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PDBsum entry 3zgb

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Top Page protein ligands Protein-protein interface(s) links
Lyase PDB id
3zgb
Jmol
Contents
Protein chains
920 a.a.
Ligands
ASP ×2
EDO ×2
SO4 ×4
Waters ×56
HEADER    LYASE                                   17-DEC-12   3ZGB
TITLE     GREATER EFFICIENCY OF PHOTOSYNTHETIC CARBON FIXATION DUE TO
TITLE    2 SINGLE AMINO ACID SUBSTITUTION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PHOSPHOENOLPYRUVATE CARBOXYLASE;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: PEPC, PEPCASE, PPCA;
COMPND   5 EC: 4.1.1.31;
COMPND   6 ENGINEERED: YES;
COMPND   7 OTHER_DETAILS: THE GENE NAME OF THE PROTEIN IS PPCA
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: FLAVERIA PRINGLEI;
SOURCE   3 ORGANISM_TAXID: 4226;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   7 EXPRESSION_SYSTEM_VARIANT: GOLD;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PETEV16B
KEYWDS    LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.K.PAULUS,D.SCHLIEPER,G.GROTH
REVDAT   4   17-DEC-14 3ZGB    1       REMARK
REVDAT   3   03-DEC-14 3ZGB    1       AUTHOR REMARK FORMUL
REVDAT   2   13-MAR-13 3ZGB    1       JRNL
REVDAT   1   27-FEB-13 3ZGB    0
JRNL        AUTH   J.K.PAULUS,D.SCHLIEPER,G.GROTH
JRNL        TITL   GREATER EFFICIENCY OF PHOTOSYNTHETIC CARBON FIXATION DUE TO
JRNL        TITL 2 SINGLE AMINO ACID SUBSTITUTION
JRNL        REF    NAT.COMMUN.                   V.   4  1518 2013
JRNL        REFN                   ISSN 2041-1723
JRNL        PMID   23443546
JRNL        DOI    10.1038/NCOMMS2504
REMARK   2
REMARK   2 RESOLUTION.    2.71 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.6.0117
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) : 2.71
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 78.72
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.97
REMARK   3   NUMBER OF REFLECTIONS             : 71548
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) : 0.18854
REMARK   3   R VALUE            (WORKING SET) : 0.18769
REMARK   3   FREE R VALUE                     : 0.22985
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.0
REMARK   3   FREE R VALUE TEST SET COUNT      : 1486
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) : 2.710
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.780
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4897
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK   3   BIN R VALUE           (WORKING SET) : 0.226
REMARK   3   BIN FREE R VALUE SET COUNT          : 100
REMARK   3   BIN FREE R VALUE                    : 0.275
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 14750
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 46
REMARK   3   SOLVENT ATOMS            : 56
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 55.8
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.580
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.24
REMARK   3    B22 (A**2) : 0.14
REMARK   3    B33 (A**2) : 0.11
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): 0.567
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.286
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.205
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.152
REMARK   3
REMARK   3  CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 15093 ; 0.016 ; 0.019
REMARK   3   BOND LENGTHS OTHERS               (A): 10545 ; 0.004 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 20405 ; 1.758 ; 1.973
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 25584 ; 1.175 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1826 ; 5.920 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   731 ;36.005 ;23.598
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2710 ;17.579 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   134 ;18.540 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2250 ; 0.094 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 16632 ; 0.008 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  3106 ; 0.004 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
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):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
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):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
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  : 6
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     8        A   223
REMARK   3    ORIGIN FOR THE GROUP (A):  12.3980  45.3400   3.8440
REMARK   3    T TENSOR
REMARK   3      T11:   0.5062 T22:   0.0368
REMARK   3      T33:   0.1349 T12:   0.0415
REMARK   3      T13:  -0.0182 T23:   0.0208
REMARK   3    L TENSOR
REMARK   3      L11:   0.7979 L22:   1.5624
REMARK   3      L33:   0.8391 L12:   0.1103
REMARK   3      L13:   0.0514 L23:   0.0402
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1164 S12:   0.0925 S13:   0.1846
REMARK   3      S21:  -0.2975 S22:   0.0794 S23:  -0.1662
REMARK   3      S31:   0.0597 S32:   0.0322 S33:   0.0370
