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PDBsum entry 1bxn

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Top Page protein ligands Protein-protein interface(s) links
Lyase PDB id
1bxn
Jmol
Contents
Protein chains
445 a.a. *
129 a.a. *
Ligands
PO4 ×8
* Residue conservation analysis
HEADER    LYASE                                   06-OCT-98   1BXN
TITLE     THE CRYSTAL STRUCTURE OF RUBISCO FROM ALCALIGENES EUTROPHUS TO 2.7
TITLE    2 ANGSTROMS.
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN (RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN);
COMPND   3 CHAIN: A, C, E, G;
COMPND   4 SYNONYM: RUBISCO;
COMPND   5 EC: 4.1.1.39;
COMPND   6 ENGINEERED: YES;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: PROTEIN (RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN);
COMPND   9 CHAIN: I, J, K, L;
COMPND  10 SYNONYM: RUBISCO;
COMPND  11 EC: 4.1.1.39;
COMPND  12 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: CUPRIAVIDUS NECATOR;
SOURCE   3 ORGANISM_TAXID: 106590;
SOURCE   4 MOL_ID: 2;
SOURCE   5 ORGANISM_SCIENTIFIC: CUPRIAVIDUS NECATOR;
SOURCE   6 ORGANISM_TAXID: 106590
KEYWDS    LYASE (CARBON-CARBON), LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.HANSEN,V.B.VOLLAN,E.HOUGH,K.ANDERSEN
REVDAT   5   13-JUL-11 1BXN    1       VERSN
REVDAT   4   24-FEB-09 1BXN    1       VERSN
REVDAT   3   05-JUN-00 1BXN    1       COMPND REMARK DBREF  SEQADV
REVDAT   3 2                   1       SEQRES HELIX
REVDAT   2   07-OCT-99 1BXN    3
REVDAT   1   06-OCT-99 1BXN    0
JRNL        AUTH   S.HANSEN,V.B.VOLLAN,E.HOUGH,K.ANDERSEN
JRNL        TITL   THE CRYSTAL STRUCTURE OF RUBISCO FROM ALCALIGENES EUTROPHUS
JRNL        TITL 2 REVEALS A NOVEL CENTRAL EIGHT-STRANDED BETA-BARREL FORMED BY
JRNL        TITL 3 BETA-STRANDS FROM FOUR SUBUNITS.
JRNL        REF    J.MOL.BIOL.                   V. 288   609 1999
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   10329167
JRNL        DOI    10.1006/JMBI.1999.2701
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   S.HANSEN,E.HOUGH,K.ANDERSEN
REMARK   1  TITL   PURIFICATION, CRYSTALLIZATION AND PRELIMINARY X-RAY STUDIES
REMARK   1  TITL 2 OF TWO ISOFORMS OF RUBISCO FROM ALCALIGENES EUTROPHUS
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  55   310 1999
REMARK   1  REFN                   ISSN 0907-4449
REMARK   2
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.8
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.0
REMARK   3   NUMBER OF REFLECTIONS             : 65785
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) : 0.266
REMARK   3   FREE R VALUE                     : 0.322
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 18104
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 40
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.010
REMARK   3   BOND ANGLES            (DEGREES) : 1.20
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.76
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.11
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1BXN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-99.
REMARK 100 THE RCSB ID CODE IS RCSB007023.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 11-MAY-97
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 8.40
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : BM1A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9117
REMARK 200  MONOCHROMATOR                  : YES
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SOFTWARE AT SYNCHROTRON
REMARK 200  DATA SCALING SOFTWARE          : CCP4
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 65785
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.0
REMARK 200  DATA REDUNDANCY                : 4.400
REMARK 200  R MERGE                    (I) : 0.12500
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 1.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1AUS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 45.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.40
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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   -Y+1/2,X+1/2,Z+3/4
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-Z+1/2
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      201.35000
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       56.00000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       56.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      302.02500
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       56.00000
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       56.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      100.67500
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       56.00000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       56.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      302.02500
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       56.00000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       56.00000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      100.67500
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      201.35000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXADECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 95060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 121570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -442.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, I, C, J, E, K, G, L
