISPHOSPHATE
REMARK 900 RELATED ID: 1RCX   RELATED DB: PDB
REMARK 900  NON-ACTIVATED SPINACH RUBISCO IN COMPLEX
REMARK 900  WITH ITS SUBSTRATE RIBULOSE-1,5-BISPHOSPHATE
REMARK 900 RELATED ID: 1RXO   RELATED DB: PDB
REMARK 900  ACTIVATED SPINACH RUBISCO IN COMPLEX WITH
REMARK 900  ITS SUBSTRATE RIBULOSE-1,5-BISPHOSPHATE AND
REMARK 900   CALCIUM
REMARK 900 RELATED ID: 1UPM   RELATED DB: PDB
REMARK 900  ACTIVATED SPINACH RUBISCO COMPLEXED WITH
REMARK 900  2-CARBOXYARABINITOL 2 BISPHOSPHAT AND CA2+
REMARK 900 RELATED ID: 8RUC   RELATED DB: PDB
REMARK 900  ACTIVATED SPINACH RUBISCO COMPLEXED WITH 2-
REMARK 900  CARBOXYARABINITOL BISPHOSPHATE
DBREF  1UPP A    1   475  UNP    P00875   RBL_SPIOL        1    475
DBREF  1UPP C    1   475  UNP    P00875   RBL_SPIOL        1    475
DBREF  1UPP E    1   475  UNP    P00875   RBL_SPIOL        1    475
DBREF  1UPP G    1   475  UNP    P00875   RBL_SPIOL        1    475
DBREF  1UPP I    1   123  UNP    Q43832   RBS2_SPIOL      58    180
DBREF  1UPP J    1   123  UNP    Q43832   RBS2_SPIOL      58    180
DBREF  1UPP K    1   123  UNP    Q43832   RBS2_SPIOL      58    180
DBREF  1UPP L    1   123  UNP    Q43832   RBS2_SPIOL      58    180
SEQADV 1UPP GLN I    2  UNP  Q43832    LYS    59 CONFLICT
SEQADV 1UPP ILE I    6  UNP  Q43832    THR    63 CONFLICT
SEQADV 1UPP LEU I    7  UNP  Q43832    GLN    64 CONFLICT
SEQADV 1UPP LEU I    9  UNP  Q43832    MET    66 CONFLICT
SEQADV 1UPP LYS I   11  UNP  Q43832    ARG    68 CONFLICT
SEQADV 1UPP GLU I  109  UNP  Q43832    GLN   166 CONFLICT
SEQADV 1UPP ILE I  113  UNP  Q43832    VAL   170 CONFLICT
SEQADV 1UPP GLN J    2  UNP  Q43832    LYS    59 CONFLICT
SEQADV 1UPP ILE J    6  UNP  Q43832    THR    63 CONFLICT
SEQADV 1UPP LEU J    7  UNP  Q43832    GLN    64 CONFLICT
SEQADV 1UPP LEU J    9  UNP  Q43832    MET    66 CONFLICT
SEQADV 1UPP LYS J   11  UNP  Q43832    ARG    68 CONFLICT
SEQADV 1UPP GLU J  109  UNP  Q43832    GLN   166 CONFLICT
SEQADV 1UPP ILE J  113  UNP  Q43832    VAL   170 CONFLICT
SEQADV 1UPP GLN K    2  UNP  Q43832    LYS    59 CONFLICT
SEQADV 1UPP ILE K    6  UNP  Q43832    THR    63 CONFLICT
SEQADV 1UPP LEU K    7  UNP  Q43832    GLN    64 CONFLICT
SEQADV 1UPP LEU K    9  UNP  Q43832    MET    66 CONFLICT
SEQADV 1UPP LYS K   11  UNP  Q43832    ARG    68 CONFLICT
SEQADV 1UPP GLU K  109  UNP  Q43832    GLN   166 CONFLICT
SEQADV 1UPP ILE K  113  UNP  Q43832    VAL   170 CONFLICT
SEQADV 1UPP GLN L    2  UNP  Q43832    LYS    59 CONFLICT
SEQADV 1UPP ILE L    6  UNP  Q43832    THR    63 CONFLICT
SEQADV 1UPP LEU L    7  UNP  Q43832    GLN    64 CONFLICT
SEQADV 1UPP LEU L    9  UNP  Q43832    MET    66 CONFLICT
SEQADV 1UPP LYS L   11  UNP  Q43832    ARG    68 CONFLICT
SEQADV 1UPP GLU L  109  UNP  Q43832    GLN   166 CONFLICT
SEQADV 1UPP ILE L  113  UNP  Q43832    VAL   170 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 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 E  475  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLU PHE
SEQRES   2 E  475  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR
SEQRES   3 E  475  PRO GLU TYR GLU THR LEU ASP THR ASP ILE LEU ALA ALA
SEQRES   4 E  475  PHE ARG VAL SER PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 E  475  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 E  475  TRP THR THR VAL TRP THR ASP GLY LEU THR ASN LEU ASP
SEQRES   7 E  475  ARG TYR LYS GLY ARG CYS TYR HIS ILE GLU PRO VAL ALA
SEQRES   8 E  475  GLY GLU GLU ASN GLN TYR ILE CYS TYR VAL ALA TYR PRO
SEQRES   9 E  475  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 E  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 E  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO VAL ALA
