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PDBsum entry 1rd5

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Top Page protein ligands Protein-protein interface(s) links
Lyase PDB id
1rd5
Jmol
Contents
Protein chains
261 a.a.
248 a.a.
Ligands
MLA ×2
Waters ×248
HEADER    LYASE                                   05-NOV-03   1RD5
TITLE     CRYSTAL STRUCTURE OF TRYPTOPHAN SYNTHASE ALPHA CHAIN HOMOLOG BX1: A
TITLE    2 MEMBER OF THE CHEMICAL PLANT DEFENSE SYSTEM
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TRYPTOPHAN SYNTHASE ALPHA CHAIN, CHLOROPLAST;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: BX1, TRYPTOPHAN SYNTHASE ALPHA HOMOLOG;
COMPND   5 EC: 4.2.1.20;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ZEA MAYS;
SOURCE   3 ORGANISM_TAXID: 4577;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    HYDROXAMIC ACID, DIBOA, DIMBOA, INDOLE, INDOLE-GLYCEROL-PHOSPHATE,
KEYWDS   2 LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    V.KULIK,E.HARTMANN,M.WEYAND,M.FREY,A.GIERL,D.NIKS,M.F.DUNN,
AUTHOR   2 I.SCHLICHTING
REVDAT   4   13-JUL-11 1RD5    1       VERSN
REVDAT   3   24-FEB-09 1RD5    1       VERSN
REVDAT   2   08-NOV-05 1RD5    1       AUTHOR JRNL
REVDAT   1   28-DEC-04 1RD5    0
JRNL        AUTH   V.KULIK,E.HARTMANN,M.WEYAND,M.FREY,A.GIERL,D.NIKS,M.F.DUNN,
JRNL        AUTH 2 I.SCHLICHTING
JRNL        TITL   ON THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND THE
JRNL        TITL 2 REGULATION OF THE ALPHA SUBUNIT OF TRYPTOPHAN SYNTHASE FROM
JRNL        TITL 3 SALMONELLA TYPHIMURIUM AND BX1 FROM MAIZE, TWO
JRNL        TITL 4 EVOLUTIONARILY RELATED ENZYMES.
JRNL        REF    J.MOL.BIOL.                   V. 352   608 2005
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   16120446
JRNL        DOI    10.1016/J.JMB.2005.07.014
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   M.FREY,P.CHOMET,E.GLAWISCHNIG,C.STETTNER,S.GRUN,A.WINKLMAIR,
REMARK   1  AUTH 2 W.EISENREICH,A.BACHER,R.B.MEELEY,S.P.BRIGGS,K.SIMCOX,A.GIERL
REMARK   1  TITL   ANALYSIS OF A CHEMICAL PLANT DEFENSE MECHANISM IN GRASSES
REMARK   1  REF    SCIENCE                       V. 277   696 1997
REMARK   1  REFN                   ISSN 0036-8075
REMARK   1  DOI    10.1126/SCIENCE.277.5326.696
REMARK   2
REMARK   2 RESOLUTION.    2.02 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.1.19
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.02
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 35151
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) : 0.248
REMARK   3   R VALUE            (WORKING SET) : 0.245
REMARK   3   FREE R VALUE                     : 0.299
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1851
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.02
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.07
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1234
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.5120
REMARK   3   BIN FREE R VALUE SET COUNT          : 76
REMARK   3   BIN FREE R VALUE                    : 0.6880
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3796
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 14
REMARK   3   SOLVENT ATOMS            : 248
REMARK   3
REMARK   3  B VALUES.