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2  0.000000 -1.000000  0.000000      112.00000
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000      112.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      201.35000
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     ASN A     2
REMARK 465     ALA A     3
REMARK 465     PRO A     4
REMARK 465     GLU A     5
REMARK 465     SER A     6
REMARK 465     VAL A     7
REMARK 465     GLN A     8
REMARK 465     ALA A     9
REMARK 465     LYS A    10
REMARK 465     PRO A    11
REMARK 465     ARG A    12
REMARK 465     LYS A    13
REMARK 465     ARG A    14
REMARK 465     TYR A    15
REMARK 465     ASP A    16
REMARK 465     ALA A    17
REMARK 465     GLY A    18
REMARK 465     VAL A    19
REMARK 465     MET A    20
REMARK 465     LYS A    21
REMARK 465     SER A   468
REMARK 465     PHE A   469
REMARK 465     ASN A   470
REMARK 465     TYR A   471
REMARK 465     THR A   472
REMARK 465     PRO A   473
REMARK 465     THR A   474
REMARK 465     ASP A   475
REMARK 465     THR A   476
REMARK 465     SER A   477
REMARK 465     ASP A   478
REMARK 465     PHE A   479
REMARK 465     ALA A   480
REMARK 465     PRO A   481
REMARK 465     THR A   482
REMARK 465     ALA A   483
REMARK 465     SER A   484
REMARK 465     VAL A   485
REMARK 465     ALA A   486
REMARK 465     VAL I   130
REMARK 465     GLN I   131
REMARK 465     ALA I   132
REMARK 465     GLY I   133
REMARK 465     PRO I   134
REMARK 465     GLU I   135
REMARK 465     GLY I   136
REMARK 465     SER I   137
REMARK 465     ARG I   138
REMARK 465     TYR I   139
REMARK 465     MET C     1
REMARK 465     ASN C     2
REMARK 465     ALA C     3
REMARK 465     PRO C     4
REMARK 465     GLU C     5
REMARK 465     SER C     6
REMARK 465     VAL C     7
REMARK 465     GLN C     8
REMARK 465     ALA C     9
REMARK 465     LYS C    10
REMARK 465     PRO C    11
REMARK 465     ARG C    12
REMARK 465     LYS C    13
REMARK 465     ARG C    14
REMARK 465     TYR C    15
REMARK 465     ASP C    16
REMARK 465     ALA C    17
REMARK 465     GLY C    18
REMARK 465     VAL C    19
REMARK 465     MET C    20
REMARK 465     LYS C    21
REMARK 465     SER C   468
REMARK 465     PHE C   469
REMARK 465     ASN C   470
REMARK 465     TYR C   471
REMARK 465     THR C   472
REMARK 465     PRO C   473
REMARK 465     THR C   474
REMARK 465     ASP C   475
REMARK 465     THR C   476
REMARK 465     SER C   477
REMARK 465     ASP C   478
REMARK 465     PHE C   479
REMARK 465     ALA C   480
REMARK 465     PRO C   481
REMARK 465     THR C   482
REMARK 465     ALA C   483
REMARK 465     SER C   484
REMARK 465     VAL C   485
REMARK 465     ALA C   486
REMARK 465     VAL J   130
REMARK 465     GLN J   131
REMARK 465     ALA J   132
REMARK 465     GLY J   133
REMARK 465     PRO J   134
REMARK 465     GLU J   135
REMARK 465     GLY J   136
REMARK 465     SER J   137
REMARK 465     ARG J   138
REMARK 465     TYR J   139
REMARK 465     MET E     1
REMARK 465     ASN E     2
REMARK 465     ALA E     3
REMARK 465     PRO E     4
REMARK 465     GLU E     5
REMARK 465     SER E     6
REMARK 465     VAL E     7
REMARK 465     GLN E     8
REMARK 465     ALA E     9
REMARK 465     LYS E    10
REMARK 465     PRO E    11
REMARK 465     ARG E    12
REMARK 465     LYS E    13
REMARK 465     ARG E    14
REMARK 465     TYR E    15
REMARK 465     ASP E    16
REMARK 465     ALA E    17
REMARK 465     GLY E    18
REMARK 465     VAL E    19
REMARK 465     MET E    20
REMARK 465     LYS E    21
REMARK 465     SER E   468
REMARK 465     PHE E   469
REMARK 465     ASN E   470
REMARK 465     TYR E   471
REMARK 465     THR E   472
REMARK 465     PRO E   473
REMARK 465     THR E   474
REMARK 465     ASP E   475
REMARK 465     THR E   476
REMARK 465     SER E   477
REMARK 465     ASP E   478
REMARK 465     PHE E   479
REMARK 465     ALA E   480
REMARK 465     PRO E   481
REMARK 465     THR E   482
REMARK 465     ALA E   483
REMARK 465     SER E   484
REMARK 465     VAL E   485
REMARK 465     ALA E   486
REMARK 465     VAL K   130
REMARK 465     GLN K   131
REMARK 465     ALA K   132
REMARK 465     GLY K   133
REMARK 465     PRO K   134
REMARK 465     GLU K   135
REMARK 465     GLY K   136
REMARK 465     SER K   137
REMARK 465     ARG K   138
REMARK 465     TYR K   139
REMARK 465     MET G     1
REMARK 465     ASN G     2
REMARK 465     ALA G     3
REMARK 465     PRO G     4
REMARK 465     GLU G     5
REMARK 465     SER G     6
REMARK 465     VAL G     7
REMARK 465     GLN G     8
REMARK 465     ALA G     9
REMARK 465     LYS G    10
REMARK 465     PRO G    11
REMARK 465     ARG G    12
REMARK 465     LYS G    13
REMARK 465     ARG G    14
REMARK 465     TYR G    15
REMARK 465     ASP G    16
REMARK 465     ALA G    17
REMARK 465     GLY G    18
REMARK 465     VAL G    19
REMARK 465     MET G    20
REMARK 465     LYS G    21
REMARK 465     SER G   468
REMARK 465     PHE G   469
REMARK 465     ASN G   470
REMARK 465     TYR G   471
REMARK 465     THR G   472
REMARK 465     PRO G   473
REMARK 465     THR G   474
REMARK 465     ASP G   475
REMARK 465     THR G   476
REMARK 465     SER G   477