SEQRES  12 E  475  TYR VAL LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 E  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU
SEQRES  14 E  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 E  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 E  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 E  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE CYS
SEQRES  18 E  475  ALA GLU ALA LEU TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 E  475  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 E  475  GLU ASP MET MET LYS ARG ALA VAL PHE ALA ARG GLU LEU
SEQRES  21 E  475  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 E  475  PHE THR ALA ASN THR THR LEU SER HIS TYR CYS ARG ASP
SEQRES  23 E  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 E  475  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG
SEQRES  25 E  475  VAL LEU ALA LYS ALA LEU ARG LEU SER GLY GLY ASP HIS
SEQRES  26 E  475  ILE HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 E  475  ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG ASP
SEQRES  28 E  475  ASP TYR THR GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 E  475  THR GLN SER TRP VAL SER THR PRO GLY VAL LEU PRO VAL
SEQRES  30 E  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 E  475  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY
SEQRES  32 E  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 E  475  ALA VAL ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN
SEQRES  34 E  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN
SEQRES  35 E  475  THR ILE ILE ARG GLU ALA THR LYS TRP SER PRO GLU LEU
SEQRES  36 E  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 E  475  PHE PRO ALA MET ASP THR VAL
SEQRES   1 G  475  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLU PHE
SEQRES   2 G  475  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR
SEQRES   3 G  475  PRO GLU TYR GLU THR LEU ASP THR ASP ILE LEU ALA ALA
SEQRES   4 G  475  PHE ARG VAL SER PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 G  475  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 G  475  TRP THR THR VAL TRP THR ASP GLY LEU THR ASN LEU ASP
SEQRES   7 G  475  ARG TYR LYS GLY ARG CYS TYR HIS ILE GLU PRO VAL ALA
SEQRES   8 G  475  GLY GLU GLU ASN GLN TYR ILE CYS TYR VAL ALA TYR PRO
SEQRES   9 G  475  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 G  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 G  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO VAL ALA
SEQRES  12 G  475  TYR VAL LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 G  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU
SEQRES  14 G  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 G  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 G  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 G  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE CYS
SEQRES  18 G  475  ALA GLU ALA LEU TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 G  475  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 G  475  GLU ASP MET MET LYS ARG ALA VAL PHE ALA ARG GLU LEU
SEQRES  21 G  475  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 G  475  PHE THR ALA ASN THR THR LEU SER HIS TYR CYS ARG ASP
SEQRES  23 G  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 G  475  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG
SEQRES  25 G  475  VAL LEU ALA LYS ALA LEU ARG LEU SER GLY GLY ASP HIS
SEQRES  26 G  475  ILE HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 G  475  ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG ASP
SEQRES  28 G  475  ASP TYR THR GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 G  475  THR GLN SER TRP VAL SER THR PRO GLY VAL LEU PRO VAL
