spacer
spacer

PDBsum entry 3fz8

Go to PDB code: 
Top Page protein ligands Protein-protein interface(s) links
Lyase PDB id
3fz8
Jmol
Contents
Protein chains
(+ 0 more) 455 a.a.
Ligands
PLR ×6
Waters ×60
HEADER    LYASE                                   23-JAN-09   3FZ8
TITLE     CRYSTAL STRUCTURE OF GLUTAMATE DECARBOXYLASE BETA FROM ESCHERICHIA
TITLE    2 COLI: REDUCED SCHIFF BASE WITH PLP
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUTAMATE DECARBOXYLASE BETA;
COMPND   3 CHAIN: A, B, C, D, E, F;
COMPND   4 SYNONYM: GAD-BETA;
COMPND   5 EC: 4.1.1.15;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;
SOURCE   3 ORGANISM_TAXID: 83333;
SOURCE   4 GENE: B1493, GADB, JW1488;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PQE60
KEYWDS    GLUTAMATE DECARBOXYLASE, REDUCED FORM, DECARBOXYLASE, LYASE,
KEYWDS   2 MEMBRANE, PYRIDOXAL PHOSPHATE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    V.N.MALASHKEVICH,D.DE BIASE,F.BOSSA
REVDAT   2   13-JUL-11 3FZ8    1       VERSN
REVDAT   1   03-FEB-09 3FZ8    0
JRNL        AUTH   V.N.MALASHKEVICH,D.DE BIASE,F.BOSSA
JRNL        TITL   CRYSTAL STRUCTURE OF GLUTAMATE DECARBOXYLASE BETA FROM
JRNL        TITL 2 ESCHERICHIA COLI: REDUCED SCHIFF BASE WITH PLP
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0070
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) : 3.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.88
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.4
REMARK   3   NUMBER OF REFLECTIONS             : 60684
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) : 0.169
REMARK   3   R VALUE            (WORKING SET) : 0.165
REMARK   3   FREE R VALUE                     : 0.237
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 3072
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) : 3.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4273
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.30
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2650
REMARK   3   BIN FREE R VALUE SET COUNT          : 208
REMARK   3   BIN FREE R VALUE                    : 0.3730
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 21835
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 90
REMARK   3   SOLVENT ATOMS            : 60
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) : 12.47
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.01000
REMARK   3    B22 (A**2) : 0.01000
REMARK   3    B33 (A**2) : -0.02000
REMARK   3    B12 (A**2) : 0.01000
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): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.455
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.327
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 40.481
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.932
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.853
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 22489 ; 0.013 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 30497 ; 1.496 ; 1.956
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2741 ; 6.271 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1092 ;35.170 ;23.974
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3718 ;19.143 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   152 ;17.463 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3185 ; 0.099 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 17470 ; 0.006 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
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): 13669 ; 1.002 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 21950 ; 4.235 ;20.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  8820 ; 8.743 ;20.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  8547 ; 3.288 ; 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 : 1
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A B C D E F
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A  -9999       A    9999      1
REMARK   3           1     B  -9999       B    9999      1
REMARK   3           1     C  -9999       C    9999      1
REMARK   3           1     D  -9999       D    9999      1
REMARK   3           1     E  -9999       E    9999      1
REMARK   3           1     F  -9999       F    9999      1
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   1    A    (A):   3631 ; 0.290 ; 5.000
REMARK   3   TIGHT POSITIONAL   1    B    (A):   3631 ; 0.270 ; 5.000
REMARK   3   TIGHT POSITIONAL   1    C    (A):   3631 ; 0.290 ; 5.000
REMARK   3   TIGHT POSITIONAL   1    D    (A):   3631 ; 0.280 ; 5.000
REMARK   3   TIGHT POSITIONAL   1    E    (A):   3631 ; 0.400 ; 5.000
REMARK   3   TIGHT POSITIONAL   1    F    (A):   3631 ; 0.290 ; 5.000
REMARK   3   TIGHT THERMAL      1    A (A**2):   3631 ; 3.210 ;10.000
REMARK   3   TIGHT THERMAL      1    B (A**2):   3631 ; 2.960 ;10.000
REMARK   3   TIGHT THERMAL      1    C (A**2):   3631 ; 3.190 ;10.000
REMARK   3   TIGHT THERMAL      1    D (A**2):   3631 ; 3.050 ;10.000
REMARK   3   TIGHT THERMAL      1    E (A**2):   3631 ; 3.450 ;10.000