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.01
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.90000
REMARK   3    B22 (A**2) : -0.57000
REMARK   3    B33 (A**2) : -0.33000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.235
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.209
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.116
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.305
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.915
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3908 ; 0.046 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  3740 ; 0.002 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5300 ; 3.021 ; 1.990
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8714 ; 1.695 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   505 ; 7.321 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   624 ; 0.206 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4283 ; 0.015 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):   700 ; 0.011 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   757 ; 0.247 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4074 ; 0.252 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2294 ; 0.110 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   194 ; 0.211 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    16 ; 0.264 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    67 ; 0.275 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     9 ; 0.313 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2537 ; 1.776 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4090 ; 2.763 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1371 ; 4.553 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1210 ; 7.032 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 2
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A     2        A   262
REMARK   3    ORIGIN FOR THE GROUP (A):  40.4980  23.2510  17.8950
REMARK   3    T TENSOR
REMARK   3      T11:   0.0784 T22:   0.0524
REMARK   3      T33:   0.0314 T12:   0.0153
REMARK   3      T13:   0.0472 T23:   0.0214
REMARK   3    L TENSOR
REMARK   3      L11:   1.7889 L22:   2.4837
REMARK   3      L33:   2.2384 L12:   0.6967
REMARK   3      L13:  -0.2639 L23:   0.6786
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0248 S12:   0.0689 S13:  -0.0658
REMARK   3      S21:  -0.0703 S22:  -0.0095 S23:  -0.0632
REMARK   3      S31:   0.0837 S32:   0.0190 S33:   0.0343
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 3
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B     2        B    58
REMARK   3    RESIDUE RANGE :   B    61        B   175
REMARK   3    RESIDUE RANGE :   B   187        B   262
REMARK   3    ORIGIN FOR THE GROUP (A):   5.6930  17.2730  27.8730
REMARK   3    T TENSOR
REMARK   3      T11:   0.0930 T22:   0.0513
REMARK   3      T33:   0.0627 T12:  -0.0426
REMARK   3      T13:  -0.0019 T23:   0.0278
REMARK   3    L TENSOR
REMARK   3      L11:   2.3490 L22:   1.9642
REMARK   3      L33:   1.4619 L12:  -0.2828
REMARK   3      L13:  -0.3373 L23:   0.8976
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0849 S12:   0.2516 S13:   0.1003
REMARK   3      S21:  -0.2520 S22:   0.0536 S23:   0.0719
REMARK   3      S31:  -0.1321 S32:  -0.0454 S33:   0.0313
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 1RD5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-NOV-03.
REMARK 100 THE RCSB ID CODE IS RCSB020662.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 07-MAY-01
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.3
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) : 0.934
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200  DATA SCALING SOFTWARE          : XDS
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37043
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.7
REMARK 200  DATA REDUNDANCY                : 5.700
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.07800
REMARK 200   FOR THE DATA SET  : 13.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10
REMARK 200  COMPLETENESS FOR SHELL     (%) : 52.7
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.34000
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 53.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MALONATE, PH 7.3, VAPOR DIFFUSION,
REMARK 280  HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 2 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X,Y,-Z
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X,Y+1/2,Z+1/2
REMARK 290       6555   -X,-Y+1/2,Z+1/2
REMARK 290       7555   -X,Y+1/2,-Z+1/2
REMARK 290       8555   X,-Y+1/2,-Z+1/2
REMARK 290       9555   X+1/2,Y,Z+1/2
REMARK 290      10555   -X+1/2,-Y,Z+1/2
REMARK 290      11555   -X+1/2,Y,-Z+1/2
REMARK 290      12555   X+1/2,-Y,-Z+1/2
REMARK 290      13555   X+1/2,Y+1/2,Z
REMARK 290      14555   -X+1/2,-Y+1/2,Z
REMARK 290      15555   -X+1/2,Y+1/2,-Z
REMARK 290      16555   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        0.00000
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        0.00000
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        0.00000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       79.90750
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       81.43850
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       79.90750
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       81.43850
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       79.90750
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       81.43850
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       79.90750
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       81.43850
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       45.54700
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       81.43850
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       45.54700
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       81.43850
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000       45.54700
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       81.43850
REMARK 290   SMTRY1  12  1.000000  0.000000  0.000000       45.54700
REMARK 290   SMTRY2  12  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       81.43850
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000       45.54700
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       79.90750
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000       45.54700
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       79.90750
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       45.54700
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000       79.90750
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000       45.54700
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000       79.90750
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 22160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 74380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -143.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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       79.90750
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       81.43850
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000       45.54700
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000       81.43850
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000       45.54700
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000       79.90750
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH A 409  LIES ON A SPECIAL POSITION.