SEQRES  30 G  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 G  475  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY
SEQRES  32 G  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 G  475  ALA VAL ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN
SEQRES  34 G  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN
SEQRES  35 G  475  THR ILE ILE ARG GLU ALA THR LYS TRP SER PRO GLU LEU
SEQRES  36 G  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 G  475  PHE PRO ALA MET ASP THR VAL
SEQRES   1 I  123  MET GLN VAL TRP PRO ILE LEU ASN LEU LYS LYS TYR GLU
SEQRES   2 I  123  THR LEU SER TYR LEU PRO PRO LEU THR THR ASP GLN LEU
SEQRES   3 I  123  ALA ARG GLN VAL ASP TYR LEU LEU ASN ASN LYS TRP VAL
SEQRES   4 I  123  PRO CYS LEU GLU PHE GLU THR ASP HIS GLY PHE VAL TYR
SEQRES   5 I  123  ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG
SEQRES   6 I  123  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR
SEQRES   7 I  123  ASP PRO ALA GLN VAL LEU ASN GLU LEU GLU GLU CYS LYS
SEQRES   8 I  123  LYS GLU TYR PRO ASN ALA PHE ILE ARG ILE ILE GLY PHE
SEQRES   9 I  123  ASP SER ASN ARG GLU VAL GLN CYS ILE SER PHE ILE ALA
SEQRES  10 I  123  TYR LYS PRO ALA GLY TYR
SEQRES   1 J  123  MET GLN VAL TRP PRO ILE LEU ASN LEU LYS LYS TYR GLU
SEQRES   2 J  123  THR LEU SER TYR LEU PRO PRO LEU THR THR ASP GLN LEU
SEQRES   3 J  123  ALA ARG GLN VAL ASP TYR LEU LEU ASN ASN LYS TRP VAL
SEQRES   4 J  123  PRO CYS LEU GLU PHE GLU THR ASP HIS GLY PHE VAL TYR
SEQRES   5 J  123  ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG
SEQRES   6 J  123  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR
SEQRES   7 J  123  ASP PRO ALA GLN VAL LEU ASN GLU LEU GLU GLU CYS LYS
SEQRES   8 J  123  LYS GLU TYR PRO ASN ALA PHE ILE ARG ILE ILE GLY PHE
SEQRES   9 J  123  ASP SER ASN ARG GLU VAL GLN CYS ILE SER PHE ILE ALA
SEQRES  10 J  123  TYR LYS PRO ALA GLY TYR
SEQRES   1 K  123  MET GLN VAL TRP PRO ILE LEU ASN LEU LYS LYS TYR GLU
SEQRES   2 K  123  THR LEU SER TYR LEU PRO PRO LEU THR THR ASP GLN LEU
SEQRES   3 K  123  ALA ARG GLN VAL ASP TYR LEU LEU ASN ASN LYS TRP VAL
SEQRES   4 K  123  PRO CYS LEU GLU PHE GLU THR ASP HIS GLY PHE VAL TYR
SEQRES   5 K  123  ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG
SEQRES   6 K  123  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR
SEQRES   7 K  123  ASP PRO ALA GLN VAL LEU ASN GLU LEU GLU GLU CYS LYS
SEQRES   8 K  123  LYS GLU TYR PRO ASN ALA PHE ILE ARG ILE ILE GLY PHE
SEQRES   9 K  123  ASP SER ASN ARG GLU VAL GLN CYS ILE SER PHE ILE ALA
SEQRES  10 K  123  TYR LYS PRO ALA GLY TYR
SEQRES   1 L  123  MET GLN VAL TRP PRO ILE LEU ASN LEU LYS LYS TYR GLU
SEQRES   2 L  123  THR LEU SER TYR LEU PRO PRO LEU THR THR ASP GLN LEU
SEQRES   3 L  123  ALA ARG GLN VAL ASP TYR LEU LEU ASN ASN LYS TRP VAL
SEQRES   4 L  123  PRO CYS LEU GLU PHE GLU THR ASP HIS GLY PHE VAL TYR
SEQRES   5 L  123  ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG
SEQRES   6 L  123  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR
SEQRES   7 L  123  ASP PRO ALA GLN VAL LEU ASN GLU LEU GLU GLU CYS LYS
SEQRES   8 L  123  LYS GLU TYR PRO ASN ALA PHE ILE ARG ILE ILE GLY PHE
SEQRES   9 L  123  ASP SER ASN ARG GLU VAL GLN CYS ILE SER PHE ILE ALA
SEQRES  10 L  123  TYR LYS PRO ALA GLY TYR
MODRES 1UPP KCX A  201  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 1UPP KCX C  201  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 1UPP KCX E  201  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 1UPP 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     CA  A 476       1
HET     CA  C 476       1
HET     CA  E 476       1
HET     CA  G 476       1
HET    CAP  A 477      21
HET    CAP  C 477      21
HET    CAP  E 477      21
HET    CAP  G 477      21
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID
HETNAM      CA CALCIUM ION
HETNAM     CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE
FORMUL   1  KCX    4(C7 H14 N2 O4)
FORMUL   9   CA    4(CA 2+)
FORMUL  13  CAP    4(C6 H14 O13 P2)
FORMUL  17  HOH   *664(H2 O1)
HELIX    1   1 TYR A   20  TYR A   25  1                                   6
HELIX    2   2 PRO A   49  SER A   61  1                                  13
HELIX    3   3 VAL A   69  THR A   75  5                                   7
HELIX    4   4 ASN A   76  LYS A   81  1                                   6
HELIX    5   5 PRO A  104  PHE A  108  5                                   5
HELIX    6   6 SER A  112  VAL A  121  1                                  10
HELIX    7   7 ASN A  123  PHE A  127  5                                   5
HELIX    8   8 PRO A  141  LYS A  146  1                                   6
HELIX    9   9 GLY A  154  ASN A  163  1                                  10
HELIX   10  10 SER A  181  GLY A  195  1                                  15
HELIX   11  11 ARG A  213  GLY A  233  1                                  21
HELIX   12  12 THR A  246  GLY A  261  1                                  16
HELIX   13  13 TYR A  269  GLY A  288  1                                  20
HELIX   14  14 MET A  297  ARG A  303  1                                   7
HELIX   15  15 HIS A  310  GLY A  322  1                                  13
HELIX   16  16 GLU A  338  ASP A  351  1                                  14
HELIX   17  17 ARG A  358  GLY A  361  5                                   4
HELIX   18  18 HIS A  383  TRP A  385  5                                   3
HELIX   19  19 HIS A  386  GLY A  395  1                                  10
HELIX   20  20 GLY A  403  GLY A  408  1                                   6
HELIX   21  21 GLY A  412  GLU A  433  1                                  22
HELIX   22  22 ASP A  436  TRP A  462  1                                  27
HELIX   23  23 TYR C   20  TYR C   25  1                                   6
HELIX   24  24 PRO C   49  SER C   61  1                                  13
HELIX   25  25 VAL C   69  THR C   75  5                                   7
HELIX   26  26 ASN C   76  LYS C   81  1                                   6
HELIX   27  27 PRO C  104  PHE C  108  5                                   5
HELIX   28  28 SER C  112  VAL C  121  1                                  10
HELIX   29  29 ASN C  123  PHE C  127  5                                   5
HELIX   30  30 PRO C  141  LYS C  146  1                                   6
HELIX   31  31 GLY C  154  ASN C  163  1                                  10
HELIX   32  32 SER C  181  GLY C  195  1                                  15
HELIX   33  33 ARG C  213  GLY C  233  1                                  21
HELIX   34  34 THR C  246  GLY C  261  1                                  16
HELIX   35  35 TYR C  269  GLY C  288  1                                  20
HELIX   36  36 MET C  297  ARG C  303  1                                   7
HELIX   37  37 HIS C  310  GLY C  322  1                                  13
HELIX   38  38 GLU C  338  ASP C  351  1                                  14
HELIX   39  39 ARG C  358  GLY C  361  5                                   4
HELIX   40  40 HIS C  383  TRP C  385  5                                   3
HELIX   41  41 HIS C  386  GLY C  395  1                                  10
HELIX   42  42 GLY C  403  GLY C  408  1                                   6
HELIX   43  43 GLY C  412  GLY C  434  1                                  23
HELIX   44  44 ASP C  436  LYS C  450  1                                  15
HELIX   45  45 SER C  452  LYS C  463  1                                  12