REMARK 465     ASP G   478
REMARK 465     PHE G   479
REMARK 465     ALA G   480
REMARK 465     PRO G   481
REMARK 465     THR G   482
REMARK 465     ALA G   483
REMARK 465     SER G   484
REMARK 465     VAL G   485
REMARK 465     ALA G   486
REMARK 465     VAL L   130
REMARK 465     GLN L   131
REMARK 465     ALA L   132
REMARK 465     GLY L   133
REMARK 465     PRO L   134
REMARK 465     GLU L   135
REMARK 465     GLY L   136
REMARK 465     SER L   137
REMARK 465     ARG L   138
REMARK 465     TYR L   139
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    LYS A  23      -48.02     72.20
REMARK 500    MET A  25      -36.04    -31.43
REMARK 500    THR A  37       50.71   -113.06
REMARK 500    ARG A  44       78.00   -119.63
REMARK 500    ASP A  49       99.57    -59.46
REMARK 500    GLU A  63       34.25    -86.23
REMARK 500    SER A  64       34.18   -163.99
REMARK 500    SER A  65     -150.09   -170.59
REMARK 500    THR A  66       33.00    -71.35
REMARK 500    ALA A  79      -34.25     73.27
REMARK 500    CYS A  80      -90.97     49.85
REMARK 500    ASP A  81      -85.22     49.53
REMARK 500    TYR A  83       40.93    -84.23
REMARK 500    TYR A  88      -91.54   -121.29
REMARK 500    ASN A  96       89.07   -160.86
REMARK 500    PRO A  97     -179.38    -69.13
REMARK 500    GLU A  98       -0.44     65.71
REMARK 500    PRO A 132       -9.23    -52.98
REMARK 500    THR A 156      -66.23   -148.76
REMARK 500    ARG A 170      140.74   -170.53
REMARK 500    LYS A 180     -151.54     56.78
REMARK 500    GLU A 207      -43.72    -15.43
REMARK 500    SER A 211       68.31   -178.35
REMARK 500    PRO A 213       72.79    -65.43
REMARK 500    PHE A 214      -48.48   -174.17
REMARK 500    TYR A 242       83.53    -68.28
REMARK 500    ARG A 297       35.98    -72.56
REMARK 500    ASN A 308      -17.34   -176.83
REMARK 500    ALA A 333       96.59     59.09
REMARK 500    VAL A 334      -41.37     67.47
REMARK 500    GLU A 338      -65.69   -154.70
REMARK 500    ALA A 371       45.75     31.75
REMARK 500    GLN A 413       31.26    -98.52
REMARK 500    ASP A 438       92.24    -64.95
REMARK 500    LEU A 440      -76.00    -56.00
REMARK 500    TRP A 464       74.61   -112.58
REMARK 500    ARG I   2      122.84   -177.60
REMARK 500    THR I   4       38.91    -96.38
REMARK 500    PHE I   8       -1.98     68.80
REMARK 500    PRO I  41       46.50    -83.01
REMARK 500    ARG I  44       48.65     75.07
REMARK 500    ASN I  45       67.25   -104.76
REMARK 500    TYR I  47       61.65     77.05
REMARK 500    PHE I  56      -87.56    -60.49
REMARK 500    ASP I  57       56.16    -93.28
REMARK 500    ASP I  60       99.12   -165.15
REMARK 500    THR I  88      -31.22   -152.77
REMARK 500    HIS I  89       -5.25   -144.14
REMARK 500    THR I  90       82.51     55.65
REMARK 500    PHE I  98      -80.66   -115.72
REMARK 500
REMARK 500 THIS ENTRY HAS     215 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 G 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 G 508
DBREF  1BXN A    1   486  PDB    1BXN     1BXN             1    486
DBREF  1BXN I    1   139  PDB    1BXN     1BXN             1    139
DBREF  1BXN C    1   486  PDB    1BXN     1BXN             1    486
DBREF  1BXN J    1   139  PDB    1BXN     1BXN             1    139
DBREF  1BXN E    1   486  PDB    1BXN     1BXN             1    486
DBREF  1BXN K    1   139  PDB    1BXN     1BXN             1    139
DBREF  1BXN G    1   486  PDB    1BXN     1BXN             1    486
DBREF  1BXN L    1   139  PDB    1BXN     1BXN             1    139
SEQRES   1 A  485  MET ASN ALA PRO GLU SER VAL GLN ALA LYS PRO ARG LYS
SEQRES   2 A  485  ARG TYR ASP ALA GLY VAL MET LYS TYR LYS MET GLY TYR
SEQRES   3 A  485  TRP ASP GLY ASP TYR VAL PRO LYS ASP THR ASP LEU LEU
SEQRES   4 A  485  ALA LEU PHE ARG ILE THR PRO GLN ASP GLY VAL ASP PRO
SEQRES   5 A  485  VAL GLU ALA ALA ALA ALA VAL ALA GLY GLU SER SER THR
SEQRES   6 A  485  ALA THR TRP THR VAL VAL TRP THR ASP ARG LEU THR ALA
SEQRES   7 A  485  CYS ASP MET TYR ARG ALA LYS ALA TYR ARG VAL ASP PRO
SEQRES   8 A  485  VAL PRO ASN ASN PRO GLU GLN PHE PHE CYS TYR VAL ALA
SEQRES   9 A  485  TYR ASP LEU SER LEU PHE GLU GLU GLY SER ILE ALA ASN
SEQRES  10 A  485  LEU THR ALA SER ILE ILE GLY ASN VAL PHE SER PHE LYS
SEQRES  11 A  485  PRO ILE LYS ALA ALA ARG LEU GLU ASP MET ARG PHE PRO
SEQRES  12 A  485  VAL ALA TYR VAL LYS THR PHE ALA GLY PRO SER THR GLY
SEQRES  13 A  485  ILE ILE VAL GLU ARG GLU ARG LEU ASP LYS PHE GLY ARG
SEQRES  14 A  485  PRO LEU LEU GLY ALA THR THR LYS PRO LYS LEU GLY LEU
SEQRES  15 A  485  SER GLY ARG ASN TYR GLY ARG VAL VAL TYR GLU GLY LEU
SEQRES  16 A  485  LYS GLY GLY LEU ASP PHE MET LYS ASP ASP GLU ASN ILE
SEQRES  17 A  485  ASN SER GLN PRO PHE MET HIS TRP ARG ASP ARG PHE LEU
SEQRES  18 A  485  PHE VAL MET ASP ALA VAL ASN LYS ALA SER ALA ALA THR
SEQRES  19 A  485  GLY GLU VAL LYS GLY SER TYR LEU ASN VAL THR ALA GLY
SEQRES  20 A  485  THR MET GLU GLU MET TYR ARG ARG ALA GLU PHE ALA LYS
SEQRES  21 A  485  SER LEU GLY SER VAL ILE ILE MET VAL ASP LEU ILE VAL
SEQRES  22 A  485  GLY TRP THR CYS ILE GLN SER MET SER ASN TRP CYS ARG
SEQRES  23 A  485  GLN ASN ASP MET ILE LEU HIS LEU HIS ARG ALA GLY HIS
SEQRES  24 A  485  GLY THR TYR THR ARG GLN LYS ASN HIS GLY VAL SER PHE