REMARK   3   TIGHT THERMAL      1    F (A**2):   3631 ; 2.940 ;10.000
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 : 2
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    12        A   466
REMARK   3    RESIDUE RANGE :   A   500        A   500
REMARK   3    ORIGIN FOR THE GROUP (A):  30.5409 -17.9361  -5.6904
REMARK   3    T TENSOR
REMARK   3      T11:   0.0443 T22:   0.0331
REMARK   3      T33:   0.0554 T12:   0.0301
REMARK   3      T13:  -0.0323 T23:  -0.0404
REMARK   3    L TENSOR
REMARK   3      L11:   0.4650 L22:   0.8414
REMARK   3      L33:   0.5724 L12:  -0.0296
REMARK   3      L13:  -0.1297 L23:   0.1955
REMARK   3    S TENSOR
REMARK   3      S11:   0.0181 S12:   0.0117 S13:  -0.0198
REMARK   3      S21:  -0.0401 S22:   0.0714 S23:  -0.1275
REMARK   3      S31:   0.0805 S32:   0.0995 S33:  -0.0895
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 2
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B     4        B   466
REMARK   3    RESIDUE RANGE :   B   500        B   500
REMARK   3    ORIGIN FOR THE GROUP (A):  12.6378 -29.8846  12.7026
REMARK   3    T TENSOR
REMARK   3      T11:   0.1299 T22:   0.0159
REMARK   3      T33:   0.0326 T12:   0.0181
REMARK   3      T13:  -0.0586 T23:   0.0005
REMARK   3    L TENSOR
REMARK   3      L11:   0.7300 L22:   0.4762
REMARK   3      L33:   0.6479 L12:  -0.0595
REMARK   3      L13:   0.2061 L23:  -0.1969
REMARK   3    S TENSOR
REMARK   3      S11:   0.0553 S12:  -0.0632 S13:  -0.0844
REMARK   3      S21:   0.1199 S22:  -0.0029 S23:  -0.0595
REMARK   3      S31:   0.1412 S32:   0.0585 S33:  -0.0524
REMARK   3
REMARK   3   TLS GROUP : 3
REMARK   3    NUMBER OF COMPONENTS GROUP : 2
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C    12        C   466
REMARK   3    RESIDUE RANGE :   C   500        C   500
REMARK   3    ORIGIN FOR THE GROUP (A): -24.8784 -14.7485 -12.6442
REMARK   3    T TENSOR
REMARK   3      T11:   0.0126 T22:   0.0240
REMARK   3      T33:   0.0035 T12:  -0.0085
REMARK   3      T13:   0.0027 T23:   0.0034
REMARK   3    L TENSOR
REMARK   3      L11:   0.4416 L22:   0.6659
REMARK   3      L33:   0.7123 L12:  -0.1313
REMARK   3      L13:   0.2872 L23:   0.1088
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0067 S12:  -0.0583 S13:  -0.0112
REMARK   3      S21:   0.0314 S22:   0.0186 S23:   0.0433
REMARK   3      S31:   0.0128 S32:  -0.1064 S33:  -0.0120
REMARK   3
REMARK   3   TLS GROUP : 4
REMARK   3    NUMBER OF COMPONENTS GROUP : 2
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   D    12        D   466
REMARK   3    RESIDUE RANGE :   D   500        D   500
REMARK   3    ORIGIN FOR THE GROUP (A): -30.6473   4.4990   8.0410
REMARK   3    T TENSOR
REMARK   3      T11:   0.0148 T22:   0.0592
REMARK   3      T33:   0.0238 T12:  -0.0082
REMARK   3      T13:   0.0172 T23:  -0.0081
REMARK   3    L TENSOR
REMARK   3      L11:   0.6531 L22:   0.5005
REMARK   3      L33:   0.5099 L12:   0.2601
REMARK   3      L13:  -0.2893 L23:   0.1482
REMARK   3    S TENSOR
REMARK   3      S11:   0.0438 S12:  -0.0478 S13:   0.0776
REMARK   3      S21:   0.0781 S22:  -0.0532 S23:   0.1060
REMARK   3      S31:   0.0280 S32:  -0.1003 S33:   0.0094
REMARK   3
REMARK   3   TLS GROUP : 5
REMARK   3    NUMBER OF COMPONENTS GROUP : 3
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   E     3        E   466
REMARK   3    RESIDUE RANGE :   E   500        E   500
REMARK   3    RESIDUE RANGE :   E   467        E   527
REMARK   3    ORIGIN FOR THE GROUP (A):   5.3713  31.9418  -7.8638
REMARK   3    T TENSOR
REMARK   3      T11:   0.0260 T22:   0.0087
REMARK   3      T33:   0.0020 T12:  -0.0054
REMARK   3      T13:  -0.0039 T23:  -0.0011
REMARK   3    L TENSOR
REMARK   3      L11:   0.5997 L22:   0.5036
REMARK   3      L33:   0.5092 L12:   0.1863
REMARK   3      L13:   0.0422 L23:  -0.0262
REMARK   3    S TENSOR
REMARK   3      S11:   0.0303 S12:   0.0180 S13:   0.0100
REMARK   3      S21:  -0.0231 S22:  -0.0315 S23:   0.0278
REMARK   3      S31:  -0.0723 S32:   0.0544 S33:   0.0012
REMARK   3
REMARK   3   TLS GROUP : 6
REMARK   3    NUMBER OF COMPONENTS GROUP : 2
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   F    12        F   466
REMARK   3    RESIDUE RANGE :   F   500        F   500
REMARK   3    ORIGIN FOR THE GROUP (A):  20.8959  25.2825  14.6224
REMARK   3    T TENSOR
REMARK   3      T11:   0.0130 T22:   0.0114
REMARK   3      T33:   0.0132 T12:  -0.0113
REMARK   3      T13:   0.0069 T23:  -0.0097
REMARK   3    L TENSOR
REMARK   3      L11:   0.3234 L22:   0.7025
REMARK   3      L33:   0.6279 L12:  -0.1150
REMARK   3      L13:   0.1493 L23:   0.1692
REMARK   3    S TENSOR
REMARK   3      S11:   0.0070 S12:  -0.0071 S13:   0.0157
REMARK   3      S21:  -0.0064 S22:   0.0370 S23:  -0.0847
REMARK   3      S31:  -0.0402 S32:   0.0520 S33:  -0.0440
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: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS. 2. U VALUES: RESIDUAL ONLY.