HELIX   46  46 TYR E   20  TYR E   25  1                                   6
HELIX   47  47 PRO E   49  SER E   61  1                                  13
HELIX   48  48 VAL E   69  THR E   75  5                                   7
HELIX   49  49 ASN E   76  LYS E   81  1                                   6
HELIX   50  50 PRO E  104  PHE E  108  5                                   5
HELIX   51  51 SER E  112  VAL E  121  1                                  10
HELIX   52  52 ASN E  123  PHE E  127  5                                   5
HELIX   53  53 PRO E  141  LYS E  146  1                                   6
HELIX   54  54 GLY E  154  ASN E  163  1                                  10
HELIX   55  55 SER E  181  GLY E  195  1                                  15
HELIX   56  56 ARG E  213  GLY E  233  1                                  21
HELIX   57  57 THR E  246  GLY E  261  1                                  16
HELIX   58  58 TYR E  269  ASP E  286  1                                  18
HELIX   59  59 MET E  297  ARG E  303  1                                   7
HELIX   60  60 HIS E  310  GLY E  322  1                                  13
HELIX   61  61 GLU E  338  ASP E  351  1                                  14
HELIX   62  62 ARG E  358  GLY E  361  5                                   4
HELIX   63  63 HIS E  383  TRP E  385  5                                   3
HELIX   64  64 HIS E  386  GLY E  395  1                                  10
HELIX   65  65 GLY E  403  GLY E  408  1                                   6
HELIX   66  66 GLY E  412  GLY E  434  1                                  23
HELIX   67  67 ASP E  436  LYS E  463  1                                  28
HELIX   68  68 TYR G   20  TYR G   25  1                                   6
HELIX   69  69 PRO G   49  SER G   61  1                                  13
HELIX   70  70 VAL G   69  THR G   75  5                                   7
HELIX   71  71 ASN G   76  TYR G   80  5                                   5
HELIX   72  72 PRO G  104  PHE G  108  5                                   5
HELIX   73  73 SER G  112  GLY G  122  1                                  11
HELIX   74  74 ASN G  123  PHE G  127  5                                   5
HELIX   75  75 PRO G  141  LYS G  146  1                                   6
HELIX   76  76 GLY G  154  ASN G  163  1                                  10
HELIX   77  77 SER G  181  ARG G  194  1                                  14
HELIX   78  78 ARG G  213  GLY G  233  1                                  21
HELIX   79  79 THR G  246  GLY G  261  1                                  16
HELIX   80  80 ASP G  268  GLY G  273  1                                   6
HELIX   81  81 GLY G  273  GLY G  288  1                                  16
HELIX   82  82 MET G  297  ARG G  303  1                                   7
HELIX   83  83 HIS G  310  GLY G  322  1                                  13
HELIX   84  84 GLU G  338  ASP G  351  1                                  14
HELIX   85  85 ARG G  358  GLY G  361  5                                   4
HELIX   86  86 HIS G  383  TRP G  385  5                                   3
HELIX   87  87 HIS G  386  GLY G  395  1                                  10
HELIX   88  88 GLY G  403  GLY G  408  1                                   6
HELIX   89  89 GLY G  412  GLY G  434  1                                  23
HELIX   90  90 ASP G  436  LYS G  450  1                                  15
HELIX   91  91 SER G  452  LYS G  463  1                                  12
HELIX   92  92 THR I   22  ASN I   36  1                                  15
HELIX   93  93 ASP I   79  TYR I   94  1                                  16
HELIX   94  94 THR J   22  ASN J   36  1                                  15