SEQRES  25 A  485  ARG VAL ILE ALA LYS TRP LEU ARG LEU ALA GLY VAL ASP
SEQRES  26 A  485  HIS MET HIS THR GLY THR ALA VAL GLY LYS LEU GLU GLY
SEQRES  27 A  485  ASP PRO LEU THR VAL GLN GLY TYR TYR ASN VAL CYS ARG
SEQRES  28 A  485  ASP ALA TYR THR GLN THR ASP LEU THR ARG GLY LEU PHE
SEQRES  29 A  485  PHE ASP GLN ASP TRP ALA SER LEU ARG LYS VAL MET PRO
SEQRES  30 A  485  VAL ALA SER GLY GLY ILE HIS ALA GLY GLN MET HIS GLN
SEQRES  31 A  485  LEU ILE HIS LEU PHE GLY ASP ASP VAL VAL LEU GLN PHE
SEQRES  32 A  485  GLY GLY GLY THR ILE GLY HIS PRO GLN GLY ILE GLN ALA
SEQRES  33 A  485  GLY ALA THR ALA ASN ARG VAL ALA LEU GLU ALA MET VAL
SEQRES  34 A  485  LEU ALA ARG ASN GLU GLY ARG ASP ILE LEU ASN GLU GLY
SEQRES  35 A  485  PRO GLU ILE LEU ARG ASP ALA ALA ARG TRP CYS GLY PRO
SEQRES  36 A  485  LEU ARG ALA ALA LEU ASP THR TRP GLY ASP ILE SER PHE
SEQRES  37 A  485  ASN TYR THR PRO THR ASP THR SER ASP PHE ALA PRO THR
SEQRES  38 A  485  ALA SER VAL ALA
SEQRES   1 I  139  MET ARG ILE THR GLN GLY THR PHE SER PHE LEU PRO GLU
SEQRES   2 I  139  LEU THR ASP GLU GLN ILE THR LYS GLN LEU GLU TYR CYS
SEQRES   3 I  139  LEU ASN GLN GLY TRP ALA VAL GLY LEU GLU TYR THR ASP
SEQRES   4 I  139  ASP PRO HIS PRO ARG ASN THR TYR TRP GLU MET PHE GLY
SEQRES   5 I  139  LEU PRO MET PHE ASP LEU ARG ASP ALA ALA GLY ILE LEU
SEQRES   6 I  139  MET GLU ILE ASN ASN ALA ARG ASN THR PHE PRO ASN HIS
SEQRES   7 I  139  TYR ILE ARG VAL THR ALA PHE ASP SER THR HIS THR VAL
SEQRES   8 I  139  GLU SER VAL VAL MET SER PHE ILE VAL ASN ARG PRO ALA
SEQRES   9 I  139  ASP GLU PRO GLY PHE ARG LEU VAL ARG GLN GLU GLU PRO
SEQRES  10 I  139  GLY ARG THR LEU ARG TYR SER ILE GLU SER TYR ALA VAL
SEQRES  11 I  139  GLN ALA GLY PRO GLU GLY SER ARG TYR
SEQRES   1 C  485  MET ASN ALA PRO GLU SER VAL GLN ALA LYS PRO ARG LYS
SEQRES   2 C  485  ARG TYR ASP ALA GLY VAL MET LYS TYR LYS MET GLY TYR
SEQRES   3 C  485  TRP ASP GLY ASP TYR VAL PRO LYS ASP THR ASP LEU LEU
SEQRES   4 C  485  ALA LEU PHE ARG ILE THR PRO GLN ASP GLY VAL ASP PRO
SEQRES   5 C  485  VAL GLU ALA ALA ALA ALA VAL ALA GLY GLU SER SER THR
SEQRES   6 C  485  ALA THR TRP THR VAL VAL TRP THR ASP ARG LEU THR ALA
SEQRES   7 C  485  CYS ASP MET TYR ARG ALA LYS ALA TYR ARG VAL ASP PRO
SEQRES   8 C  485  VAL PRO ASN ASN PRO GLU GLN PHE PHE CYS TYR VAL ALA
SEQRES   9 C  485  TYR ASP LEU SER LEU PHE GLU GLU GLY SER ILE ALA ASN
SEQRES  10 C  485  LEU THR ALA SER ILE ILE GLY ASN VAL PHE SER PHE LYS
SEQRES  11 C  485  PRO ILE LYS ALA ALA ARG LEU GLU ASP MET ARG PHE PRO
SEQRES  12 C  485  VAL ALA TYR VAL LYS THR PHE ALA GLY PRO SER THR GLY
SEQRES  13 C  485  ILE ILE VAL GLU ARG GLU ARG LEU ASP LYS PHE GLY ARG
SEQRES  14 C  485  PRO LEU LEU GLY ALA THR THR LYS PRO LYS LEU GLY LEU
SEQRES  15 C  485  SER GLY ARG ASN TYR GLY ARG VAL VAL TYR GLU GLY LEU
SEQRES  16 C  485  LYS GLY GLY LEU ASP PHE MET LYS ASP ASP GLU ASN ILE
SEQRES  17 C  485  ASN SER GLN PRO PHE MET HIS TRP ARG ASP ARG PHE LEU
SEQRES  18 C  485  PHE VAL MET ASP ALA VAL ASN LYS ALA SER ALA ALA THR
SEQRES  19 C  485  GLY GLU VAL LYS GLY SER TYR LEU ASN VAL THR ALA GLY
SEQRES  20 C  485  THR MET GLU GLU MET TYR ARG ARG ALA GLU PHE ALA LYS
SEQRES  21 C  485  SER LEU GLY SER VAL ILE ILE MET VAL ASP LEU ILE VAL
SEQRES  22 C  485  GLY TRP THR CYS ILE GLN SER MET SER ASN TRP CYS ARG
SEQRES  23 C  485  GLN ASN ASP MET ILE LEU HIS LEU HIS ARG ALA GLY HIS
SEQRES  24 C  485  GLY THR TYR THR ARG GLN LYS ASN HIS GLY VAL SER PHE
SEQRES  25 C  485  ARG VAL ILE ALA LYS TRP LEU ARG LEU ALA GLY VAL ASP
SEQRES  26 C  485  HIS MET HIS THR GLY THR ALA VAL GLY LYS LEU GLU GLY
SEQRES  27 C  485  ASP PRO LEU THR VAL GLN GLY TYR TYR ASN VAL CYS ARG
SEQRES  28 C  485  ASP ALA TYR THR GLN THR ASP LEU THR ARG GLY LEU PHE
SEQRES  29 C  485  PHE ASP GLN ASP TRP ALA SER LEU ARG LYS VAL MET PRO
SEQRES  30 C  485  VAL ALA SER GLY GLY ILE HIS ALA GLY GLN MET HIS GLN
SEQRES  31 C  485  LEU ILE HIS LEU PHE GLY ASP ASP VAL VAL LEU GLN PHE
SEQRES  32 C  485  GLY GLY GLY THR ILE GLY HIS PRO GLN GLY ILE GLN ALA
SEQRES  33 C  485  GLY ALA THR ALA ASN ARG VAL ALA LEU GLU ALA MET VAL
SEQRES  34 C  485  LEU ALA ARG ASN GLU GLY ARG ASP ILE LEU ASN GLU GLY
SEQRES  35 C  485  PRO GLU ILE LEU ARG ASP ALA ALA ARG TRP CYS GLY PRO
SEQRES  36 C  485  LEU ARG ALA ALA LEU ASP THR TRP GLY ASP ILE SER PHE
SEQRES  37 C  485  ASN TYR THR PRO THR ASP THR SER ASP PHE ALA PRO THR
SEQRES  38 C  485  ALA SER VAL ALA
SEQRES   1 J  139  MET ARG ILE THR GLN GLY THR PHE SER PHE LEU PRO GLU
SEQRES   2 J  139  LEU THR ASP GLU GLN ILE THR LYS GLN LEU GLU TYR CYS
SEQRES   3 J  139  LEU ASN GLN GLY TRP ALA VAL GLY LEU GLU TYR THR ASP
SEQRES   4 J  139  ASP PRO HIS PRO ARG ASN THR TYR TRP GLU MET PHE GLY
SEQRES   5 J  139  LEU PRO MET PHE ASP LEU ARG ASP ALA ALA GLY ILE LEU
SEQRES   6 J  139  MET GLU ILE ASN ASN ALA ARG ASN THR PHE PRO ASN HIS
SEQRES   7 J  139  TYR ILE ARG VAL THR ALA PHE ASP SER THR HIS THR VAL
SEQRES   8 J  139  GLU SER VAL VAL MET SER PHE ILE VAL ASN ARG PRO ALA
SEQRES   9 J  139  ASP GLU PRO GLY PHE ARG LEU VAL ARG GLN GLU GLU PRO
SEQRES  10 J  139  GLY ARG THR LEU ARG TYR SER ILE GLU SER TYR ALA VAL
SEQRES  11 J  139  GLN ALA GLY PRO GLU GLY SER ARG TYR
SEQRES   1 E  485  MET ASN ALA PRO GLU SER VAL GLN ALA LYS PRO ARG LYS
SEQRES   2 E  485  ARG TYR ASP ALA GLY VAL MET LYS TYR LYS MET GLY TYR