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   224        A   704
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.5530  33.7750  26.8280
REMARK   3    T TENSOR
REMARK   3      T11:   0.5094 T22:   0.0390
REMARK   3      T33:   0.1306 T12:  -0.0054
REMARK   3      T13:  -0.0057 T23:  -0.0356
REMARK   3    L TENSOR
REMARK   3      L11:   0.4103 L22:   1.7494
REMARK   3      L33:   0.6756 L12:  -0.1381
REMARK   3      L13:   0.0027 L23:  -0.7432
REMARK   3    S TENSOR
REMARK   3      S11:   0.0305 S12:  -0.0559 S13:   0.0946
REMARK   3      S21:   0.1539 S22:   0.0581 S23:   0.1454
REMARK   3      S31:  -0.0156 S32:  -0.0925 S33:  -0.0886
REMARK   3
REMARK   3   TLS GROUP : 3
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   705        A   966
REMARK   3    ORIGIN FOR THE GROUP (A):  18.7570  22.4980   7.0600
REMARK   3    T TENSOR
REMARK   3      T11:   0.5720 T22:   0.0687
REMARK   3      T33:   0.1570 T12:   0.0907
REMARK   3      T13:   0.0312 T23:  -0.0262
REMARK   3    L TENSOR
REMARK   3      L11:   1.5771 L22:   1.3133
REMARK   3      L33:   1.0003 L12:   0.2881
REMARK   3      L13:   0.1190 L23:  -0.1785
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0449 S12:   0.0777 S13:  -0.1102
REMARK   3      S21:  -0.2448 S22:  -0.0146 S23:  -0.3179
REMARK   3      S31:   0.2901 S32:   0.2067 S33:   0.0595
REMARK   3
REMARK   3   TLS GROUP : 4
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B     8        B   223
REMARK   3    ORIGIN FOR THE GROUP (A): -16.2540  50.1310 -28.9590
REMARK   3    T TENSOR
REMARK   3      T11:   0.4775 T22:   0.0468
REMARK   3      T33:   0.1238 T12:  -0.1096
REMARK   3      T13:   0.0160 T23:   0.0028
REMARK   3    L TENSOR
REMARK   3      L11:   1.4867 L22:   1.6459
REMARK   3      L33:   0.8893 L12:   0.1816
REMARK   3      L13:  -0.1341 L23:   0.0183
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0649 S12:   0.0452 S13:   0.3229
REMARK   3      S21:   0.3005 S22:   0.0627 S23:   0.0658
REMARK   3      S31:   0.0522 S32:  -0.0502 S33:   0.0022
REMARK   3
REMARK   3   TLS GROUP : 5
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   224        B   704
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.8000  33.1810 -51.8300
REMARK   3    T TENSOR
REMARK   3      T11:   0.5141 T22:   0.1284
REMARK   3      T33:   0.1458 T12:  -0.0989
REMARK   3      T13:   0.0916 T23:  -0.0546
REMARK   3    L TENSOR
REMARK   3      L11:   0.7727 L22:   1.1795
REMARK   3      L33:   0.9242 L12:   0.3387
REMARK   3      L13:   0.0346 L23:   0.4805
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0554 S12:   0.1631 S13:  -0.0710
REMARK   3      S21:  -0.1764 S22:   0.0916 S23:  -0.2211
REMARK   3      S31:   0.0743 S32:   0.0254 S33:  -0.0362
REMARK   3
REMARK   3   TLS GROUP : 6
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   705        B   966
REMARK   3    ORIGIN FOR THE GROUP (A): -30.1730  30.6890 -31.3570
REMARK   3    T TENSOR
REMARK   3      T11:   0.4531 T22:   0.1812
REMARK   3      T33:   0.1541 T12:  -0.1768
REMARK   3      T13:   0.0612 T23:  -0.0097
REMARK   3    L TENSOR
REMARK   3      L11:   1.8034 L22:   1.9644
REMARK   3      L33:   1.1279 L12:  -0.2492
REMARK   3      L13:  -0.0731 L23:   0.1430
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0666 S12:   0.0541 S13:  -0.0649
REMARK   3      S21:   0.0782 S22:   0.0418 S23:   0.3806
REMARK   3      S31:   0.1559 S32:  -0.2691 S33:   0.0248
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   : 1.20
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
REMARK   3   RIDING POSITIONS.
REMARK   4
REMARK   4 3ZGB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-DEC-12.
REMARK 100 THE PDBE ID CODE IS EBI-55151.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 27-SEP-11
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.6
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : PETRA III
REMARK 200  BEAMLINE                       : P14 (MX2)
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.12678
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD (MX-225)
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 71548
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.71
REMARK 200  RESOLUTION RANGE LOW       (A) : 165.55
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 15.8
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.099
REMARK 200   FOR THE DATA SET  : 6.30
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.71
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.86
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 16.4
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.334
REMARK 200   FOR SHELL         : 2.00
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3ZBE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.2
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 0.1 M
REMARK 280  TRI-SODIUM CITRATE/HCL PH 5.6, 10 % (W/V) PEG 4000
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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+1/2,Y+1/2,-Z