REMARK   4
REMARK   4 3FZ8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JAN-09.
REMARK 100 THE RCSB ID CODE IS RCSB051222.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 07-OCT-96
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.6
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG
REMARK 200  BEAMLINE                       : BW7B
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63606
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.4
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 52.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 M AMMONIUM SULFATE, 0.1 M TRIS-
REMARK 280  HCL, PH 7.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+2/3
REMARK 290       3555   -X+Y,-X,Z+1/3
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -0.499991 -0.866040  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866011 -0.500009  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      139.05733
REMARK 290   SMTRY1   3 -0.500009  0.866040  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866011 -0.499991  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       69.52867
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 47410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 87500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -217.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 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     ASP A     2
REMARK 465     LYS A     3
REMARK 465     LYS A     4
REMARK 465     GLN A     5
REMARK 465     VAL A     6
REMARK 465     THR A     7
REMARK 465     ASP A     8
REMARK 465     LEU A     9
REMARK 465     ARG A    10
REMARK 465     SER A    11
REMARK 465     MET B     1
REMARK 465     ASP B     2
REMARK 465     LYS B     3
REMARK 465     MET C     1
REMARK 465     ASP C     2
REMARK 465     LYS C     3
REMARK 465     LYS C     4
REMARK 465     GLN C     5
REMARK 465     VAL C     6
REMARK 465     THR C     7
REMARK 465     ASP C     8
REMARK 465     LEU C     9
REMARK 465     ARG C    10
REMARK 465     SER C    11
REMARK 465     MET D     1
REMARK 465     ASP D     2
REMARK 465     LYS D     3
REMARK 465     LYS D     4
REMARK 465     GLN D     5
REMARK 465     VAL D     6
REMARK 465     THR D     7
REMARK 465     ASP D     8
REMARK 465     LEU D     9
REMARK 465     ARG D    10
REMARK 465     SER D    11
REMARK 465     MET E     1
REMARK 465     ASP E     2
REMARK 465     MET F     1
REMARK 465     ASP F     2
REMARK 465     LYS F     3
REMARK 465     LYS F     4
REMARK 465     GLN F     5
REMARK 465     VAL F     6
REMARK 465     THR F     7
REMARK 465     ASP F     8
REMARK 465     LEU F     9
REMARK 465     ARG F    10
REMARK 465     SER F    11
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 D   352     OE1  GLU D   435              2.14
REMARK 500   O    ALA A    27     N    SER A    29              2.18
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    LYS C 276   CE    LYS C 276   NZ     -0.175
REMARK 500    CYS E 367   CB    CYS E 367   SG     -0.101
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    LYS C 276   CD  -  CE  -  NZ  ANGL. DEV. =  19.9 DEGREES
REMARK 500    LEU E 157   CA  -  CB  -  CG  ANGL. DEV. =  19.0 DEGREES
REMARK 500    LEU E 436   CA  -  CB  -  CG  ANGL. DEV. =  15.3 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    ALA A  27     -113.69    -73.66
REMARK 500    GLU A  28       66.29    -46.12
REMARK 500    SER A  29       37.49   -150.19
REMARK 500    ALA A  56      -13.71     74.53
REMARK 500    PRO A 161       75.17    -58.73
REMARK 500    ARG A 178       72.26   -107.47
REMARK 500    GLN A 186       87.68   -156.23
REMARK 500    MET A 194      -71.11    -51.83
REMARK 500    ASP A 199     -168.38   -164.18
REMARK 500    LEU A 250      -59.12   -126.58
REMARK 500    ALA A 255       72.30   -161.67
REMARK 500    ASP A 261     -152.49   -108.21
REMARK 500    PHE A 262       -8.42    -59.09
REMARK 500    LYS A 276     -113.57    -98.84
REMARK 500    PHE A 317      -96.44   -113.64
REMARK 500    PRO A 376       76.63    -69.40
REMARK 500    GLN A 459       35.79   -157.72
REMARK 500    SER B  11       50.17   -101.59
REMARK 500    GLU B  28       65.61     20.71
REMARK 500    ALA B  56       -9.23     72.78
REMARK 500    TYR B  90       69.35   -116.57
REMARK 500    ALA B 112      125.36    -38.42
REMARK 500    PRO B 161       83.12    -65.15
REMARK 500    GLN B 186       66.63   -178.92
REMARK 500    ALA B 244       37.40    -87.89
REMARK 500    LEU B 250      -72.07   -109.80
REMARK 500    TRP B 260      -18.22   -148.55
REMARK 500    ASP B 261     -146.96    -97.67
REMARK 500    SER B 269      141.89   -174.51
REMARK 500    LYS B 276     -111.90   -114.30
REMARK 500    LEU B 282      135.75    -36.94
REMARK 500    PHE B 317      -95.30   -117.28
REMARK 500    ARG B 319      161.86    175.46
REMARK 500    ALA B 434      -51.14    -29.34
REMARK 500    GLN B 459       23.29   -151.10
REMARK 500    GLU C  28       36.04     39.94
REMARK 500    ALA C  56       -4.35     73.92
REMARK 500    TYR C  90       67.08   -114.19
REMARK 500    ALA C 112      124.61    -38.82
REMARK 500    PRO C 161       66.54    -68.30
REMARK 500    ALA C 244       37.00    -94.56
REMARK 500    LEU C 250      -68.46   -123.06
REMARK 500    ASP C 261     -150.23   -109.13
REMARK 500    PHE C 262        6.01    -65.92
REMARK 500    LYS C 276     -114.71    -92.62
REMARK 500    LEU C 282      128.62    -37.98
REMARK 500    PHE C 317      -99.39   -119.55
REMARK 500    GLN C 459       25.56   -145.57
REMARK 500    ALA D  27     -173.39    -69.03
REMARK 500    GLU D  28       46.27     22.14
REMARK 500
REMARK 500 THIS ENTRY HAS      92 RAMACHANDRAN OUTLIERS.