SEQRES   3 E  485  TRP ASP GLY ASP TYR VAL PRO LYS ASP THR ASP LEU LEU
SEQRES   4 E  485  ALA LEU PHE ARG ILE THR PRO GLN ASP GLY VAL ASP PRO
SEQRES   5 E  485  VAL GLU ALA ALA ALA ALA VAL ALA GLY GLU SER SER THR
SEQRES   6 E  485  ALA THR TRP THR VAL VAL TRP THR ASP ARG LEU THR ALA
SEQRES   7 E  485  CYS ASP MET TYR ARG ALA LYS ALA TYR ARG VAL ASP PRO
SEQRES   8 E  485  VAL PRO ASN ASN PRO GLU GLN PHE PHE CYS TYR VAL ALA
SEQRES   9 E  485  TYR ASP LEU SER LEU PHE GLU GLU GLY SER ILE ALA ASN
SEQRES  10 E  485  LEU THR ALA SER ILE ILE GLY ASN VAL PHE SER PHE LYS
SEQRES  11 E  485  PRO ILE LYS ALA ALA ARG LEU GLU ASP MET ARG PHE PRO
SEQRES  12 E  485  VAL ALA TYR VAL LYS THR PHE ALA GLY PRO SER THR GLY
SEQRES  13 E  485  ILE ILE VAL GLU ARG GLU ARG LEU ASP LYS PHE GLY ARG
SEQRES  14 E  485  PRO LEU LEU GLY ALA THR THR LYS PRO LYS LEU GLY LEU
SEQRES  15 E  485  SER GLY ARG ASN TYR GLY ARG VAL VAL TYR GLU GLY LEU
SEQRES  16 E  485  LYS GLY GLY LEU ASP PHE MET LYS ASP ASP GLU ASN ILE
SEQRES  17 E  485  ASN SER GLN PRO PHE MET HIS TRP ARG ASP ARG PHE LEU
SEQRES  18 E  485  PHE VAL MET ASP ALA VAL ASN LYS ALA SER ALA ALA THR
SEQRES  19 E  485  GLY GLU VAL LYS GLY SER TYR LEU ASN VAL THR ALA GLY
SEQRES  20 E  485  THR MET GLU GLU MET TYR ARG ARG ALA GLU PHE ALA LYS
SEQRES  21 E  485  SER LEU GLY SER VAL ILE ILE MET VAL ASP LEU ILE VAL
SEQRES  22 E  485  GLY TRP THR CYS ILE GLN SER MET SER ASN TRP CYS ARG
SEQRES  23 E  485  GLN ASN ASP MET ILE LEU HIS LEU HIS ARG ALA GLY HIS
SEQRES  24 E  485  GLY THR TYR THR ARG GLN LYS ASN HIS GLY VAL SER PHE
SEQRES  25 E  485  ARG VAL ILE ALA LYS TRP LEU ARG LEU ALA GLY VAL ASP
SEQRES  26 E  485  HIS MET HIS THR GLY THR ALA VAL GLY LYS LEU GLU GLY
SEQRES  27 E  485  ASP PRO LEU THR VAL GLN GLY TYR TYR ASN VAL CYS ARG
SEQRES  28 E  485  ASP ALA TYR THR GLN THR ASP LEU THR ARG GLY LEU PHE
SEQRES  29 E  485  PHE ASP GLN ASP TRP ALA SER LEU ARG LYS VAL MET PRO
SEQRES  30 E  485  VAL ALA SER GLY GLY ILE HIS ALA GLY GLN MET HIS GLN
SEQRES  31 E  485  LEU ILE HIS LEU PHE GLY ASP ASP VAL VAL LEU GLN PHE
SEQRES  32 E  485  GLY GLY GLY THR ILE GLY HIS PRO GLN GLY ILE GLN ALA
SEQRES  33 E  485  GLY ALA THR ALA ASN ARG VAL ALA LEU GLU ALA MET VAL
SEQRES  34 E  485  LEU ALA ARG ASN GLU GLY ARG ASP ILE LEU ASN GLU GLY
SEQRES  35 E  485  PRO GLU ILE LEU ARG ASP ALA ALA ARG TRP CYS GLY PRO
SEQRES  36 E  485  LEU ARG ALA ALA LEU ASP THR TRP GLY ASP ILE SER PHE
SEQRES  37 E  485  ASN TYR THR PRO THR ASP THR SER ASP PHE ALA PRO THR
SEQRES  38 E  485  ALA SER VAL ALA
SEQRES   1 K  139  MET ARG ILE THR GLN GLY THR PHE SER PHE LEU PRO GLU
SEQRES   2 K  139  LEU THR ASP GLU GLN ILE THR LYS GLN LEU GLU TYR CYS
SEQRES   3 K  139  LEU ASN GLN GLY TRP ALA VAL GLY LEU GLU TYR THR ASP
SEQRES   4 K  139  ASP PRO HIS PRO ARG ASN THR TYR TRP GLU MET PHE GLY
SEQRES   5 K  139  LEU PRO MET PHE ASP LEU ARG ASP ALA ALA GLY ILE LEU
SEQRES   6 K  139  MET GLU ILE ASN ASN ALA ARG ASN THR PHE PRO ASN HIS
SEQRES   7 K  139  TYR ILE ARG VAL THR ALA PHE ASP SER THR HIS THR VAL
SEQRES   8 K  139  GLU SER VAL VAL MET SER PHE ILE VAL ASN ARG PRO ALA
SEQRES   9 K  139  ASP GLU PRO GLY PHE ARG LEU VAL ARG GLN GLU GLU PRO
SEQRES  10 K  139  GLY ARG THR LEU ARG TYR SER ILE GLU SER TYR ALA VAL
SEQRES  11 K  139  GLN ALA GLY PRO GLU GLY SER ARG TYR
SEQRES   1 G  485  MET ASN ALA PRO GLU SER VAL GLN ALA LYS PRO ARG LYS
SEQRES   2 G  485  ARG TYR ASP ALA GLY VAL MET LYS TYR LYS MET GLY TYR
SEQRES   3 G  485  TRP ASP GLY ASP TYR VAL PRO LYS ASP THR ASP LEU LEU
SEQRES   4 G  485  ALA LEU PHE ARG ILE THR PRO GLN ASP GLY VAL ASP PRO
SEQRES   5 G  485  VAL GLU ALA ALA ALA ALA VAL ALA GLY GLU SER SER THR
SEQRES   6 G  485  ALA THR TRP THR VAL VAL TRP THR ASP ARG LEU THR ALA
SEQRES   7 G  485  CYS ASP MET TYR ARG ALA LYS ALA TYR ARG VAL ASP PRO
SEQRES   8 G  485  VAL PRO ASN ASN PRO GLU GLN PHE PHE CYS TYR VAL ALA
SEQRES   9 G  485  TYR ASP LEU SER LEU PHE GLU GLU GLY SER ILE ALA ASN
SEQRES  10 G  485  LEU THR ALA SER ILE ILE GLY ASN VAL PHE SER PHE LYS
SEQRES  11 G  485  PRO ILE LYS ALA ALA ARG LEU GLU ASP MET ARG PHE PRO
SEQRES  12 G  485  VAL ALA TYR VAL LYS THR PHE ALA GLY PRO SER THR GLY
SEQRES  13 G  485  ILE ILE VAL GLU ARG GLU ARG LEU ASP LYS PHE GLY ARG
SEQRES  14 G  485  PRO LEU LEU GLY ALA THR THR LYS PRO LYS LEU GLY LEU
SEQRES  15 G  485  SER GLY ARG ASN TYR GLY ARG VAL VAL TYR GLU GLY LEU
SEQRES  16 G  485  LYS GLY GLY LEU ASP PHE MET LYS ASP ASP GLU ASN ILE
SEQRES  17 G  485  ASN SER GLN PRO PHE MET HIS TRP ARG ASP ARG PHE LEU
SEQRES  18 G  485  PHE VAL MET ASP ALA VAL ASN LYS ALA SER ALA ALA THR
SEQRES  19 G  485  GLY GLU VAL LYS GLY SER TYR LEU ASN VAL THR ALA GLY
SEQRES  20 G  485  THR MET GLU GLU MET TYR ARG ARG ALA GLU PHE ALA LYS
SEQRES  21 G  485  SER LEU GLY SER VAL ILE ILE MET VAL ASP LEU ILE VAL
SEQRES  22 G  485  GLY TRP THR CYS ILE GLN SER MET SER ASN TRP CYS ARG
SEQRES  23 G  485  GLN ASN ASP MET ILE LEU HIS LEU HIS ARG ALA GLY HIS
SEQRES  24 G  485  GLY THR TYR THR ARG GLN LYS ASN HIS GLY VAL SER PHE
SEQRES  25 G  485  ARG VAL ILE ALA LYS TRP LEU ARG LEU ALA GLY VAL ASP
SEQRES  26 G  485  HIS MET HIS THR GLY THR ALA VAL GLY LYS LEU GLU GLY
SEQRES  27 G  485  ASP PRO LEU THR VAL GLN GLY TYR TYR ASN VAL CYS ARG
SEQRES  28 G  485  ASP ALA TYR THR GLN THR ASP LEU THR ARG GLY LEU PHE