HELIX   95  95 ASP J   79  TYR J   94  1                                  16
HELIX   96  96 THR K   22  ASN K   36  1                                  15
HELIX   97  97 ASP K   79  TYR K   94  1                                  16
HELIX   98  98 THR L   22  ASN L   36  1                                  15
HELIX   99  99 ASP L   79  TYR L   94  1                                  16
SHEET    1  AA 5 ARG A  83  PRO A  89  0
SHEET    2  AA 5 TYR A  97  TYR A 103 -1  O  ILE A  98   N  GLU A  88
SHEET    3  AA 5 ILE A  36  PRO A  44 -1  O  ILE A  36   N  TYR A 103
SHEET    4  AA 5 LEU A 130  ARG A 139 -1  N  ARG A 131   O  SER A  43
SHEET    5  AA 5 GLY A 308  MET A 309  1  O  GLY A 308   N  LEU A 135
SHEET    1  AB 8 LEU A 169  GLY A 171  0
SHEET    2  AB 8 VAL A 399  GLN A 401  1  O  LEU A 400   N  GLY A 171
SHEET    3  AB 8 LEU A 375  SER A 379  1  O  PRO A 376   N  VAL A 399
SHEET    4  AB 8 HIS A 325  HIS A 327  1  O  ILE A 326   N  VAL A 377
SHEET    5  AB 8 LEU A 290  HIS A 294  1  O  ILE A 293   N  HIS A 327
SHEET    6  AB 8 ILE A 264  ASP A 268  1  O  VAL A 265   N  HIS A 292
SHEET    7  AB 8 GLY A 237  ASN A 241  1  O  LEU A 240   N  MET A 266
SHEET    8  AB 8 PHE A 199  KCX A 201  1  O  THR A 200   N  TYR A 239
SHEET    1  AC 2 TYR A 353  THR A 354  0
SHEET    2  AC 2 GLN A 366  SER A 367 -1  O  GLN A 366   N  THR A 354
SHEET    1  CA 5 ARG C  83  PRO C  89  0
SHEET    2  CA 5 TYR C  97  TYR C 103 -1  O  ILE C  98   N  GLU C  88
SHEET    3  CA 5 ILE C  36  PRO C  44 -1  O  ILE C  36   N  TYR C 103
SHEET    4  CA 5 LEU C 130  ARG C 139 -1  N  ARG C 131   O  SER C  43
SHEET    5  CA 5 GLY C 308  MET C 309  1  O  GLY C 308   N  LEU C 135
SHEET    1  CB 8 LEU C 169  GLY C 171  0
SHEET    2  CB 8 VAL C 399  GLN C 401  1  O  LEU C 400   N  GLY C 171
SHEET    3  CB 8 LEU C 375  SER C 379  1  O  PRO C 376   N  VAL C 399
SHEET    4  CB 8 HIS C 325  HIS C 327  1  O  ILE C 326   N  VAL C 377
SHEET    5  CB 8 LEU C 290  HIS C 294  1  O  ILE C 293   N  HIS C 327
SHEET    6  CB 8 ILE C 264  ASP C 268  1  O  VAL C 265   N  HIS C 292
SHEET    7  CB 8 GLY C 237  ASN C 241  1  O  LEU C 240   N  MET C 266
SHEET    8  CB 8 PHE C 199  KCX C 201  1  O  THR C 200   N  TYR C 239
SHEET    1  CC 2 TYR C 353  THR C 354  0
SHEET    2  CC 2 GLN C 366  SER C 367 -1  O  GLN C 366   N  THR C 354
SHEET    1  EA 5 ARG E  83  PRO E  89  0
SHEET    2  EA 5 TYR E  97  TYR E 103 -1  O  ILE E  98   N  GLU E  88
SHEET    3  EA 5 ILE E  36  PRO E  44 -1  O  ILE E  36   N  TYR E 103
SHEET    4  EA 5 LEU E 130  ARG E 139 -1  N  ARG E 131   O  SER E  43
SHEET    5  EA 5 GLY E 308  MET E 309  1  O  GLY E 308   N  LEU E 135
SHEET    1  EB 8 LEU E 169  GLY E 171  0
SHEET    2  EB 8 VAL E 399  GLN E 401  1  O  LEU E 400   N  GLY E 171
SHEET    3  EB 8 LEU E 375  ALA E 378  1  O  PRO E 376   N  VAL E 399
SHEET    4  EB 8 HIS E 325  HIS E 327  1  O  ILE E 326   N  VAL E 377
SHEET    5  EB 8 LEU E 290  HIS E 294  1  O  ILE E 293   N  HIS E 327
SHEET    6  EB 8 ILE E 264  ASP E 268  1  O  VAL E 265   N  HIS E 292
SHEET    7  EB 8 GLY E 237  ASN E 241  1  O  LEU E 240   N  MET E 266
SHEET    8  EB 8 PHE E 199  KCX E 201  1  O  THR E 200   N  TYR E 239
SHEET    1  EC 2 TYR E 353  THR E 354  0
SHEET    2  EC 2 GLN E 366  SER E 367 -1  O  GLN E 366   N  THR E 354
SHEET    1  GA 5 ARG G  83  PRO G  89  0
SHEET    2  GA 5 TYR G  97  TYR G 103 -1  O  ILE G  98   N  GLU G  88
SHEET    3  GA 5 ILE G  36  PRO G  44 -1  O  ILE G  36   N  TYR G 103
SHEET    4  GA 5 LEU G 130  ARG G 139 -1  N  ARG G 131   O  SER G  43
SHEET    5  GA 5 GLY G 308  MET G 309  1  O  GLY G 308   N  LEU G 135
SHEET    1  GB 8 LEU G 169  GLY G 171  0
SHEET    2  GB 8 VAL G 399  GLN G 401  1  O  LEU G 400   N  GLY G 171