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    GLU A  49        23.1      L          L   OUTSIDE RANGE
REMARK 500    GLU C  49        23.2      L          L   OUTSIDE RANGE
REMARK 500    ASP C 257        22.6      L          L   OUTSIDE RANGE
REMARK 500    GLU D  49        24.9      L          L   OUTSIDE RANGE
REMARK 500    GLU F  28        23.7      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH E 486        DISTANCE =  7.59 ANGSTROMS
REMARK 525    HOH E 519        DISTANCE =  5.96 ANGSTROMS
REMARK 525    HOH E 525        DISTANCE =  5.18 ANGSTROMS
REMARK 525    HOH E 526        DISTANCE =  6.34 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLR A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLR B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLR C 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLR D 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLR E 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLR F 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FZ6   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GLUTAMATE DECARBOXYLASE BETA FROM
REMARK 900 ESCHERICHIA COLI: COMPLEX WITH XENON
REMARK 900 RELATED ID: 3FZ7   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF APO GLUTAMATE DECARBOXYLASE BETA FROM
REMARK 900 ESCHERICHIA COLI
DBREF  3FZ8 A    1   466  UNP    P69910   DCEB_ECOLI       1    466
DBREF  3FZ8 B    1   466  UNP    P69910   DCEB_ECOLI       1    466
DBREF  3FZ8 C    1   466  UNP    P69910   DCEB_ECOLI       1    466
DBREF  3FZ8 D    1   466  UNP    P69910   DCEB_ECOLI       1    466
DBREF  3FZ8 E    1   466  UNP    P69910   DCEB_ECOLI       1    466
DBREF  3FZ8 F    1   466  UNP    P69910   DCEB_ECOLI       1    466
SEQRES   1 A  466  MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU
SEQRES   2 A  466  LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE
SEQRES   3 A  466  ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP
SEQRES   4 A  466  ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU
SEQRES   5 A  466  ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN
SEQRES   6 A  466  THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU
SEQRES   7 A  466  SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO
SEQRES   8 A  466  GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL
SEQRES   9 A  466  ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN
SEQRES  10 A  466  ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS
SEQRES  11 A  466  MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS
SEQRES  12 A  466  ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN
SEQRES  13 A  466  LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE
SEQRES  14 A  466  ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET
SEQRES  15 A  466  ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE
SEQRES  16 A  466  GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR
SEQRES  17 A  466  PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN
SEQRES  18 A  466  PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR
SEQRES  19 A  466  GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY
SEQRES  20 A  466  GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP
SEQRES  21 A  466  ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER
SEQRES  22 A  466  GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP
SEQRES  23 A  466  VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU
SEQRES  24 A  466  VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR
SEQRES  25 A  466  PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE
SEQRES  26 A  466  ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY
SEQRES  27 A  466  TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA
SEQRES  28 A  466  TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU
SEQRES  29 A  466  PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA
SEQRES  30 A  466  VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR
SEQRES  31 A  466  THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY
SEQRES  32 A  466  TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR
SEQRES  33 A  466  ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE
SEQRES  34 A  466  GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS
SEQRES  35 A  466  ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN
SEQRES  36 A  466  GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR
SEQRES   1 B  466  MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU
SEQRES   2 B  466  LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE
SEQRES   3 B  466  ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP
SEQRES   4 B  466  ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU
SEQRES   5 B  466  ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN
SEQRES   6 B  466  THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU
SEQRES   7 B  466  SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO
SEQRES   8 B  466  GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL
SEQRES   9 B  466  ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN
SEQRES  10 B  466  ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS
SEQRES  11 B  466  MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS
SEQRES  12 B  466  ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN
SEQRES  13 B  466  LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE
SEQRES  14 B  466  ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET
SEQRES  15 B  466  ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE
SEQRES  16 B  466  GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR
SEQRES  17 B  466  PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN
SEQRES  18 B  466  PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR
SEQRES  19 B  466  GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY
SEQRES  20 B  466  GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP
SEQRES  21 B  466  ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER
SEQRES  22 B  466  GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP
SEQRES  23 B  466  VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU
SEQRES  24 B  466  VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR
SEQRES  25 B  466  PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE
SEQRES  26 B  466  ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY
SEQRES  27 B  466  TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA
SEQRES  28 B  466  TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU
SEQRES  29 B  466  PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA
SEQRES  30 B  466  VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR
SEQRES  31 B  466  THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY
SEQRES  32 B  466  TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR
SEQRES  33 B  466  ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE
SEQRES  34 B  466  GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS
SEQRES  35 B  466  ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN
SEQRES  36 B  466  GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR
SEQRES   1 C  466  MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU
SEQRES   2 C  466  LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE
SEQRES   3 C  466  ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP
SEQRES   4 C  466  ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU
SEQRES   5 C  466  ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN
SEQRES   6 C  466  THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU
SEQRES   7 C  466  SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO
SEQRES   8 C  466  GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL
SEQRES   9 C  466  ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN
SEQRES  10 C  466  ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS
SEQRES  11 C  466  MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS
SEQRES  12 C  466  ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN
SEQRES  13 C  466  LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE
SEQRES  14 C  466  ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET
SEQRES  15 C  466  ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE
SEQRES  16 C  466  GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR
SEQRES  17 C  466  PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN
SEQRES  18 C  466  PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR
SEQRES  19 C  466  GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY
SEQRES  20 C  466  GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP
SEQRES  21 C  466  ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER
SEQRES  22 C  466  GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP
SEQRES  23 C  466  VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU
SEQRES  24 C  466  VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR
SEQRES  25 C  466  PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE
SEQRES  26 C  466  ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY
SEQRES  27 C  466  TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA
SEQRES  28 C  466  TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU
SEQRES  29 C  466  PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA
SEQRES  30 C  466  VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR
SEQRES  31 C  466  THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY
SEQRES  32 C  466  TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR
SEQRES  33 C  466  ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE
SEQRES  34 C  466  GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS
SEQRES  35 C  466  ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN
SEQRES  36 C  466  GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR
SEQRES   1 D  466  MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU
SEQRES   2 D  466  LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE
SEQRES   3 D  466  ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP
SEQRES   4 D  466  ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU
SEQRES   5 D  466  ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN
SEQRES   6 D  466  THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU
SEQRES   7 D  466  SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO
SEQRES   8 D  466  GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL
SEQRES   9 D  466  ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN
SEQRES  10 D  466  ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS
SEQRES  11 D  466  MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS
SEQRES  12 D  466  ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN
SEQRES  13 D  466  LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE
SEQRES  14 D  466  ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET
SEQRES  15 D  466  ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE
SEQRES  16 D  466  GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR
SEQRES  17 D  466  PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN
SEQRES  18 D  466  PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR
SEQRES  19 D  466  GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY
SEQRES  20 D  466  GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP
SEQRES  21 D  466  ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER
SEQRES  22 D  466  GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP
SEQRES  23 D  466  VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU
SEQRES  24 D  466  VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR
SEQRES  25 D  466  PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE
SEQRES  26 D  466  ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY
SEQRES  27 D  466  TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA
SEQRES  28 D  466  TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU
SEQRES  29 D  466  PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA
SEQRES  30 D  466  VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR
SEQRES  31 D  466  THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY
SEQRES  32 D  466  TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR
SEQRES  33 D  466  ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE
SEQRES  34 D  466  GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS
SEQRES  35 D  466  ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN
SEQRES  36 D  466  GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR
SEQRES   1 E  466  MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU
SEQRES   2 E  466  LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE
SEQRES   3 E  466  ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP
SEQRES   4 E  466  ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU
SEQRES   5 E  466  ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN
SEQRES   6 E  466  THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU
SEQRES   7 E  466  SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO
SEQRES   8 E  466  GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL
SEQRES   9 E  466  ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN
SEQRES  10 E  466  ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS
SEQRES  11 E  466  MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS
SEQRES  12 E  466  ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN
SEQRES  13 E  466  LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE
SEQRES  14 E  466  ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET
SEQRES  15 E  466  ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE
SEQRES  16 E  466  GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR
SEQRES  17 E  466  PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN
SEQRES  18 E  466  PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR
SEQRES  19 E  466  GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY
SEQRES  20 E  466  GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP
SEQRES  21 E  466  ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER
SEQRES  22 E  466  GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP
SEQRES  23 E  466  VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU
SEQRES  24 E  466  VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR
SEQRES  25 E  466  PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE
SEQRES  26 E  466  ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY
SEQRES  27 E  466  TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA
SEQRES  28 E  466  TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU
SEQRES  29 E  466  PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA
SEQRES  30 E  466  VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR
SEQRES  31 E  466  THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY
SEQRES  32 E  466  TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR
SEQRES  33 E  466  ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE
SEQRES  34 E  466  GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS
SEQRES  35 E  466  ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN
SEQRES  36 E  466  GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR
SEQRES   1 F  466  MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU
SEQRES   2 F  466  LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE
SEQRES   3 F  466  ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP
SEQRES   4 F  466  ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU
SEQRES   5 F  466  ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN
SEQRES   6 F  466  THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU
SEQRES   7 F  466  SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO
SEQRES   8 F  466  GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL
SEQRES   9 F  466  ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN
SEQRES  10 F  466  ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS
SEQRES  11 F  466  MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS
SEQRES  12 F  466  ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN
SEQRES  13 F  466  LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE
SEQRES  14 F  466  ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET
SEQRES  15 F  466  ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE
SEQRES  16 F  466  GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR
SEQRES  17 F  466  PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN
SEQRES  18 F  466  PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR
SEQRES  19 F  466  GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY
SEQRES  20 F  466  GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP
SEQRES  21 F  466  ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER
SEQRES  22 F  466  GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP
SEQRES  23 F  466  VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU
SEQRES  24 F  466  VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR
SEQRES  25 F  466  PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE
SEQRES  26 F  466  ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY
SEQRES  27 F  466  TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA
SEQRES  28 F  466  TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU
SEQRES  29 F  466  PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA
SEQRES  30 F  466  VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR
SEQRES  31 F  466  THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY
SEQRES  32 F  466  TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR
SEQRES  33 F  466  ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE
SEQRES  34 F  466  GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS
SEQRES  35 F  466  ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN
SEQRES  36 F  466  GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR
HET    PLR  A 500      15
HET    PLR  B 500      15
HET    PLR  C 500      15
HET    PLR  D 500      15
HET    PLR  E 500      15
HET    PLR  F 500      15
HETNAM     PLR (5-HYDROXY-4,6-DIMETHYLPYRIDIN-3-YL)METHYL DIHYDROGEN
HETNAM   2 PLR  PHOSPHATE
HETSYN     PLR 4'-DEOXYPYRIDOXINE PHOSPHATE
FORMUL   7  PLR    6(C8 H12 N O5 P)
FORMUL  13  HOH   *60(H2 O)
HELIX    1   1 ARG A   38  TYR A   51  1                                  14
HELIX    2   2 ASP A   69  SER A   79  1                                  11
HELIX    3   3 TYR A   90  TRP A  108  1                                  19