SEQRES  29 G  485  PHE ASP GLN ASP TRP ALA SER LEU ARG LYS VAL MET PRO
SEQRES  30 G  485  VAL ALA SER GLY GLY ILE HIS ALA GLY GLN MET HIS GLN
SEQRES  31 G  485  LEU ILE HIS LEU PHE GLY ASP ASP VAL VAL LEU GLN PHE
SEQRES  32 G  485  GLY GLY GLY THR ILE GLY HIS PRO GLN GLY ILE GLN ALA
SEQRES  33 G  485  GLY ALA THR ALA ASN ARG VAL ALA LEU GLU ALA MET VAL
SEQRES  34 G  485  LEU ALA ARG ASN GLU GLY ARG ASP ILE LEU ASN GLU GLY
SEQRES  35 G  485  PRO GLU ILE LEU ARG ASP ALA ALA ARG TRP CYS GLY PRO
SEQRES  36 G  485  LEU ARG ALA ALA LEU ASP THR TRP GLY ASP ILE SER PHE
SEQRES  37 G  485  ASN TYR THR PRO THR ASP THR SER ASP PHE ALA PRO THR
SEQRES  38 G  485  ALA SER VAL ALA
SEQRES   1 L  139  MET ARG ILE THR GLN GLY THR PHE SER PHE LEU PRO GLU
SEQRES   2 L  139  LEU THR ASP GLU GLN ILE THR LYS GLN LEU GLU TYR CYS
SEQRES   3 L  139  LEU ASN GLN GLY TRP ALA VAL GLY LEU GLU TYR THR ASP
SEQRES   4 L  139  ASP PRO HIS PRO ARG ASN THR TYR TRP GLU MET PHE GLY
SEQRES   5 L  139  LEU PRO MET PHE ASP LEU ARG ASP ALA ALA GLY ILE LEU
SEQRES   6 L  139  MET GLU ILE ASN ASN ALA ARG ASN THR PHE PRO ASN HIS
SEQRES   7 L  139  TYR ILE ARG VAL THR ALA PHE ASP SER THR HIS THR VAL
SEQRES   8 L  139  GLU SER VAL VAL MET SER PHE ILE VAL ASN ARG PRO ALA
SEQRES   9 L  139  ASP GLU PRO GLY PHE ARG LEU VAL ARG GLN GLU GLU PRO
SEQRES  10 L  139  GLY ARG THR LEU ARG TYR SER ILE GLU SER TYR ALA VAL
SEQRES  11 L  139  GLN ALA GLY PRO GLU GLY SER ARG TYR
HET    PO4  A 501       5
HET    PO4  A 502       5
HET    PO4  C 503       5
HET    PO4  C 504       5
HET    PO4  E 505       5
HET    PO4  E 506       5
HET    PO4  G 507       5
HET    PO4  G 508       5
HETNAM     PO4 PHOSPHATE ION
FORMUL   9  PO4    8(O4 P 3-)
HELIX    1   1 PRO A   53  GLY A   62  1                                  10
HELIX    2   2 THR A   74  THR A   78  5                                   5
HELIX    3   3 ASP A   81  TYR A   83  5                                   3
HELIX    4   4 LEU A  108  LEU A  110  5                                   3
HELIX    5   5 ILE A  116  ILE A  124  1                                   9
HELIX    6   6 VAL A  127  SER A  129  5                                   3
HELIX    7   7 VAL A  145  THR A  150  1                                   6
HELIX    8   8 ILE A  158  LEU A  165  1                                   8
HELIX    9   9 GLY A  185  LYS A  197  1                                  13
HELIX   10  10 TRP A  217  THR A  235  1                                  19
HELIX   11  11 MET A  250  LEU A  263  1                                  14
HELIX   12  12 LEU A  272  VAL A  274  5                                   3
HELIX   13  13 TRP A  276  ASN A  289  1                                  14
HELIX   14  14 HIS A  300  THR A  304  5                                   5
HELIX   15  15 PHE A  313  ALA A  323  1                                  11
HELIX   16  16 PRO A  341  ARG A  352  1                                  12
HELIX   17  17 LEU A  360  ARG A  362  5                                   3
HELIX   18  18 ALA A  386  PHE A  396  5                                  11
HELIX   19  19 GLY A  406  ILE A  409  1                                   4
HELIX   20  20 GLY A  414  GLU A  435  1                                  22
HELIX   21  21 ILE A  439  TRP A  453  1                                  15
HELIX   22  22 GLY A  455  THR A  463  1                                   9
HELIX   23  23 ASP I   16  GLN I   29  1                                  14
HELIX   24  24 ALA I   61  THR I   74  1                                  14
HELIX   25  25 ARG I  102  ALA I  104  5                                   3
HELIX   26  26 PRO C   53  GLY C   62  1                                  10
HELIX   27  27 THR C   74  THR C   78  5                                   5
HELIX   28  28 ASP C   81  TYR C   83  5                                   3
HELIX   29  29 LEU C  108  LEU C  110  5                                   3
HELIX   30  30 ILE C  116  ILE C  124  1                                   9
HELIX   31  31 VAL C  127  SER C  129  5                                   3
HELIX   32  32 VAL C  145  THR C  150  1                                   6
HELIX   33  33 ILE C  158  LEU C  165  1                                   8
HELIX   34  34 GLY C  185  LYS C  197  1                                  13
HELIX   35  35 TRP C  217  THR C  235  1                                  19
HELIX   36  36 MET C  250  SER C  262  1                                  13
HELIX   37  37 LEU C  272  VAL C  274  5                                   3
HELIX   38  38 TRP C  276  ASN C  289  1                                  14
HELIX   39  39 HIS C  300  THR C  304  5                                   5
HELIX   40  40 PHE C  313  ALA C  323  1                                  11
HELIX   41  41 PRO C  341  ARG C  352  1                                  12
HELIX   42  42 LEU C  360  ARG C  362  5                                   3
HELIX   43  43 ALA C  386  LEU C  395  5                                  10
HELIX   44  44 GLY C  406  ILE C  409  1                                   4
HELIX   45  45 GLY C  414  GLU C  435  1                                  22
HELIX   46  46 ILE C  439  TRP C  453  1                                  15
HELIX   47  47 GLY C  455  THR C  463  1                                   9