REMARK 290       4555   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       82.77450
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       60.85000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       82.77450
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       60.85000
REMARK 290   SMTRY3   4  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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 134490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -114.2 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      121.70000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A    -5
REMARK 465     GLY A    -4
REMARK 465     HIS A    -3
REMARK 465     HIS A    -2
REMARK 465     HIS A    -1
REMARK 465     HIS A     0
REMARK 465     HIS A     1
REMARK 465     HIS A     2
REMARK 465     HIS A     3
REMARK 465     HIS A     4
REMARK 465     HIS A     5
REMARK 465     ALA A   345
REMARK 465     ARG A   346
REMARK 465     ARG A   347
REMARK 465     ASP A   348
REMARK 465     VAL A   349
REMARK 465     LYS A   350
REMARK 465     HIS A   351
REMARK 465     TYR A   352
REMARK 465     ILE A   353
REMARK 465     GLU A   354
REMARK 465     PHE A   355
REMARK 465     TRP A   356
REMARK 465     LYS A   357
REMARK 465     ARG A   757
REMARK 465     LYS A   758
REMARK 465     PRO A   759
REMARK 465     SER A   760
REMARK 465     GLU A   922
REMARK 465     TYR A   923
REMARK 465     ALA A   924
REMARK 465     ALA A   925
REMARK 465     GLU A   926
REMARK 465     PRO A   927
REMARK 465     SER A   928
REMARK 465     LYS A   929
REMARK 465     PRO A   930
REMARK 465     ALA A   931
REMARK 465     ASP A   932
REMARK 465     GLU A   933
REMARK 465     LEU A   934
REMARK 465     ILE A   935
REMARK 465     HIS A   936
REMARK 465     LEU A   937
REMARK 465     ASN A   938
REMARK 465     PRO A   939
REMARK 465     THR A   940
REMARK 465     SER A   941
REMARK 465     GLU A   942
REMARK 465     TYR A   943
REMARK 465     ALA A   944
REMARK 465     PRO A   945
REMARK 465     MET B    -5
REMARK 465     GLY B    -4
REMARK 465     HIS B    -3
REMARK 465     HIS B    -2
REMARK 465     HIS B    -1
REMARK 465     HIS B     0
REMARK 465     HIS B     1
REMARK 465     HIS B     2
REMARK 465     HIS B     3
REMARK 465     HIS B     4
REMARK 465     HIS B     5
REMARK 465     LEU B     6
REMARK 465     GLU B     7
REMARK 465     LYS B     8
REMARK 465     LEU B     9
REMARK 465     ARG B   227
REMARK 465     ARG B   347
REMARK 465     ASP B   348
REMARK 465     VAL B   349
REMARK 465     LYS B   350
REMARK 465     HIS B   351
REMARK 465     TYR B   352
REMARK 465     ILE B   353
REMARK 465     GLU B   354
REMARK 465     PHE B   355
REMARK 465     TRP B   356
REMARK 465     LYS B   357
REMARK 465     ARG B   757
REMARK 465     LYS B   758
REMARK 465     PRO B   759
REMARK 465     SER B   760
REMARK 465     GLY B   761
REMARK 465     LYS B   921
REMARK 465     GLU B   922
REMARK 465     TYR B   923
REMARK 465     ALA B   924
REMARK 465     ALA B   925
REMARK 465     GLU B   926
REMARK 465     PRO B   927
REMARK 465     SER B   928
REMARK 465     LYS B   929
REMARK 465     PRO B   930
REMARK 465     ALA B   931
REMARK 465     ASP B   932
REMARK 465     GLU B   933
REMARK 465     LEU B   934
REMARK 465     ILE B   935
REMARK 465     HIS B   936
REMARK 465     LEU B   937
REMARK 465     ASN B   938
REMARK 465     PRO B   939
REMARK 465     THR B   940
REMARK 465     SER B   941
REMARK 465     GLU B   942
REMARK 465     TYR B   943
REMARK 465     ALA B   944
REMARK 465     PRO B   945
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   OH   TYR A   273     OE2  GLU A   411              1.92
REMARK 500   OH   TYR B   273     OE2  GLU B   411              1.90
REMARK 500   O    LEU B   488     NH2  ARG B   545              2.11
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    ASP A 137   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES
REMARK 500    ARG A 189   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    ARG A 288   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    LEU A 444   C   -  N   -  CA  ANGL. DEV. = -16.4 DEGREES
REMARK 500    ASP A 448   CB  -  CG  -  OD1 ANGL. DEV. =   6.7 DEGREES
REMARK 500    ARG A 455   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES
REMARK 500    ARG A 455   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.0 DEGREES
REMARK 500    LEU A 494   CB  -  CG  -  CD1 ANGL. DEV. = -11.7 DEGREES
REMARK 500    CYS A 689   CA  -  CB  -  SG  ANGL. DEV. = -10.0 DEGREES
REMARK 500    ASP A 712   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ASP A 821   CB  -  CG  -  OD1 ANGL. DEV. =   7.0 DEGREES
REMARK 500    ASP A 821   CB  -  CG  -  OD2 ANGL. DEV. =  -7.5 DEGREES
REMARK 500    ASP A 889   CB  -  CG  -  OD2 ANGL. DEV. =  -7.5 DEGREES
REMARK 500    ARG B 288   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    ASP B 448   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES
REMARK 500    CYS B 689   CA  -  CB  -  SG  ANGL. DEV. =  -9.5 DEGREES
REMARK 500    MET B 697   CG  -  SD  -  CE  ANGL. DEV. = -10.6 DEGREES