REMARK 375      HOH B 330  LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A     1
REMARK 465     MET B     1
REMARK 465     TYR B    59
REMARK 465     ILE B    60
REMARK 465     ASN B   176
REMARK 465     GLY B   177
REMARK 465     VAL B   178
REMARK 465     THR B   179
REMARK 465     GLY B   180
REMARK 465     PRO B   181
REMARK 465     ARG B   182
REMARK 465     ALA B   183
REMARK 465     ASN B   184
REMARK 465     VAL B   185
REMARK 465     ASN B   186
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 108    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     ARG A 109    CG   CD   NE   CZ   NH1  NH2
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   OE1  GLN B   245     O    HOH B   364              2.16
REMARK 500   O    SER A   174     O    HOH A   405              2.19
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    GLU A  36   CD    GLU A  36   OE2     0.080
REMARK 500    CYS A  44   CB    CYS A  44   SG      0.114
REMARK 500    GLU A  84   CG    GLU A  84   CD      0.128
REMARK 500    GLU A  84   CD    GLU A  84   OE1     0.067
REMARK 500    GLU A  84   CD    GLU A  84   OE2     0.095
REMARK 500    ARG A  87   CG    ARG A  87   CD      0.150
REMARK 500    GLU A  88   CG    GLU A  88   CD      0.096
REMARK 500    GLU A  88   CD    GLU A  88   OE2     0.084
REMARK 500    GLU A  92   CD    GLU A  92   OE1     0.067
REMARK 500    VAL A  97   CB    VAL A  97   CG1     0.138
REMARK 500    TYR A 103   CB    TYR A 103   CG     -0.118
REMARK 500    PHE A 108   CA    PHE A 108   CB      0.159
REMARK 500    ARG A 109   CA    ARG A 109   CB      0.186
REMARK 500    ARG A 109   C     ARG A 109   O       0.118
REMARK 500    MET A 114   SD    MET A 114   CE     -0.481
REMARK 500    VAL A 130   CB    VAL A 130   CG2    -0.195
REMARK 500    GLN A 194   CG    GLN A 194   CD      0.167
REMARK 500    LYS A 197   CE    LYS A 197   NZ      0.150
REMARK 500    ALA A 220   CA    ALA A 220   CB      0.137
REMARK 500    TRP A 222   CB    TRP A 222   CG     -0.129
REMARK 500    SER A 231   CB    SER A 231   OG      0.128
REMARK 500    LYS A 244   CD    LYS A 244   CE      0.190
REMARK 500    ARG A 255   CG    ARG A 255   CD      0.159
REMARK 500    ARG A 255   NE    ARG A 255   CZ      0.090
REMARK 500    LYS A 258   CD    LYS A 258   CE      0.212
REMARK 500    GLU B  50   CD    GLU B  50   OE1     0.074
REMARK 500    PRO B  58   CA    PRO B  58   C       0.139
REMARK 500    SER B  75   CB    SER B  75   OG      0.088
REMARK 500    VAL B  89   CB    VAL B  89   CG2     0.147
REMARK 500    TYR B 102   CB    TYR B 102   CG      0.097
REMARK 500    TYR B 102   CG    TYR B 102   CD2     0.148
REMARK 500    TYR B 102   CG    TYR B 102   CD1     0.111
REMARK 500    TYR B 102   CD1   TYR B 102   CE1     0.154
REMARK 500    MET B 107   CG    MET B 107   SD      0.232
REMARK 500    LYS B 115   CD    LYS B 115   CE      0.153
REMARK 500    GLU B 116   CD    GLU B 116   OE1     0.084
REMARK 500    GLU B 116   CD    GLU B 116   OE2     0.092
REMARK 500    SER B 137   CA    SER B 137   CB      0.104
REMARK 500    GLU B 138   CD    GLU B 138   OE1     0.067
REMARK 500    GLU B 167   CD    GLU B 167   OE2     0.078
REMARK 500    VAL B 173   CB    VAL B 173   CG1    -0.232
REMARK 500    ARG B 188   CG    ARG B 188   CD      0.170
REMARK 500    GLU B 195   CD    GLU B 195   OE2     0.068
REMARK 500    LYS B 198   CD    LYS B 198   CE      0.169
REMARK 500    VAL B 206   CB    VAL B 206   CG1    -0.154
REMARK 500    LYS B 212   CE    LYS B 212   NZ      0.182
REMARK 500    SER B 231   CB    SER B 231   OG     -0.084