SHEET    3  GB 8 LEU G 375  SER G 379  1  O  PRO G 376   N  VAL G 399
SHEET    4  GB 8 HIS G 325  HIS G 327  1  O  ILE G 326   N  VAL G 377
SHEET    5  GB 8 LEU G 290  ILE G 293  1  O  ILE G 293   N  HIS G 327
SHEET    6  GB 8 ILE G 264  HIS G 267  1  O  VAL G 265   N  HIS G 292
SHEET    7  GB 8 GLY G 237  ASN G 241  1  O  LEU G 240   N  MET G 266
SHEET    8  GB 8 PHE G 199  KCX G 201  1  O  THR G 200   N  TYR G 239
SHEET    1  GC 2 TYR G 353  THR G 354  0
SHEET    2  GC 2 GLN G 366  SER G 367 -1  O  GLN G 366   N  THR G 354
SHEET    1  IA 4 THR I  68  TRP I  70  0
SHEET    2  IA 4 VAL I  39  GLU I  45 -1  O  LEU I  42   N  TRP I  70
SHEET    3  IA 4 PHE I  98  ASP I 105 -1  O  PHE I  98   N  GLU I  45
SHEET    4  IA 4 VAL I 110  TYR I 118 -1  O  VAL I 110   N  ASP I 105
SHEET    1  JA 4 THR J  68  MET J  69  0
SHEET    2  JA 4 VAL J  39  GLU J  45 -1  O  PHE J  44   N  THR J  68
SHEET    3  JA 4 PHE J  98  ASP J 105 -1  O  PHE J  98   N  GLU J  45
SHEET    4  JA 4 VAL J 110  TYR J 118 -1  O  VAL J 110   N  ASP J 105
SHEET    1  KA 4 THR K  68  MET K  69  0
SHEET    2  KA 4 VAL K  39  GLU K  45 -1  O  PHE K  44   N  THR K  68
SHEET    3  KA 4 PHE K  98  ASP K 105 -1  O  PHE K  98   N  GLU K  45
SHEET    4  KA 4 VAL K 110  TYR K 118 -1  O  VAL K 110   N  ASP K 105
SHEET    1  LA 4 THR L  68  TRP L  70  0
SHEET    2  LA 4 VAL L  39  GLU L  45 -1  O  LEU L  42   N  TRP L  70
SHEET    3  LA 4 PHE L  98  ASP L 105 -1  O  PHE L  98   N  GLU L  45
SHEET    4  LA 4 VAL L 110  TYR L 118 -1  O  VAL L 110   N  ASP L 105
SSBOND   1 CYS A  247    CYS E  247                          1555   3555  2.58
LINK         C   THR A 200                 N   KCX A 201     1555   1555  1.30
LINK         C   KCX A 201                 N   ASP A 202     1555   1555  1.34
LINK        CA    CA A 476                 O2  CAP A 477     1555   1555  2.71
LINK        CA    CA A 476                 O6  CAP A 477     1555   1555  2.50
LINK        CA    CA A 476                 OE1 GLU A 204     1555   1555  2.47
LINK        CA    CA A 476                 O3  CAP A 477     1555   1555  2.69
LINK        CA    CA A 476                 OQ2 KCX A 201     1555   1555  2.54
LINK        CA    CA A 476                 OD1 ASP A 203     1555   1555  2.59
LINK         C   THR C 200                 N   KCX C 201     1555   1555  1.33
LINK         C   KCX C 201                 N   ASP C 202     1555   1555  1.33
LINK        CA    CA C 476                 O2  CAP C 477     1555   1555  2.63
LINK        CA    CA C 476                 O6  CAP C 477     1555   1555  2.62
LINK        CA    CA C 476                 OQ2 KCX C 201     1555   1555  2.42
LINK        CA    CA C 476                 O3  CAP C 477     1555   1555  2.69
LINK        CA    CA C 476                 OE1 GLU C 204     1555   1555  2.45
LINK        CA    CA C 476                 OD1 ASP C 203     1555   1555  2.51
LINK         C   THR E 200                 N   KCX E 201     1555   1555  1.28
LINK         C   KCX E 201                 N   ASP E 202     1555   1555  1.29
LINK        CA    CA E 476                 O6  CAP E 477     1555   1555  2.60
LINK        CA    CA E 476                 O2  CAP E 477     1555   1555  2.73
LINK        CA    CA E 476                 OQ2 KCX E 201     1555   1555  2.45
LINK        CA    CA E 476                 OD1 ASP E 203     1555   1555  2.45
LINK        CA    CA E 476                 OE1 GLU E 204     1555   1555  2.56
LINK        CA    CA E 476                 O3  CAP E 477     1555   1555  2.70
LINK         C   THR G 200                 N   KCX G 201     1555   1555  1.33
LINK         C   KCX G 201                 N   ASP G 202     1555   1555  1.31
LINK        CA    CA G 476                 O6  CAP G 477     1555   1555  2.60