REMARK 500    ARG B 817   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    ASP B 821   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES
REMARK 500    ASP B 821   CB  -  CG  -  OD2 ANGL. DEV. =  -6.0 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    GLN A 175      129.34     79.37
REMARK 500    THR A 222       75.72   -114.86
REMARK 500    ASP A 223       30.39   -147.99
REMARK 500    THR A 246      -37.31   -146.47
REMARK 500    ASN A 291       88.56   -150.39
REMARK 500    GLU A 363       66.51   -119.50
REMARK 500    HIS A 389      -16.55   -141.10
REMARK 500    THR A 532      -26.27   -142.92
REMARK 500    HIS A 548       42.29     71.06
REMARK 500    ASN A 698       56.13   -152.19
REMARK 500    PRO A 699      153.70    -48.64
REMARK 500    PRO A 741       32.34    -87.81
REMARK 500    MET A 748       38.65    -99.76
REMARK 500    ASN A 749      117.95    -36.98
REMARK 500    SER A 752     -124.17    -79.75
REMARK 500    ASP A 799      111.41   -164.22
REMARK 500    GLN A 963     -125.75     36.72
REMARK 500    THR A 965      -89.85   -129.85
REMARK 500    GLN B 175      129.28     79.88
REMARK 500    THR B 222       74.03   -116.72
REMARK 500    ASP B 223       26.61   -143.89
REMARK 500    PRO B 229      155.39    -44.59
REMARK 500    THR B 246      -36.67   -148.90
REMARK 500    ALA B 345       58.55    -66.76
REMARK 500    GLU B 363       66.53   -119.31
REMARK 500    HIS B 389      -14.40   -148.71
REMARK 500    ASP B 498      -16.43    -43.61
REMARK 500    THR B 532      -29.54   -140.29
REMARK 500    ASN B 698       57.46   -153.09
REMARK 500    ASN B 749      119.53    -35.78
REMARK 500    SER B 752     -125.54    -78.63
REMARK 500    ASP B 799      110.05   -165.66
REMARK 500    GLN B 963     -126.09     35.69
REMARK 500    THR B 965      -89.42   -130.08
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    ILE A 200        25.0      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700
REMARK 700 THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ASP A1967
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1968
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ASP B1967
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1968
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1969
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1969
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1970
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1970
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ZGE   RELATED DB: PDB
REMARK 900  GREATER EFFICIENCY OF PHOTOSYNTHETIC CARBON FIXATION DUE
REMARK 900  TO SINGLE AMINO ACID SUBSTITUTION
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CRYSTALLIZED SEQUENCE ACTUALLY MAPS TO NCBI ACCESSION
REMARK 999 CODE Z48966 WITHOUT ANY CONFLICTS OR GAPS. THE CLOSEST UNIPROT
REMARK 999 MATCH FOR THE SEQUENCE IS Q01647
DBREF  3ZGB A    6   290  UNP    Q01647   CAPP1_FLAPR      6    290
DBREF  3ZGB A  291   966  UNP    Q01647   CAPP1_FLAPR    292    967
DBREF  3ZGB B    6   290  UNP    Q01647   CAPP1_FLAPR      6    290
DBREF  3ZGB B  291   966  UNP    Q01647   CAPP1_FLAPR    292    967
SEQADV 3ZGB MET A   -5  UNP  Q01647              EXPRESSION TAG
SEQADV 3ZGB GLY A   -4  UNP  Q01647              EXPRESSION TAG
SEQADV 3ZGB HIS A   -3  UNP  Q01647              EXPRESSION TAG
SEQADV 3ZGB HIS A   -2  UNP  Q01647              EXPRESSION TAG
SEQADV 3ZGB HIS A   -1  UNP  Q01647              EXPRESSION TAG
SEQADV 3ZGB HIS A    0  UNP  Q01647              EXPRESSION TAG
SEQADV 3ZGB HIS A    1  UNP  Q01647              EXPRESSION TAG
SEQADV 3ZGB HIS A    2  UNP  Q01647              EXPRESSION TAG
SEQADV 3ZGB HIS A    3  UNP  Q01647              EXPRESSION TAG
SEQADV 3ZGB HIS A    4  UNP  Q01647              EXPRESSION TAG
SEQADV 3ZGB HIS A    5  UNP  Q01647              EXPRESSION TAG
SEQADV 3ZGB     A       UNP  Q01647    LYS   291 SEE REMARK 999
SEQADV 3ZGB ASN A  291  UNP  Q01647    HIS   292 SEE REMARK 999
SEQADV 3ZGB MET B   -5  UNP  Q01647              EXPRESSION TAG
SEQADV 3ZGB GLY B   -4  UNP  Q01647              EXPRESSION TAG
SEQADV 3ZGB HIS B   -3  UNP  Q01647              EXPRESSION TAG
SEQADV 3ZGB HIS B   -2  UNP  Q01647              EXPRESSION TAG
SEQADV 3ZGB HIS B   -1  UNP  Q01647              EXPRESSION TAG
SEQADV 3ZGB HIS B    0  UNP  Q01647              EXPRESSION TAG
SEQADV 3ZGB HIS B    1  UNP  Q01647              EXPRESSION TAG
SEQADV 3ZGB HIS B    2  UNP  Q01647              EXPRESSION TAG
SEQADV 3ZGB HIS B    3  UNP  Q01647              EXPRESSION TAG
SEQADV 3ZGB HIS B    4  UNP  Q01647              EXPRESSION TAG
SEQADV 3ZGB HIS B    5  UNP  Q01647              EXPRESSION TAG
SEQADV 3ZGB     B       UNP  Q01647    LYS   291 SEE REMARK 999
SEQADV 3ZGB ASN B  291  UNP  Q01647    HIS   292 SEE REMARK 999
SEQRES   1 A  972  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS LEU GLU
SEQRES   2 A  972  LYS LEU ALA SER ILE ASP ALA GLN LEU ARG LEU LEU VAL
SEQRES   3 A  972  PRO GLY LYS VAL SER GLU ASP ASP LYS LEU ILE GLU TYR