REMARK 500    VAL B 234   CB    VAL B 234   CG2    -0.150
REMARK 500    GLU B 252   CD    GLU B 252   OE2     0.083
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ARG A   3   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES
REMARK 500    ASP A  30   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES
REMARK 500    ARG A  39   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    ASP A  61   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES
REMARK 500    LEU A  73   CB  -  CG  -  CD1 ANGL. DEV. = -12.8 DEGREES
REMARK 500    LYS A 104   CD  -  CE  -  NZ  ANGL. DEV. = -22.0 DEGREES
REMARK 500    LEU A 149   CB  -  CG  -  CD1 ANGL. DEV. =  12.6 DEGREES
REMARK 500    ARG A 158   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 DEGREES
REMARK 500    TYR A 171   CB  -  CG  -  CD2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    TYR A 171   CB  -  CG  -  CD1 ANGL. DEV. =   4.5 DEGREES
REMARK 500    ARG A 248   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES
REMARK 500    ARG A 255   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    LYS B  17   CD  -  CE  -  NZ  ANGL. DEV. = -20.0 DEGREES
REMARK 500    LEU B  31   CB  -  CG  -  CD1 ANGL. DEV. = -11.1 DEGREES
REMARK 500    ARG B  39   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES
REMARK 500    LEU B  40   CA  -  CB  -  CG  ANGL. DEV. =  15.4 DEGREES
REMARK 500    ASP B  42   CB  -  CG  -  OD2 ANGL. DEV. =   7.0 DEGREES
REMARK 500    GLU B  50   OE1 -  CD  -  OE2 ANGL. DEV. =   7.5 DEGREES
REMARK 500    ASP B  61   CB  -  CA  -  C   ANGL. DEV. =  24.9 DEGREES
REMARK 500    GLN B  66   CA  -  CB  -  CG  ANGL. DEV. =  14.5 DEGREES
REMARK 500    ARG B  87   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES
REMARK 500    LEU B 111   CB  -  CG  -  CD2 ANGL. DEV. =  10.2 DEGREES
REMARK 500    LYS B 115   CD  -  CE  -  NZ  ANGL. DEV. = -19.3 DEGREES
REMARK 500    LYS B 244   CD  -  CE  -  NZ  ANGL. DEV. = -14.8 DEGREES
REMARK 500    MET B 257   CG  -  SD  -  CE  ANGL. DEV. = -15.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    PHE B 208      -36.70   -173.37
REMARK 500    GLU B 239       46.29   -108.43
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 ARG A  109     SER A  110                  126.26
REMARK 500 ASP B   61     GLY B   62                 -147.25
REMARK 500 VAL B  206     GLY B  207                  148.68
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 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
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    THR A  90        19.7      L          L   OUTSIDE RANGE
REMARK 500    LYS A 104        24.1      L          L   OUTSIDE RANGE
REMARK 500    PHE A 108        23.0      L          L   OUTSIDE RANGE
REMARK 500    ARG A 109        23.9      L          L   OUTSIDE RANGE
REMARK 500    VAL A 189        23.9      L          L   OUTSIDE RANGE
REMARK 500    THR B  90        24.6      L          L   OUTSIDE RANGE
REMARK 500    LEU B 111        24.9      L          L   OUTSIDE RANGE
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 MLA B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLA A 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BKS   RELATED DB: PDB
REMARK 900 TRYPTOPHAN SYNTHASE (E.C. 4.2.1.20) FROM SALMONELLA
REMARK 900 TYPHIMURIUM
REMARK 900 RELATED ID: 1KFK   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TRYPTOPHAN SYNTHASE FROM SALMONELLA
REMARK 900 TYPHIMURIUM
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHORS INFORMED THAT THEIR SEQUENCE IS CORRECT
REMARK 999 AT THE POSITIONS WHERE IT CONFLICTS WITH THE SWISS
REMARK 999 PROT SEQUENCE.