HELIX   48  48 ASP J   16  GLN J   29  1                                  14
HELIX   49  49 ALA J   61  THR J   74  1                                  14
HELIX   50  50 ARG J  102  ALA J  104  5                                   3
HELIX   51  51 PRO E   53  GLY E   62  1                                  10
HELIX   52  52 THR E   74  THR E   78  5                                   5
HELIX   53  53 ASP E   81  TYR E   83  5                                   3
HELIX   54  54 LEU E  108  LEU E  110  5                                   3
HELIX   55  55 ILE E  116  ILE E  124  1                                   9
HELIX   56  56 VAL E  127  SER E  129  5                                   3
HELIX   57  57 VAL E  145  THR E  150  1                                   6
HELIX   58  58 ILE E  158  LEU E  165  1                                   8
HELIX   59  59 GLY E  185  LYS E  197  1                                  13
HELIX   60  60 TRP E  217  THR E  235  1                                  19
HELIX   61  61 MET E  250  LEU E  263  1                                  14
HELIX   62  62 LEU E  272  VAL E  274  5                                   3
HELIX   63  63 TRP E  276  ASN E  289  1                                  14
HELIX   64  64 HIS E  300  THR E  304  5                                   5
HELIX   65  65 PHE E  313  ALA E  323  1                                  11
HELIX   66  66 PRO E  341  ARG E  352  1                                  12
HELIX   67  67 LEU E  360  ARG E  362  5                                   3
HELIX   68  68 ALA E  386  PHE E  396  5                                  11
HELIX   69  69 GLY E  406  ILE E  409  1                                   4
HELIX   70  70 GLY E  414  GLU E  435  1                                  22
HELIX   71  71 ILE E  439  TRP E  453  1                                  15
HELIX   72  72 GLY E  455  THR E  463  1                                   9
HELIX   73  73 ASP K   16  GLN K   29  1                                  14
HELIX   74  74 ALA K   61  THR K   74  1                                  14
HELIX   75  75 ARG K  102  ALA K  104  5                                   3
HELIX   76  76 PRO G   53  GLY G   62  1                                  10
HELIX   77  77 THR G   74  THR G   78  5                                   5
HELIX   78  78 ASP G   81  TYR G   83  5                                   3
HELIX   79  79 LEU G  108  LEU G  110  5                                   3
HELIX   80  80 ILE G  116  ILE G  124  1                                   9
HELIX   81  81 VAL G  127  SER G  129  5                                   3
HELIX   82  82 VAL G  145  THR G  150  1                                   6
HELIX   83  83 ILE G  158  LEU G  165  1                                   8
HELIX   84  84 GLY G  185  LYS G  197  1                                  13
HELIX   85  85 TRP G  217  THR G  235  1                                  19
HELIX   86  86 MET G  250  LEU G  263  1                                  14
HELIX   87  87 LEU G  272  VAL G  274  5                                   3
HELIX   88  88 TRP G  276  ASN G  289  1                                  14
HELIX   89  89 HIS G  300  THR G  304  5                                   5
HELIX   90  90 PHE G  313  ALA G  323  1                                  11
HELIX   91  91 PRO G  341  ARG G  352  1                                  12
HELIX   92  92 LEU G  360  ARG G  362  5                                   3
HELIX   93  93 ALA G  386  PHE G  396  5                                  11
HELIX   94  94 GLY G  406  ILE G  409  1                                   4
HELIX   95  95 GLY G  414  GLU G  435  1                                  22
HELIX   96  96 ILE G  439  TRP G  453  1                                  15
HELIX   97  97 GLY G  455  THR G  463  1                                   9
HELIX   98  98 ASP L   16  GLN L   29  1                                  14
HELIX   99  99 ALA L   61  THR L   74  1                                  14
HELIX  100 100 ARG L  102  ALA L  104  5                                   3
SHEET    1   A 4 VAL A  90  PRO A  92  0
SHEET    2   A 4 PHE A 100  ASP A 107 -1  N  PHE A 101   O  ASP A  91
SHEET    3   A 4 ASP A  38  ILE A  45 -1  N  ILE A  45   O  PHE A 100
SHEET    4   A 4 LEU A 138  ARG A 142 -1  N  ARG A 142   O  LEU A  40
SHEET    1   B 6 GLY A 240  TYR A 242  0
SHEET    2   B 6 PHE A 202  LYS A 204  1  N  MET A 203   O  GLY A 240
SHEET    3   B 6 LEU A 172  THR A 176  1  N  ALA A 175   O  PHE A 202
SHEET    4   B 6 VAL A 400  PHE A 404  1  N  LEU A 402   O  LEU A 172
SHEET    5   B 6 MET A 377  GLY A 382  1  N  PRO A 378   O  VAL A 401
SHEET    6   B 6 HIS A 327  HIS A 329  1  N  MET A 328   O  MET A 377
SHEET    1   C 2 ILE A 267  ASP A 271  0
SHEET    2   C 2 ILE A 292  HIS A 296  1  N  ILE A 292   O  ILE A 268
SHEET    1   D 3 ALA I  32  THR I  38  0
SHEET    2   D 3 TYR I  79  ASP I  86 -1  N  PHE I  85   O  ALA I  32
SHEET    3   D 3 VAL I  91  SER I  97 -1  N  MET I  96   O  VAL I  82
SHEET    1   E 2 ARG I 110  GLU I 115  0
SHEET    2   E 2 LEU I 121  GLU I 126 -1  N  GLU I 126   O  ARG I 110
SHEET    1   F 4 VAL C  90  PRO C  92  0
SHEET    2   F 4 PHE C 100  ASP C 107 -1  N  PHE C 101   O  ASP C  91