SEQRES   4 A  972  ASP ALA LEU LEU LEU ASP LYS PHE LEU ASP ILE LEU GLN
SEQRES   5 A  972  ASP LEU HIS GLY GLU ASP LEU LYS GLU ALA VAL GLN GLU
SEQRES   6 A  972  CYS TYR GLU LEU SER ALA GLU TYR GLU GLY LYS HIS ASP
SEQRES   7 A  972  PRO LYS LYS LEU GLU GLU LEU GLY SER VAL LEU THR SER
SEQRES   8 A  972  LEU ASP PRO GLY ASP SER ILE VAL ILE ALA LYS ALA PHE
SEQRES   9 A  972  SER HIS MET LEU ASN LEU ALA ASN LEU ALA GLU GLU VAL
SEQRES  10 A  972  GLN ILE ALA TYR ARG ARG ARG ILE LYS LEU LYS ARG GLY
SEQRES  11 A  972  ASP PHE ALA ASP GLU ALA ASN ALA THR THR GLU SER ASP
SEQRES  12 A  972  ILE GLU GLU THR PHE LYS LYS LEU VAL LEU LYS LEU ASN
SEQRES  13 A  972  LYS SER PRO GLU GLU VAL PHE ASP ALA LEU LYS ASN GLN
SEQRES  14 A  972  THR VAL ASP LEU VAL LEU THR ALA HIS PRO THR GLN SER
SEQRES  15 A  972  VAL ARG ARG SER LEU LEU GLN LYS HIS GLY ARG ILE ARG
SEQRES  16 A  972  ASN CYS LEU ALA GLN LEU TYR ALA LYS ASP ILE THR PRO
SEQRES  17 A  972  ASP ASP LYS GLN GLU LEU ASP GLU ALA LEU HIS ARG GLU
SEQRES  18 A  972  ILE GLN ALA ALA PHE ARG THR ASP GLU ILE ARG ARG THR
SEQRES  19 A  972  PRO PRO THR PRO GLN ASP GLU MET ARG ALA GLY MET SER
SEQRES  20 A  972  TYR PHE HIS GLU THR ILE TRP LYS GLY VAL PRO LYS PHE
SEQRES  21 A  972  LEU ARG ARG VAL ASP THR ALA LEU LYS ASN ILE GLY ILE
SEQRES  22 A  972  ASN GLU ARG VAL PRO TYR ASN ALA PRO LEU ILE GLN PHE
SEQRES  23 A  972  SER SER TRP MET GLY GLY ASP ARG ASP GLY ASN PRO ARG
SEQRES  24 A  972  VAL THR PRO GLU VAL THR ARG ASP VAL CYS LEU LEU ALA
SEQRES  25 A  972  ARG MET MET ALA SER ASN MET TYR PHE SER GLN ILE GLU
SEQRES  26 A  972  ASP LEU MET PHE GLU MET SER MET TRP ARG CYS ASN SER
SEQRES  27 A  972  GLU LEU ARG VAL ARG ALA GLU GLU LEU TYR ARG THR ALA
SEQRES  28 A  972  ARG ARG ASP VAL LYS HIS TYR ILE GLU PHE TRP LYS GLN
SEQRES  29 A  972  VAL PRO PRO THR GLU PRO TYR ARG VAL ILE LEU GLY ASP
SEQRES  30 A  972  VAL ARG ASP LYS LEU TYR ASN THR ARG GLU ARG SER ARG
SEQRES  31 A  972  HIS LEU LEU ALA HIS GLY ILE SER ASP ILE PRO GLU GLU
SEQRES  32 A  972  ALA VAL TYR THR ASN VAL GLU GLN PHE LEU GLU PRO LEU
SEQRES  33 A  972  GLU LEU CYS TYR ARG SER LEU CYS ASP CYS GLY ASP ARG
SEQRES  34 A  972  VAL ILE ALA ASP GLY SER LEU LEU ASP PHE LEU ARG GLN
SEQRES  35 A  972  VAL SER THR PHE GLY LEU SER LEU VAL LYS LEU ASP ILE
SEQRES  36 A  972  ARG GLN GLU SER ASP ARG HIS THR ASP VAL LEU ASP ALA
SEQRES  37 A  972  ILE THR GLN HIS LEU GLU ILE GLY SER TYR ARG GLU TRP
SEQRES  38 A  972  SER GLU GLU LYS ARG GLN GLU TRP LEU LEU ALA GLU LEU
SEQRES  39 A  972  SER GLY LYS ARG PRO LEU PHE GLY SER ASP LEU PRO LYS
SEQRES  40 A  972  THR GLU GLU VAL LYS ASP VAL LEU ASP THR PHE ASN VAL
SEQRES  41 A  972  LEU ALA GLU LEU PRO SER ASP CYS PHE GLY ALA TYR ILE
SEQRES  42 A  972  ILE SER MET ALA THR SER PRO SER ASP VAL LEU ALA VAL
SEQRES  43 A  972  GLU LEU LEU GLN ARG GLU CYS HIS VAL LYS HIS PRO LEU
SEQRES  44 A  972  ARG VAL VAL PRO LEU PHE GLU LYS LEU ALA ASP LEU GLU
SEQRES  45 A  972  ALA ALA PRO ALA ALA MET ALA ARG LEU PHE SER ILE ASP
SEQRES  46 A  972  TRP TYR ARG ASN ARG ILE ASP GLY LYS GLN GLU VAL MET
SEQRES  47 A  972  ILE GLY TYR SER ASP SER GLY LYS ASP ALA GLY ARG PHE
SEQRES  48 A  972  SER ALA ALA TRP GLN LEU TYR LYS ALA GLN GLU GLU ILE
SEQRES  49 A  972  ILE LYS VAL ALA LYS GLU PHE GLY VAL LYS LEU VAL ILE
SEQRES  50 A  972  PHE HIS GLY ARG GLY GLY THR VAL GLY ARG GLY GLY GLY
SEQRES  51 A  972  PRO THR HIS LEU ALA ILE LEU SER GLN PRO PRO ASP THR
SEQRES  52 A  972  ILE HIS GLY SER LEU ARG VAL THR VAL GLN GLY GLU VAL
SEQRES  53 A  972  ILE GLU GLN SER PHE GLY GLU GLU HIS LEU CYS PHE ARG
SEQRES  54 A  972  THR LEU GLN ARG PHE CYS ALA ALA THR LEU GLU HIS GLY
SEQRES  55 A  972  MET ASN PRO PRO ILE SER PRO ARG PRO GLU TRP ARG GLU
SEQRES  56 A  972  LEU MET ASP GLN MET ALA VAL VAL ALA THR GLU GLU TYR
SEQRES  57 A  972  ARG SER ILE VAL PHE LYS GLU PRO ARG PHE VAL GLU TYR
SEQRES  58 A  972  PHE ARG LEU ALA THR PRO GLU LEU GLU TYR GLY ARG MET
SEQRES  59 A  972  ASN ILE GLY SER ARG PRO SER LYS ARG LYS PRO SER GLY
SEQRES  60 A  972  GLY ILE GLU SER LEU ARG ALA ILE PRO TRP ILE PHE ALA
SEQRES  61 A  972  TRP THR GLN THR ARG PHE HIS LEU PRO VAL TRP LEU GLY
SEQRES  62 A  972  PHE GLY ALA ALA PHE LYS HIS ALA ILE LYS LYS ASP SER
SEQRES  63 A  972  LYS ASN LEU GLN MET LEU GLN GLU MET TYR LYS THR TRP
SEQRES  64 A  972  PRO PHE PHE ARG VAL THR ILE ASP LEU VAL GLU MET VAL
SEQRES  65 A  972  PHE ALA LYS GLY ASP PRO GLY ILE ALA ALA LEU ASN ASP
SEQRES  66 A  972  LYS LEU LEU VAL SER GLU ASP LEU TRP PRO PHE GLY GLU
SEQRES  67 A  972  SER LEU ARG ALA ASN TYR GLU GLU THR LYS ASP TYR LEU
SEQRES  68 A  972  LEU LYS ILE ALA GLY HIS ARG ASP LEU LEU GLU GLY ASP
SEQRES  69 A  972  PRO TYR LEU LYS GLN ARG ILE ARG LEU ARG ASP SER TYR
SEQRES  70 A  972  ILE THR THR LEU ASN VAL CYS GLN ALA TYR THR LEU LYS
SEQRES  71 A  972  ARG ILE ARG ASP PRO ASN TYR HIS VAL THR LEU ARG PRO
SEQRES  72 A  972  HIS ILE SER LYS GLU TYR ALA ALA GLU PRO SER LYS PRO
SEQRES  73 A  972  ALA ASP GLU LEU ILE HIS LEU ASN PRO THR SER GLU TYR
SEQRES  74 A  972  ALA PRO GLY LEU GLU ASP THR LEU ILE LEU THR MET LYS
SEQRES  75 A  972  GLY ILE ALA ALA GLY MET GLN ASN THR GLY