DBREF  1RD5 A    2   262  UNP    P42390   TRPA_MAIZE      86    346
DBREF  1RD5 B    2   262  UNP    P42390   TRPA_MAIZE      86    346
SEQADV 1RD5 MET A    1  UNP  P42390              INITIATING MET
SEQADV 1RD5 PHE A  108  UNP  P42390    SER   192 SEE REMARK 999
SEQADV 1RD5 LYS A  113  UNP  P42390    GLU   197 SEE REMARK 999
SEQADV 1RD5 GLY A  262  UNP  P42390    PRO   346 SEE REMARK 999
SEQADV 1RD5 MET B    1  UNP  P42390              INITIATING MET
SEQADV 1RD5 PHE B  108  UNP  P42390    SER   192 SEE REMARK 999
SEQADV 1RD5 LYS B  113  UNP  P42390    GLU   197 SEE REMARK 999
SEQADV 1RD5 GLY B  262  UNP  P42390    PRO   346 SEE REMARK 999
SEQRES   1 A  262  MET SER ARG PRO VAL SER ASP THR MET ALA ALA LEU MET
SEQRES   2 A  262  ALA LYS GLY LYS THR ALA PHE ILE PRO TYR ILE THR ALA
SEQRES   3 A  262  GLY ASP PRO ASP LEU ALA THR THR ALA GLU ALA LEU ARG
SEQRES   4 A  262  LEU LEU ASP GLY CYS GLY ALA ASP VAL ILE GLU LEU GLY
SEQRES   5 A  262  VAL PRO CYS SER ASP PRO TYR ILE ASP GLY PRO ILE ILE
SEQRES   6 A  262  GLN ALA SER VAL ALA ARG ALA LEU ALA SER GLY THR THR
SEQRES   7 A  262  MET ASP ALA VAL LEU GLU MET LEU ARG GLU VAL THR PRO
SEQRES   8 A  262  GLU LEU SER CYS PRO VAL VAL LEU LEU SER TYR TYR LYS
SEQRES   9 A  262  PRO ILE MET PHE ARG SER LEU ALA LYS MET LYS GLU ALA
SEQRES  10 A  262  GLY VAL HIS GLY LEU ILE VAL PRO ASP LEU PRO TYR VAL
SEQRES  11 A  262  ALA ALA HIS SER LEU TRP SER GLU ALA LYS ASN ASN ASN
SEQRES  12 A  262  LEU GLU LEU VAL LEU LEU THR THR PRO ALA ILE PRO GLU
SEQRES  13 A  262  ASP ARG MET LYS GLU ILE THR LYS ALA SER GLU GLY PHE
SEQRES  14 A  262  VAL TYR LEU VAL SER VAL ASN GLY VAL THR GLY PRO ARG
SEQRES  15 A  262  ALA ASN VAL ASN PRO ARG VAL GLU SER LEU ILE GLN GLU
SEQRES  16 A  262  VAL LYS LYS VAL THR ASN LYS PRO VAL ALA VAL GLY PHE
SEQRES  17 A  262  GLY ILE SER LYS PRO GLU HIS VAL LYS GLN ILE ALA GLN
SEQRES  18 A  262  TRP GLY ALA ASP GLY VAL ILE ILE GLY SER ALA MET VAL
SEQRES  19 A  262  ARG GLN LEU GLY GLU ALA ALA SER PRO LYS GLN GLY LEU
SEQRES  20 A  262  ARG ARG LEU GLU GLU TYR ALA ARG GLY MET LYS ASN ALA
SEQRES  21 A  262  LEU GLY
SEQRES   1 B  262  MET SER ARG PRO VAL SER ASP THR MET ALA ALA LEU MET
SEQRES   2 B  262  ALA LYS GLY LYS THR ALA PHE ILE PRO TYR ILE THR ALA
SEQRES   3 B  262  GLY ASP PRO ASP LEU ALA THR THR ALA GLU ALA LEU ARG
SEQRES   4 B  262  LEU LEU ASP GLY CYS GLY ALA ASP VAL ILE GLU LEU GLY
SEQRES   5 B  262  VAL PRO CYS SER ASP PRO TYR ILE ASP GLY PRO ILE ILE
SEQRES   6 B  262  GLN ALA SER VAL ALA ARG ALA LEU ALA SER GLY THR THR