LINK        CA    CA G 476                 OE1 GLU G 204     1555   1555  2.56
LINK        CA    CA G 476                 O3  CAP G 477     1555   1555  2.63
LINK        CA    CA G 476                 OQ2 KCX G 201     1555   1555  2.50
LINK        CA    CA G 476                 OD1 ASP G 203     1555   1555  2.52
LINK        CA    CA G 476                 O2  CAP G 477     1555   1555  2.74
CISPEP   1 LYS C  175    PRO C  176          0        27.88
SITE     1 AC1  6 LYS A 175  LYS A 177  KCX A 201  ASP A 203
SITE     2 AC1  6 GLU A 204  CAP A 477
SITE     1 AC2  6 LYS C 175  LYS C 177  KCX C 201  ASP C 203
SITE     2 AC2  6 GLU C 204  CAP C 477
SITE     1 AC3  5 LYS E 177  KCX E 201  ASP E 203  GLU E 204
SITE     2 AC3  5 CAP E 477
SITE     1 AC4  5 LYS G 177  KCX G 201  ASP G 203  GLU G 204
SITE     2 AC4  5 CAP G 477
SITE     1 AC5 25 THR A 173  LYS A 175  LYS A 177  KCX A 201
SITE     2 AC5 25 GLU A 204  HIS A 294  ARG A 295  HIS A 327
SITE     3 AC5 25 LYS A 334  LEU A 335  SER A 379  GLY A 380
SITE     4 AC5 25 GLY A 381  GLY A 403  GLY A 404   CA A 476
SITE     5 AC5 25 HOH A2070  HOH A2110  HOH A2111  HOH A2112
SITE     6 AC5 25 GLU E  60  THR E  65  TRP E  66  ASN E 123
SITE     7 AC5 25 HOH E2016
SITE     1 AC6 24 GLU C  60  THR C  65  TRP C  66  ASN C 123
SITE     2 AC6 24 THR C 173  LYS C 175  LYS C 177  KCX C 201
SITE     3 AC6 24 HIS C 294  ARG C 295  HIS C 327  LYS C 334
SITE     4 AC6 24 LEU C 335  SER C 379  GLY C 380  GLY C 381
SITE     5 AC6 24 PHE C 402  GLY C 403  GLY C 404   CA C 476
SITE     6 AC6 24 HOH C2082  HOH C2083  HOH C2105  HOH C2108
SITE     1 AC7 25 GLU A  60  THR A  65  TRP A  66  ASN A 123
SITE     2 AC7 25 THR E 173  LYS E 175  LYS E 177  KCX E 201
SITE     3 AC7 25 HIS E 294  ARG E 295  HIS E 327  LYS E 334
SITE     4 AC7 25 LEU E 335  SER E 379  GLY E 380  GLY E 381
SITE     5 AC7 25 GLY E 403  GLY E 404   CA E 476  HOH E2080
SITE     6 AC7 25 HOH E2081  HOH E2129  HOH E2130  HOH E2131
SITE     7 AC7 25 HOH E2132
SITE     1 AC8 23 GLU G  60  THR G  65  TRP G  66  ASN G 123
SITE     2 AC8 23 THR G 173  LYS G 175  LYS G 177  KCX G 201
SITE     3 AC8 23 HIS G 294  ARG G 295  HIS G 327  LYS G 334
SITE     4 AC8 23 LEU G 335  SER G 379  GLY G 380  GLY G 381
SITE     5 AC8 23 GLY G 403  GLY G 404   CA G 476  HOH G2088
SITE     6 AC8 23 HOH G2104  HOH G2132  HOH G2133
CRYST1  155.880  156.250  199.750  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      0.006415  0.000000  0.000000        0.00000
SCALE2      0.000000  0.006400  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005006        0.00000
MTRIX1   1  0.002971 -0.999600 -0.029320       40.80000    1
MTRIX2   1  0.999500  0.002027  0.032170       37.50000    1
MTRIX3   1 -0.032100 -0.029400  0.999100        1.18700    1
MTRIX1   2 -0.998200 -0.000725 -0.059900        3.03700    1
MTRIX2   2  0.000669 -1.000000  0.000961       78.37000    1
MTRIX3   2 -0.059900  0.000919  0.998200        0.01699    1
MTRIX1   3 -0.000760  0.999600 -0.029090      -37.60000    1
MTRIX2   3 -0.999600 -0.001593 -0.028620       40.69000    1
MTRIX3   3 -0.028650  0.029060  0.999200       -1.15200    1
MTRIX1   4  0.004315 -0.999600 -0.029290       40.76000    1
MTRIX2   4  0.999600  0.003458  0.029260       37.58000    1
MTRIX3   4 -0.029150 -0.029410  0.999100        1.14200    1
MTRIX1   5 -0.998100 -0.000958 -0.061800        3.03200    1
MTRIX2   5  0.001024 -1.000000 -0.001030       78.38000    1
MTRIX3   5 -0.061800 -0.001092  0.998100        0.10630    1
MTRIX1   6 -0.001617  0.999300 -0.036420      -37.59000    1
MTRIX2   6 -0.999600 -0.002643 -0.028130       40.75000    1
MTRIX3   6 -0.028210  0.036360  0.998900       -1.30100    1
      
PROCHECK
Go to PROCHECK summary
 References