SEQRES   1 B  972  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS LEU GLU
SEQRES   2 B  972  LYS LEU ALA SER ILE ASP ALA GLN LEU ARG LEU LEU VAL
SEQRES   3 B  972  PRO GLY LYS VAL SER GLU ASP ASP LYS LEU ILE GLU TYR
SEQRES   4 B  972  ASP ALA LEU LEU LEU ASP LYS PHE LEU ASP ILE LEU GLN
SEQRES   5 B  972  ASP LEU HIS GLY GLU ASP LEU LYS GLU ALA VAL GLN GLU
SEQRES   6 B  972  CYS TYR GLU LEU SER ALA GLU TYR GLU GLY LYS HIS ASP
SEQRES   7 B  972  PRO LYS LYS LEU GLU GLU LEU GLY SER VAL LEU THR SER
SEQRES   8 B  972  LEU ASP PRO GLY ASP SER ILE VAL ILE ALA LYS ALA PHE
SEQRES   9 B  972  SER HIS MET LEU ASN LEU ALA ASN LEU ALA GLU GLU VAL
SEQRES  10 B  972  GLN ILE ALA TYR ARG ARG ARG ILE LYS LEU LYS ARG GLY
SEQRES  11 B  972  ASP PHE ALA ASP GLU ALA ASN ALA THR THR GLU SER ASP
SEQRES  12 B  972  ILE GLU GLU THR PHE LYS LYS LEU VAL LEU LYS LEU ASN
SEQRES  13 B  972  LYS SER PRO GLU GLU VAL PHE ASP ALA LEU LYS ASN GLN
SEQRES  14 B  972  THR VAL ASP LEU VAL LEU THR ALA HIS PRO THR GLN SER
SEQRES  15 B  972  VAL ARG ARG SER LEU LEU GLN LYS HIS GLY ARG ILE ARG
SEQRES  16 B  972  ASN CYS LEU ALA GLN LEU TYR ALA LYS ASP ILE THR PRO
SEQRES  17 B  972  ASP ASP LYS GLN GLU LEU ASP GLU ALA LEU HIS ARG GLU
SEQRES  18 B  972  ILE GLN ALA ALA PHE ARG THR ASP GLU ILE ARG ARG THR
SEQRES  19 B  972  PRO PRO THR PRO GLN ASP GLU MET ARG ALA GLY MET SER
SEQRES  20 B  972  TYR PHE HIS GLU THR ILE TRP LYS GLY VAL PRO LYS PHE
SEQRES  21 B  972  LEU ARG ARG VAL ASP THR ALA LEU LYS ASN ILE GLY ILE
SEQRES  22 B  972  ASN GLU ARG VAL PRO TYR ASN ALA PRO LEU ILE GLN PHE
SEQRES  23 B  972  SER SER TRP MET GLY GLY ASP ARG ASP GLY ASN PRO ARG
SEQRES  24 B  972  VAL THR PRO GLU VAL THR ARG ASP VAL CYS LEU LEU ALA
SEQRES  25 B  972  ARG MET MET ALA SER ASN MET TYR PHE SER GLN ILE GLU
SEQRES  26 B  972  ASP LEU MET PHE GLU MET SER MET TRP ARG CYS ASN SER
SEQRES  27 B  972  GLU LEU ARG VAL ARG ALA GLU GLU LEU TYR ARG THR ALA
SEQRES  28 B  972  ARG ARG ASP VAL LYS HIS TYR ILE GLU PHE TRP LYS GLN
SEQRES  29 B  972  VAL PRO PRO THR GLU PRO TYR ARG VAL ILE LEU GLY ASP
SEQRES  30 B  972  VAL ARG ASP LYS LEU TYR ASN THR ARG GLU ARG SER ARG
SEQRES  31 B  972  HIS LEU LEU ALA HIS GLY ILE SER ASP ILE PRO GLU GLU
SEQRES  32 B  972  ALA VAL TYR THR ASN VAL GLU GLN PHE LEU GLU PRO LEU
SEQRES  33 B  972  GLU LEU CYS TYR ARG SER LEU CYS ASP CYS GLY ASP ARG
SEQRES  34 B  972  VAL ILE ALA ASP GLY SER LEU LEU ASP PHE LEU ARG GLN
SEQRES  35 B  972  VAL SER THR PHE GLY LEU SER LEU VAL LYS LEU ASP ILE
SEQRES  36 B  972  ARG GLN GLU SER ASP ARG HIS THR ASP VAL LEU ASP ALA
SEQRES  37 B  972  ILE THR GLN HIS LEU GLU ILE GLY SER TYR ARG GLU TRP
SEQRES  38 B  972  SER GLU GLU LYS ARG GLN GLU TRP LEU LEU ALA GLU LEU
SEQRES  39 B  972  SER GLY LYS ARG PRO LEU PHE GLY SER ASP LEU PRO LYS
SEQRES  40 B  972  THR GLU GLU VAL LYS ASP VAL LEU ASP THR PHE ASN VAL
SEQRES  41 B  972  LEU ALA GLU LEU PRO SER ASP CYS PHE GLY ALA TYR ILE
SEQRES  42 B  972  ILE SER MET ALA THR SER PRO SER ASP VAL LEU ALA VAL
SEQRES  43 B  972  GLU LEU LEU GLN ARG GLU CYS HIS VAL LYS HIS PRO LEU
SEQRES  44 B  972  ARG VAL VAL PRO LEU PHE GLU LYS LEU ALA ASP LEU GLU
SEQRES  45 B  972  ALA ALA PRO ALA ALA MET ALA ARG LEU PHE SER ILE ASP
SEQRES  46 B  972  TRP TYR ARG ASN ARG ILE ASP GLY LYS GLN GLU VAL MET
SEQRES  47 B  972  ILE GLY TYR SER ASP SER GLY LYS ASP ALA GLY ARG PHE
SEQRES  48 B  972  SER ALA ALA TRP GLN LEU TYR LYS ALA GLN GLU GLU ILE
SEQRES  49 B  972  ILE LYS VAL ALA LYS GLU PHE GLY VAL LYS LEU VAL ILE
SEQRES  50 B  972  PHE HIS GLY ARG GLY GLY THR VAL GLY ARG GLY GLY GLY
SEQRES  51 B  972  PRO THR HIS LEU ALA ILE LEU SER GLN PRO PRO ASP THR
SEQRES  52 B  972  ILE HIS GLY SER LEU ARG VAL THR VAL GLN GLY GLU VAL
SEQRES  53 B  972  ILE GLU GLN SER PHE GLY GLU GLU HIS LEU CYS PHE ARG
SEQRES  54 B  972  THR LEU GLN ARG PHE CYS ALA ALA THR LEU GLU HIS GLY
SEQRES  55 B  972  MET ASN PRO PRO ILE SER PRO ARG PRO GLU TRP ARG GLU
SEQRES  56 B  972  LEU MET ASP GLN MET ALA VAL VAL ALA THR GLU GLU TYR
SEQRES  57 B  972  ARG SER ILE VAL PHE LYS GLU PRO ARG PHE VAL GLU TYR
SEQRES  58 B  972  PHE ARG LEU ALA THR PRO GLU LEU GLU TYR GLY ARG MET
SEQRES  59 B  972  ASN ILE GLY SER ARG PRO SER LYS ARG LYS PRO SER GLY
SEQRES  60 B  972  GLY ILE GLU SER LEU ARG ALA ILE PRO TRP ILE PHE ALA
SEQRES  61 B  972  TRP THR GLN THR ARG PHE HIS LEU PRO VAL TRP LEU GLY
SEQRES  62 B  972  PHE GLY ALA ALA PHE LYS HIS ALA ILE LYS LYS ASP SER
SEQRES  63 B  972  LYS ASN LEU GLN MET LEU GLN GLU MET TYR LYS THR TRP
SEQRES  64 B  972  PRO PHE PHE ARG VAL THR ILE ASP LEU VAL GLU MET VAL
SEQRES  65 B  972  PHE ALA LYS GLY ASP PRO GLY ILE ALA ALA LEU ASN ASP
SEQRES  66 B  972  LYS LEU LEU VAL SER GLU ASP LEU TRP PRO PHE GLY GLU
SEQRES  67 B  972  SER LEU ARG ALA ASN TYR GLU GLU THR LYS ASP TYR LEU
SEQRES  68 B  972  LEU LYS ILE ALA GLY HIS ARG ASP LEU LEU GLU GLY ASP
SEQRES  69 B  972  PRO TYR LEU LYS GLN ARG ILE ARG LEU ARG ASP SER TYR
SEQRES  70 B  972  ILE THR THR LEU ASN VAL CYS GLN ALA TYR THR LEU LYS
SEQRES  71 B  972  ARG ILE ARG ASP PRO ASN TYR HIS VAL THR LEU ARG PRO