SEQRES   7 B  262  MET ASP ALA VAL LEU GLU MET LEU ARG GLU VAL THR PRO
SEQRES   8 B  262  GLU LEU SER CYS PRO VAL VAL LEU LEU SER TYR TYR LYS
SEQRES   9 B  262  PRO ILE MET PHE ARG SER LEU ALA LYS MET LYS GLU ALA
SEQRES  10 B  262  GLY VAL HIS GLY LEU ILE VAL PRO ASP LEU PRO TYR VAL
SEQRES  11 B  262  ALA ALA HIS SER LEU TRP SER GLU ALA LYS ASN ASN ASN
SEQRES  12 B  262  LEU GLU LEU VAL LEU LEU THR THR PRO ALA ILE PRO GLU
SEQRES  13 B  262  ASP ARG MET LYS GLU ILE THR LYS ALA SER GLU GLY PHE
SEQRES  14 B  262  VAL TYR LEU VAL SER VAL ASN GLY VAL THR GLY PRO ARG
SEQRES  15 B  262  ALA ASN VAL ASN PRO ARG VAL GLU SER LEU ILE GLN GLU
SEQRES  16 B  262  VAL LYS LYS VAL THR ASN LYS PRO VAL ALA VAL GLY PHE
SEQRES  17 B  262  GLY ILE SER LYS PRO GLU HIS VAL LYS GLN ILE ALA GLN
SEQRES  18 B  262  TRP GLY ALA ASP GLY VAL ILE ILE GLY SER ALA MET VAL
SEQRES  19 B  262  ARG GLN LEU GLY GLU ALA ALA SER PRO LYS GLN GLY LEU
SEQRES  20 B  262  ARG ARG LEU GLU GLU TYR ALA ARG GLY MET LYS ASN ALA
SEQRES  21 B  262  LEU GLY
HET    MLA  B 301       7
HET    MLA  A 302       7
HETNAM     MLA MALONIC ACID
HETSYN     MLA DICARBOXYLIC ACID C3; PROPANEDIOLIC ACID;
HETSYN   2 MLA  METAHNEDICARBOXYLIC ACID
FORMUL   3  MLA    2(C3 H4 O4)
FORMUL   5  HOH   *248(H2 O)
HELIX    1   1 PRO A    4  LYS A   15  1                                  12
HELIX    2   2 ASP A   30  CYS A   44  1                                  15
HELIX    3   3 GLY A   62  ALA A   74  1                                  13
HELIX    4   4 THR A   78  THR A   90  1                                  13
HELIX    5   5 PRO A   91  LEU A   93  5                                   3
HELIX    6   6 TYR A  103  PHE A  108  1                                   6
HELIX    7   7 LEU A  111  ALA A  117  1                                   7
HELIX    8   8 ALA A  131  ASN A  142  1                                  12
HELIX    9   9 PRO A  155  SER A  166  1                                  12
HELIX   10  10 PRO A  187  THR A  200  1                                  14
HELIX   11  11 LYS A  212  TRP A  222  1                                  11
HELIX   12  12 GLY A  230  GLU A  239  1                                  10
HELIX   13  13 SER A  242  LEU A  261  1                                  20
HELIX   14  14 PRO B    4  LYS B   15  1                                  12
HELIX   15  15 ASP B   30  CYS B   44  1                                  15
HELIX   16  16 GLY B   62  SER B   75  1                                  14
HELIX   17  17 THR B   78  THR B   90  1                                  13