HELIX    4   4 GLY A  125  ALA A  148  1                                  24
HELIX    5   5 GLN A  163  TRP A  173  1                                  11
HELIX    6   6 ASP A  190  ALA A  197  1                                   8
HELIX    7   7 PHE A  219  GLY A  235  1                                  17
HELIX    8   8 SER A  246  PHE A  249  5                                   4
HELIX    9   9 LEU A  250  ALA A  255  1                                   6
HELIX   10  10 ASP A  291  LEU A  295  5                                   5
HELIX   11  11 PRO A  296  VAL A  300  5                                   5
HELIX   12  12 ALA A  321  LYS A  359  1                                  39
HELIX   13  13 THR A  391  ARG A  402  1                                  12
HELIX   14  14 GLU A  430  HIS A  451  1                                  22
HELIX   15  15 PRO A  452  GLN A  455  5                                   4
HELIX   16  16 ARG B   38  GLU B   49  1                                  12
HELIX   17  17 ASP B   69  SER B   79  1                                  11
HELIX   18  18 TYR B   90  TRP B  108  1                                  19
HELIX   19  19 GLY B  125  ALA B  148  1                                  24
HELIX   20  20 GLN B  163  TRP B  173  1                                  11
HELIX   21  21 ASP B  190  CYS B  198  1                                   9
HELIX   22  22 PHE B  219  GLY B  235  1                                  17
HELIX   23  23 SER B  246  PHE B  249  5                                   4
HELIX   24  24 LEU B  250  ALA B  255  1                                   6
HELIX   25  25 ASP B  291  LEU B  295  5                                   5
HELIX   26  26 PRO B  296  VAL B  300  5                                   5
HELIX   27  27 ALA B  321  ALA B  358  1                                  38
HELIX   28  28 LYS B  359  GLY B  361  5                                   3
HELIX   29  29 THR B  391  LEU B  401  1                                  11
HELIX   30  30 GLU B  414  ASP B  417  5                                   4
HELIX   31  31 GLU B  430  HIS B  451  1                                  22
HELIX   32  32 PRO B  452  GLN B  455  5                                   4
HELIX   33  33 ARG C   38  TYR C   51  1                                  14
HELIX   34  34 ASP C   69  SER C   79  1                                  11
HELIX   35  35 ILE C   80  LYS C   82  5                                   3
HELIX   36  36 TYR C   90  TRP C  108  1                                  19
HELIX   37  37 GLY C  125  ALA C  148  1                                  24
HELIX   38  38 ILE C  164  TRP C  173  1                                  10
HELIX   39  39 ASP C  190  ALA C  197  1                                   8
HELIX   40  40 PHE C  219  GLY C  235  1                                  17
HELIX   41  41 SER C  246  PHE C  249  5                                   4
HELIX   42  42 LEU C  250  ALA C  255  1                                   6
HELIX   43  43 ASP C  291  LEU C  295  5                                   5
HELIX   44  44 PRO C  296  VAL C  300  5                                   5
HELIX   45  45 ALA C  321  ALA C  358  1                                  38
HELIX   46  46 THR C  391  LEU C  401  1                                  11
HELIX   47  47 GLU C  430  HIS C  451  1                                  22
HELIX   48  48 PRO C  452  GLN C  455  5                                   4
HELIX   49  49 ARG D   38  TYR D   51  1                                  14
HELIX   50  50 ASP D   69  SER D   79  1                                  11
HELIX   51  51 TYR D   90  TRP D  108  1                                  19
HELIX   52  52 GLY D  125  GLY D  149  1                                  25
HELIX   53  53 ILE D  164  ASP D  174  1                                  11
HELIX   54  54 ASP D  190  ALA D  197  1                                   8
HELIX   55  55 PHE D  219  GLY D  235  1                                  17
HELIX   56  56 SER D  246  PHE D  249  5                                   4
HELIX   57  57 LEU D  250  ALA D  255  1                                   6
HELIX   58  58 ALA D  321  LYS D  359  1                                  39
HELIX   59  59 THR D  391  LEU D  401  1                                  11
HELIX   60  60 GLU D  430  HIS D  451  1                                  22
HELIX   61  61 PRO D  452  GLN D  455  5                                   4
HELIX   62  62 ARG E   38  LEU E   50  1                                  13
HELIX   63  63 TYR E   51  ASP E   53  5                                   3
HELIX   64  64 ASP E   69  ILE E   80  1                                  12
HELIX   65  65 TYR E   90  TRP E  108  1                                  19
HELIX   66  66 GLY E  125  ALA E  148  1                                  24
HELIX   67  67 GLN E  163  TRP E  173  1                                  11
HELIX   68  68 ASP E  190  ALA E  197  1                                   8
HELIX   69  69 PHE E  219  GLY E  235  1                                  17
HELIX   70  70 SER E  246  PHE E  249  5                                   4
HELIX   71  71 LEU E  250  ALA E  255  1                                   6
HELIX   72  72 ASP E  291  LEU E  295  5                                   5
HELIX   73  73 PRO E  296  VAL E  300  5                                   5
HELIX   74  74 ALA E  321  ALA E  358  1                                  38
HELIX   75  75 THR E  391  ARG E  402  1                                  12
HELIX   76  76 GLY E  412  THR E  416  5                                   5
HELIX   77  77 GLU E  430  HIS E  451  1                                  22
HELIX   78  78 PRO E  452  GLN E  455  5                                   4
HELIX   79  79 ARG F   38  LEU F   50  1                                  13
HELIX   80  80 TYR F   51  ASP F   53  5                                   3
HELIX   81  81 ASP F   69  SER F   79  1                                  11
HELIX   82  82 TYR F   90  TRP F  108  1                                  19
HELIX   83  83 GLY F  125  GLY F  149  1                                  25