SEQRES  72 B  972  HIS ILE SER LYS GLU TYR ALA ALA GLU PRO SER LYS PRO
SEQRES  73 B  972  ALA ASP GLU LEU ILE HIS LEU ASN PRO THR SER GLU TYR
SEQRES  74 B  972  ALA PRO GLY LEU GLU ASP THR LEU ILE LEU THR MET LYS
SEQRES  75 B  972  GLY ILE ALA ALA GLY MET GLN ASN THR GLY
HET    ASP  A1967       9
HET    EDO  A1968       4
HET    ASP  B1967       9
HET    EDO  B1968       4
HET    SO4  B1969       5
HET    SO4  A1969       5
HET    SO4  A1970       5
HET    SO4  B1970       5
HETNAM     EDO 1,2-ETHANEDIOL
HETNAM     ASP ASPARTIC ACID
HETNAM     SO4 SULFATE ION
HETSYN     EDO ETHYLENE GLYCOL
FORMUL   3  EDO    2(C2 H6 O2)
FORMUL   4  SO4    4(O4 S 2-)
FORMUL   5  ASP    2(C4 H7 N O4)
FORMUL   6  HOH   *56(H2 O)
HELIX    1   1 LYS A    8  VAL A   20  1                                  13
HELIX    2   2 LYS A   29  GLY A   50  1                                  22
HELIX    3   3 GLY A   50  HIS A   71  1                                  22
HELIX    4   4 PRO A   73  THR A   84  1                                  12
HELIX    5   5 ASP A   87  ARG A  116  1                                  30
HELIX    6   6 ASP A  125  ASN A  131  5                                   7
HELIX    7   7 ASP A  137  LEU A  149  1                                  13
HELIX    8   8 SER A  152  ASN A  162  1                                  11
HELIX    9   9 ARG A  178  TYR A  196  1                                  19
HELIX   10  10 THR A  201  ARG A  221  1                                  21
HELIX   11  11 THR A  231  MET A  240  1                                  10
HELIX   12  12 SER A  241  THR A  246  1                                   6
HELIX   13  13 THR A  246  ILE A  265  1                                  20
HELIX   14  14 THR A  295  MET A  325  1                                  31
HELIX   15  15 ASN A  331  THR A  344  1                                  14
HELIX   16  16 GLU A  363  GLY A  390  1                                  28
HELIX   17  17 PRO A  395  VAL A  399  5                                   5
HELIX   18  18 ASN A  402  CYS A  420  1                                  19
HELIX   19  19 ASP A  422  ASP A  427  1                                   6
HELIX   20  20 GLY A  428  GLY A  441  1                                  14
HELIX   21  21 SER A  453  LEU A  467  1                                  15
HELIX   22  22 SER A  476  SER A  489  1                                  14
HELIX   23  23 THR A  502  LEU A  518  1                                  17
HELIX   24  24 PRO A  519  ASP A  521  5                                   3
HELIX   25  25 SER A  533  CYS A  547  1                                  15
HELIX   26  26 LYS A  561  SER A  577  1                                  17
HELIX   27  27 ILE A  578  ASP A  586  1                                   9
HELIX   28  28 GLY A  594  GLY A  603  1                                  10
HELIX   29  29 GLY A  603  GLY A  626  1                                  24
HELIX   30  30 GLY A  637  ARG A  641  5                                   5
HELIX   31  31 GLY A  643  SER A  652  1                                  10
HELIX   32  32 VAL A  670  GLY A  676  1                                   7
HELIX   33  33 GLU A  677  ASN A  698  1                                  22
HELIX   34  34 ARG A  704  PHE A  727  1                                  24
HELIX   35  35 ARG A  731  THR A  740  1                                  10
HELIX   36  36 PRO A  741  MET A  748  1                                   8
HELIX   37  37 ARG A  767  GLN A  777  1                                  11
HELIX   38  38 HIS A  781  LEU A  786  1                                   6
HELIX   39  39 GLY A  787  ASP A  799  1                                  13
HELIX   40  40 SER A  800  TRP A  813  1                                  14
HELIX   41  41 TRP A  813  LYS A  829  1                                  17
HELIX   42  42 ASP A  831  VAL A  843  1                                  13
HELIX   43  43 SER A  844  ASP A  846  5                                   3
HELIX   44  44 LEU A  847  GLY A  870  1                                  24
HELIX   45  45 ASP A  878  ASP A  908  1                                  31
HELIX   46  46 GLY A  946  GLN A  963  1                                  18
HELIX   47  47 ALA B   10  VAL B   20  1                                  11
HELIX   48  48 LYS B   29  GLY B   50  1                                  22
HELIX   49  49 GLY B   50  HIS B   71  1                                  22
HELIX   50  50 PRO B   73  THR B   84  1                                  12
HELIX   51  51 ASP B   87  ARG B  116  1                                  30
HELIX   52  52 ASP B  125  ASN B  131  5                                   7
HELIX   53  53 ASP B  137  LEU B  149  1                                  13
HELIX   54  54 SER B  152  ASN B  162  1                                  11
HELIX   55  55 ARG B  178  TYR B  196  1                                  19
HELIX   56  56 THR B  201  ARG B  221  1                                  21