SHEET    3   F 4 ASP C  38  ILE C  45 -1  N  ILE C  45   O  PHE C 100
SHEET    4   F 4 LEU C 138  ARG C 142 -1  N  ARG C 142   O  LEU C  40
SHEET    1   G 6 GLY C 240  TYR C 242  0
SHEET    2   G 6 PHE C 202  LYS C 204  1  N  MET C 203   O  GLY C 240
SHEET    3   G 6 LEU C 172  THR C 176  1  N  ALA C 175   O  PHE C 202
SHEET    4   G 6 VAL C 400  PHE C 404  1  N  LEU C 402   O  LEU C 172
SHEET    5   G 6 MET C 377  GLY C 382  1  N  PRO C 378   O  VAL C 401
SHEET    6   G 6 HIS C 327  HIS C 329  1  N  MET C 328   O  MET C 377
SHEET    1   H 2 ILE C 267  ASP C 271  0
SHEET    2   H 2 ILE C 292  HIS C 296  1  N  ILE C 292   O  ILE C 268
SHEET    1   I 3 ALA J  32  THR J  38  0
SHEET    2   I 3 TYR J  79  ASP J  86 -1  N  PHE J  85   O  ALA J  32
SHEET    3   I 3 VAL J  91  SER J  97 -1  N  MET J  96   O  VAL J  82
SHEET    1   J 2 ARG J 110  GLU J 115  0
SHEET    2   J 2 LEU J 121  GLU J 126 -1  N  GLU J 126   O  ARG J 110
SHEET    1   K 4 VAL E  90  PRO E  92  0
SHEET    2   K 4 PHE E 100  ASP E 107 -1  N  PHE E 101   O  ASP E  91
SHEET    3   K 4 ASP E  38  ILE E  45 -1  N  ILE E  45   O  PHE E 100
SHEET    4   K 4 LEU E 138  ARG E 142 -1  N  ARG E 142   O  LEU E  40
SHEET    1   L 6 GLY E 240  TYR E 242  0
SHEET    2   L 6 PHE E 202  LYS E 204  1  N  MET E 203   O  GLY E 240
SHEET    3   L 6 LEU E 172  THR E 176  1  N  ALA E 175   O  PHE E 202
SHEET    4   L 6 VAL E 400  PHE E 404  1  N  LEU E 402   O  LEU E 172
SHEET    5   L 6 MET E 377  GLY E 382  1  N  PRO E 378   O  VAL E 401
SHEET    6   L 6 HIS E 327  HIS E 329  1  N  MET E 328   O  MET E 377
SHEET    1   M 2 ILE E 267  ASP E 271  0
SHEET    2   M 2 ILE E 292  HIS E 296  1  N  ILE E 292   O  ILE E 268
SHEET    1   N 3 ALA K  32  THR K  38  0
SHEET    2   N 3 TYR K  79  ASP K  86 -1  N  PHE K  85   O  ALA K  32
SHEET    3   N 3 VAL K  91  SER K  97 -1  N  MET K  96   O  VAL K  82
SHEET    1   O 2 ARG K 110  GLU K 115  0
SHEET    2   O 2 LEU K 121  GLU K 126 -1  N  GLU K 126   O  ARG K 110
SHEET    1   P 4 VAL G  90  PRO G  92  0
SHEET    2   P 4 PHE G 100  ASP G 107 -1  N  PHE G 101   O  ASP G  91
SHEET    3   P 4 ASP G  38  ILE G  45 -1  N  ILE G  45   O  PHE G 100
SHEET    4   P 4 LEU G 138  ARG G 142 -1  N  ARG G 142   O  LEU G  40
SHEET    1   Q 6 GLY G 240  TYR G 242  0
SHEET    2   Q 6 PHE G 202  LYS G 204  1  N  MET G 203   O  GLY G 240
SHEET    3   Q 6 LEU G 172  THR G 176  1  N  ALA G 175   O  PHE G 202
SHEET    4   Q 6 VAL G 400  PHE G 404  1  N  LEU G 402   O  LEU G 172
SHEET    5   Q 6 MET G 377  GLY G 382  1  N  PRO G 378   O  VAL G 401
SHEET    6   Q 6 HIS G 327  HIS G 329  1  N  MET G 328   O  MET G 377
SHEET    1   R 2 ILE G 267  ASP G 271  0
SHEET    2   R 2 ILE G 292  HIS G 296  1  N  ILE G 292   O  ILE G 268
SHEET    1   S 3 ALA L  32  THR L  38  0
SHEET    2   S 3 TYR L  79  ASP L  86 -1  N  PHE L  85   O  ALA L  32
SHEET    3   S 3 VAL L  91  SER L  97 -1  N  MET L  96   O  VAL L  82
SHEET    1   T 2 ARG L 110  GLU L 115  0
SHEET    2   T 2 LEU L 121  GLU L 126 -1  N  GLU L 126   O  ARG L 110
SSBOND   1 CYS A  278    CYS E  278                          1555   8665  2.86
SSBOND   2 CYS C  278    CYS C  278                          1555   8665  2.78
SSBOND   3 CYS G  278    CYS G  278                          1555   8665  2.88
SITE     1 AC1  5 ARG A 297  HIS A 329  GLU A 338  SER A 381
SITE     2 AC1  5 ASN E 126
SITE     1 AC2  5 GLY A 382  GLY A 405  GLY A 406  THR E  68
SITE     2 AC2  5 TRP E  69
SITE     1 AC3  4 ARG C 297  HIS C 329  GLU C 338  SER C 381
SITE     1 AC4  6 THR C  68  TRP C  69  GLY C 382  GLY C 383
SITE     2 AC4  6 GLY C 405  GLY C 406
SITE     1 AC5  4 ARG E 297  HIS E 329  GLU E 338  SER E 381
SITE     1 AC6  5 THR A  68  TRP A  69  GLY E 382  GLY E 405
SITE     2 AC6  5 GLY E 406
SITE     1 AC7  4 ARG G 297  HIS G 329  GLU G 338  SER G 381
SITE     1 AC8  4 THR G  68  TRP G  69  GLY G 405  GLY G 406
CRYST1  112.000  112.000  402.700  90.00  90.00  90.00 P 43 21 2    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      0.008929  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008929  0.000000        0.00000
SCALE3      0.000000  0.000000  0.002483        0.00000
MTRIX1   1  0.013000 -0.987000  0.163000       93.96200    1
MTRIX2   1  1.000000  0.014000  0.001000      100.37800    1
MTRIX3   1 -0.003000  0.163000  0.987000      -16.07900    1
MTRIX1   2  0.014000 -0.986000  0.168000       93.52000    1
MTRIX2   2  1.000000  0.014000 -0.001000      100.51000    1
MTRIX3   2 -0.001000  0.168000  0.986000      -16.49300    1
MTRIX1   3 -0.987000  0.006000  0.160000       -6.82400    1
MTRIX2   3  0.020000 -0.987000  0.162000      196.01401    1
MTRIX3   3  0.159000  0.164000  0.974000      -15.70500    1
MTRIX1   4 -0.986000  0.012000  0.165000       -7.68900    1
MTRIX2   4  0.015000 -0.987000  0.162000      196.03500    1
MTRIX3   4  0.165000  0.162000  0.973000      -15.43400    1
MTRIX1   5  0.004000  1.000000  0.000000     -101.89000    1
MTRIX2   5 -0.987000  0.004000  0.161000       95.24400    1
MTRIX3   5  0.161000 -0.001000  0.987000        0.53300    1
MTRIX1   6  0.008000  1.000000  0.002000     -102.03200    1
MTRIX2   6 -0.986000  0.008000  0.166000       94.50700    1
MTRIX3   6  0.166000 -0.004000  0.986000        0.95800    1
      
PROCHECK
Go to PROCHECK summary
 References