HELIX   18  18 PRO B   91  LEU B   93  5                                   3
HELIX   19  19 TYR B  103  MET B  107  5                                   5
HELIX   20  20 SER B  110  ALA B  117  1                                   8
HELIX   21  21 PRO B  128  VAL B  130  5                                   3
HELIX   22  22 ALA B  131  ASN B  142  1                                  12
HELIX   23  23 PRO B  155  SER B  166  1                                  12
HELIX   24  24 ARG B  188  THR B  200  1                                  13
HELIX   25  25 LYS B  212  TRP B  222  1                                  11
HELIX   26  26 GLY B  230  GLU B  239  1                                  10
HELIX   27  27 SER B  242  LEU B  261  1                                  20
SHEET    1   A 9 GLU A 145  LEU A 146  0
SHEET    2   A 9 GLY A 121  ILE A 123  1  N  LEU A 122   O  GLU A 145
SHEET    3   A 9 VAL A  97  LEU A 100  1  N  LEU A  99   O  GLY A 121
SHEET    4   A 9 ILE A  49  GLY A  52  1  N  LEU A  51   O  LEU A 100
SHEET    5   A 9 ALA A  19  THR A  25  1  N  ILE A  24   O  GLY A  52
SHEET    6   A 9 GLY A 226  ILE A 229  1  O  VAL A 227   N  ILE A  21
SHEET    7   A 9 VAL A 204  GLY A 207  1  N  VAL A 206   O  ILE A 228
SHEET    8   A 9 VAL A 170  VAL A 173  1  N  LEU A 172   O  GLY A 207
SHEET    9   A 9 LEU A 148  THR A 150  1  N  THR A 150   O  VAL A 173
SHEET    1   B 9 GLU B 145  LEU B 146  0
SHEET    2   B 9 VAL B 119  ILE B 123  1  N  LEU B 122   O  GLU B 145
SHEET    3   B 9 VAL B  97  LEU B 100  1  N  LEU B  99   O  ILE B 123
SHEET    4   B 9 ILE B  49  GLY B  52  1  N  LEU B  51   O  LEU B 100
SHEET    5   B 9 ALA B  19  THR B  25  1  N  ILE B  24   O  GLY B  52
SHEET    6   B 9 GLY B 226  ILE B 229  1  O  VAL B 227   N  ILE B  21
SHEET    7   B 9 VAL B 204  VAL B 206  1  N  VAL B 206   O  ILE B 228
SHEET    8   B 9 VAL B 170  LEU B 172  1  N  LEU B 172   O  ALA B 205
SHEET    9   B 9 LEU B 148  THR B 150  1  N  THR B 150   O  TYR B 171
CISPEP   1 ASP A   28    PRO A   29          0         3.47
CISPEP   2 ASP B   28    PRO B   29          0         2.93
SITE     1 AC1  4 TYR A 129  ARG B 158  HOH B 402  HOH B 413
SITE     1 AC2  6 ALA A 132  ARG A 158  ALA A 165  HOH A 395
SITE     2 AC2  6 HOH A 415  ARG B 158
CRYST1   91.094  159.815  162.877  90.00  90.00  90.00 F 2 2 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      0.010978  0.000000  0.000000        0.00000
SCALE2      0.000000  0.006257  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006140        0.00000
      
PROCHECK
Go to PROCHECK summary
 References