HELIX   57  57 THR B  231  MET B  240  1                                  10
HELIX   58  58 SER B  241  THR B  246  1                                   6
HELIX   59  59 THR B  246  ILE B  265  1                                  20
HELIX   60  60 THR B  295  MET B  325  1                                  31
HELIX   61  61 ASN B  331  THR B  344  1                                  14
HELIX   62  62 GLU B  363  GLY B  390  1                                  28
HELIX   63  63 PRO B  395  VAL B  399  5                                   5
HELIX   64  64 ASN B  402  CYS B  420  1                                  19
HELIX   65  65 ASP B  422  ASP B  427  1                                   6
HELIX   66  66 GLY B  428  GLY B  441  1                                  14
HELIX   67  67 SER B  453  LEU B  467  1                                  15
HELIX   68  68 SER B  476  SER B  489  1                                  14
HELIX   69  69 THR B  502  LEU B  518  1                                  17
HELIX   70  70 PRO B  519  ASP B  521  5                                   3
HELIX   71  71 SER B  533  CYS B  547  1                                  15
HELIX   72  72 LYS B  561  SER B  577  1                                  17
HELIX   73  73 ILE B  578  ASP B  586  1                                   9
HELIX   74  74 GLY B  594  GLY B  603  1                                  10
HELIX   75  75 GLY B  603  GLY B  626  1                                  24
HELIX   76  76 GLY B  637  ARG B  641  5                                   5
HELIX   77  77 GLY B  643  SER B  652  1                                  10
HELIX   78  78 VAL B  670  GLY B  676  1                                   7
HELIX   79  79 GLU B  677  ASN B  698  1                                  22
HELIX   80  80 ARG B  704  PHE B  727  1                                  24
HELIX   81  81 ARG B  731  THR B  740  1                                  10
HELIX   82  82 PRO B  741  MET B  748  1                                   8
HELIX   83  83 ARG B  767  GLN B  777  1                                  11
HELIX   84  84 HIS B  781  LEU B  786  1                                   6
HELIX   85  85 GLY B  787  ASP B  799  1                                  13
HELIX   86  86 SER B  800  TRP B  813  1                                  14
HELIX   87  87 TRP B  813  LYS B  829  1                                  17
HELIX   88  88 ASP B  831  VAL B  843  1                                  13
HELIX   89  89 SER B  844  ASP B  846  5                                   3
HELIX   90  90 LEU B  847  GLY B  870  1                                  24
HELIX   91  91 ASP B  878  ASP B  908  1                                  31
HELIX   92  92 GLY B  946  GLN B  963  1                                  18
SHEET    1  AA 9 THR A 164  LEU A 169  0
SHEET    2  AA 9 SER A 661  VAL A 666  1  O  LEU A 662   N  ASP A 166
SHEET    3  AA 9 LYS A 628  HIS A 633  1  O  ILE A 631   N  ARG A 663
SHEET    4  AA 9 LYS A 588  ILE A 593  1  O  GLN A 589   N  VAL A 630
SHEET    5  AA 9 ARG A 554  PHE A 559  1  O  PRO A 557   N  MET A 592
SHEET    6  AA 9 PHE A 523  SER A 529  1  O  GLY A 524   N  ARG A 554
SHEET    7  AA 9 LYS A 446  GLU A 452  1  O  LEU A 447   N  GLY A 524
SHEET    8  AA 9 ILE A 278  SER A 282  1  O  PHE A 280   N  LYS A 446
SHEET    9  AA 9 THR A 164  LEU A 169  1  O  VAL A 165   N  GLN A 279
SHEET    1  BA 9 THR B 164  LEU B 169  0
SHEET    2  BA 9 SER B 661  VAL B 666  1  O  LEU B 662   N  ASP B 166
SHEET    3  BA 9 LYS B 628  HIS B 633  1  O  ILE B 631   N  ARG B 663
SHEET    4  BA 9 LYS B 588  ILE B 593  1  O  GLN B 589   N  VAL B 630
SHEET    5  BA 9 ARG B 554  PHE B 559  1  O  PRO B 557   N  MET B 592
SHEET    6  BA 9 PHE B 523  SER B 529  1  O  GLY B 524   N  ARG B 554
SHEET    7  BA 9 LYS B 446  GLU B 452  1  O  LEU B 447   N  GLY B 524
SHEET    8  BA 9 ILE B 278  SER B 282  1  O  PHE B 280   N  LYS B 446
SHEET    9  BA 9 THR B 164  LEU B 169  1  O  VAL B 165   N  GLN B 279
SITE     1 AC1  6 ARG A 641  GLN A 673  LYS A 829  ARG A 884
SITE     2 AC1  6 ARG A 888  ASN A 964
SITE     1 AC2  7 GLY A 636  GLY A 637  ARG A 641  GLN A 667
SITE     2 AC2  7 ASN A 964  THR A 965  GLY A 966
SITE     1 AC3  8 ARG B 641  GLN B 673  MET B 825  LYS B 829
SITE     2 AC3  8 LEU B 881  ARG B 884  ARG B 888  ASN B 964
SITE     1 AC4  8 GLY B 636  GLY B 637  ARG B 641  GLN B 667
SITE     2 AC4  8 LEU B 822  ASN B 964  THR B 965  GLY B 966
SITE     1 AC5  4 ARG B 178  ARG B 179  SER B 180  ARG B 366
SITE     1 AC6  4 ARG A 178  ARG A 179  SER A 180  ARG A 366
SITE     1 AC7  5 ARG A 450  ASP A 597  ARG A 767  ALA A 768
SITE     2 AC7  5 ILE A 769
SITE     1 AC8  6 ARG B 450  ASP B 597  ARG B 635  ARG B 767
SITE     2 AC8  6 ALA B 768  ILE B 769
CRYST1  165.549  121.700  132.031  90.00  90.00  90.00 P 21 21 2     8
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      0.006041  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008217  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007574        0.00000
      
PROCHECK
Go to PROCHECK summary
 References