HELIX   84  84 GLN F  163  TRP F  173  1                                  11
HELIX   85  85 ASP F  190  CYS F  198  1                                   9
HELIX   86  86 PHE F  219  GLY F  235  1                                  17
HELIX   87  87 SER F  246  PHE F  249  5                                   4
HELIX   88  88 LEU F  250  ALA F  255  1                                   6
HELIX   89  89 ASP F  291  LEU F  295  5                                   5
HELIX   90  90 PRO F  296  VAL F  300  5                                   5
HELIX   91  91 ALA F  321  LYS F  359  1                                  39
HELIX   92  92 THR F  391  LEU F  401  1                                  11
HELIX   93  93 GLU F  430  HIS F  451  1                                  22
HELIX   94  94 PRO F  452  GLN F  455  5                                   4
SHEET    1   A 2 LEU A  14  ASP A  15  0
SHEET    2   A 2 ALA A  20  LYS A  21 -1  O  ALA A  20   N  ASP A  15
SHEET    1   B 4 GLY A 120  THR A 123  0
SHEET    2   B 4 GLY A 285  TRP A 289 -1  O  GLY A 285   N  THR A 123
SHEET    3   B 4 VAL A 267  SER A 273 -1  N  ALA A 272   O  TRP A 286
SHEET    4   B 4 MET A 240  ASP A 243  1  N  MET A 240   O  LYS A 268
SHEET    1   C 3 GLU A 176  GLU A 179  0
SHEET    2   C 3 ASN A 156  CYS A 159  1  N  LEU A 157   O  ARG A 178
SHEET    3   C 3 THR A 202  VAL A 206  1  O  ILE A 203   N  ASN A 156
SHEET    1   D 2 PHE A 301  TYR A 305  0
SHEET    2   D 2 GLY A 308  THR A 312 -1  O  THR A 312   N  PHE A 301
SHEET    1   E 4 TYR A 363  THR A 368  0
SHEET    2   E 4 ALA A 377  LEU A 382 -1  O  CYS A 379   N  ILE A 366
SHEET    3   E 4 VAL A 419  MET A 424 -1  O  ILE A 423   N  VAL A 378
SHEET    4   E 4 ALA A 408  THR A 410 -1  N  PHE A 409   O  VAL A 420
SHEET    1   F 2 LEU B  14  ASP B  15  0
SHEET    2   F 2 ALA B  20  LYS B  21 -1  O  ALA B  20   N  ASP B  15
SHEET    1   G 4 VAL B 119  THR B 123  0
SHEET    2   G 4 GLY B 285  TRP B 289 -1  O  TRP B 289   N  VAL B 119
SHEET    3   G 4 VAL B 267  SER B 273 -1  N  ILE B 270   O  ILE B 288
SHEET    4   G 4 MET B 240  ASP B 243  1  N  ILE B 242   O  SER B 271
SHEET    1   H 3 GLU B 176  GLU B 179  0
SHEET    2   H 3 ASN B 156  CYS B 159  1  N  LEU B 157   O  ARG B 178
SHEET    3   H 3 THR B 202  VAL B 206  1  O  ILE B 203   N  ASN B 156
SHEET    1   I 2 PHE B 301  TYR B 305  0
SHEET    2   I 2 GLY B 308  THR B 312 -1  O  THR B 312   N  PHE B 301
SHEET    1   J 4 TYR B 363  THR B 368  0
SHEET    2   J 4 ALA B 377  LEU B 382 -1  O  LYS B 381   N  GLU B 364
SHEET    3   J 4 VAL B 419  MET B 424 -1  O  ILE B 423   N  VAL B 378
SHEET    4   J 4 ALA B 408  THR B 410 -1  N  PHE B 409   O  VAL B 420
SHEET    1   K 2 LEU C  14  ASP C  15  0
SHEET    2   K 2 ALA C  20  LYS C  21 -1  O  ALA C  20   N  ASP C  15
SHEET    1   L 4 VAL C 119  THR C 123  0
SHEET    2   L 4 GLY C 285  TRP C 289 -1  O  TRP C 289   N  VAL C 119
SHEET    3   L 4 VAL C 267  SER C 273 -1  N  ALA C 272   O  TRP C 286
SHEET    4   L 4 MET C 240  ASP C 243  1  N  MET C 240   O  LYS C 268
SHEET    1   M 3 GLU C 176  GLU C 179  0
SHEET    2   M 3 ASN C 156  CYS C 159  1  N  LEU C 157   O  ARG C 178
SHEET    3   M 3 THR C 202  VAL C 206  1  O  ILE C 203   N  ASN C 156
SHEET    1   N 2 PHE C 301  TYR C 305  0
SHEET    2   N 2 GLY C 308  THR C 312 -1  O  THR C 312   N  PHE C 301
SHEET    1   O 4 TYR C 363  THR C 368  0
SHEET    2   O 4 ALA C 377  LEU C 382 -1  O  LYS C 381   N  GLU C 364
SHEET    3   O 4 VAL C 419  MET C 424 -1  O  ILE C 423   N  VAL C 378
SHEET    4   O 4 ALA C 408  THR C 410 -1  N  PHE C 409   O  VAL C 420
SHEET    1   P 2 LEU D  14  ASP D  15  0
SHEET    2   P 2 ALA D  20  LYS D  21 -1  O  ALA D  20   N  ASP D  15
SHEET    1   Q 4 GLY D 120  THR D 123  0
SHEET    2   Q 4 GLY D 285  TRP D 289 -1  O  GLY D 285   N  THR D 123
SHEET    3   Q 4 VAL D 267  SER D 273 -1  N  ILE D 270   O  ILE D 288
SHEET    4   Q 4 MET D 240  ASP D 243  1  N  ILE D 242   O  SER D 269
SHEET    1   R 3 GLU D 176  GLU D 179  0
SHEET    2   R 3 ASN D 156  CYS D 159  1  N  LEU D 157   O  ARG D 178
SHEET    3   R 3 THR D 202  VAL D 206  1  O  VAL D 206   N  VAL D 158
SHEET    1   S 2 PHE D 301  TYR D 305  0
SHEET    2   S 2 GLY D 308  THR D 312 -1  O  THR D 312   N  PHE D 301
SHEET    1   T 4 TYR D 363  THR D 368  0
SHEET    2   T 4 ALA D 377  LEU D 382 -1  O  LYS D 381   N  GLU D 364
SHEET    3   T 4 VAL D 419  MET D 424 -1  O  ILE D 423   N  VAL D 378
SHEET    4   T 4 ALA D 408  THR D 410 -1  N  PHE D 409   O  VAL D 420
SHEET    1   U 4 VAL E 119  THR E 123  0
SHEET    2   U 4 GLY E 285  TRP E 289 -1  O  GLY E 285   N  THR E 123
SHEET    3   U 4 VAL E 267  SER E 273 -1  N  ALA E 272   O  TRP E 286
SHEET    4   U 4 MET E 240  ASP E 243  1  N  MET E 240   O  LYS E 268
SHEET    1   V 3 GLU E 176  GLU E 179  0
SHEET    2   V 3 ASN E 156  CYS E 159  1  N  LEU E 157   O  ARG E 178
SHEET    3   V 3 THR E 202  VAL E 206  1  O  ILE E 203   N  ASN E 156
SHEET    1   W 2 PHE E 301  TYR E 305  0
SHEET    2   W 2 GLY E 308  THR E 312 -1  O  THR E 312   N  PHE E 301
SHEET    1   X 4 TYR E 363  THR E 368  0
SHEET    2   X 4 ALA E 377  LEU E 382 -1  O  LYS E 381   N  GLU E 364
SHEET    3   X 4 VAL E 419  MET E 424 -1  O  ILE E 423   N  VAL E 378
SHEET    4   X 4 ALA E 408  THR E 410 -1  N  PHE E 409   O  VAL E 420
SHEET    1   Y 2 LEU F  14  ASP F  15  0
SHEET    2   Y 2 ALA F  20  LYS F  21 -1  O  ALA F  20   N  ASP F  15
SHEET    1   Z 4 GLY F 120  THR F 123  0
SHEET    2   Z 4 GLY F 285  TRP F 289 -1  O  GLY F 285   N  THR F 123
SHEET    3   Z 4 VAL F 267  SER F 273 -1  N  ILE F 270   O  ILE F 288
SHEET    4   Z 4 MET F 240  ASP F 243  1  N  MET F 240   O  LYS F 268
SHEET    1  AA 3 GLU F 176  GLU F 179  0
SHEET    2  AA 3 ASN F 156  CYS F 159  1  N  LEU F 157   O  ARG F 178
SHEET    3  AA 3 THR F 202  VAL F 206  1  O  ILE F 203   N  ASN F 156
SHEET    1  AB 2 PHE F 301  TYR F 305  0
SHEET    2  AB 2 GLY F 308  THR F 312 -1  O  THR F 312   N  PHE F 301
SHEET    1  AC 4 TYR F 363  CYS F 367  0
SHEET    2  AC 4 ALA F 377  LEU F 382 -1  O  CYS F 379   N  CYS F 367
SHEET    3  AC 4 VAL F 419  MET F 424 -1  O  ILE F 423   N  VAL F 378
SHEET    4  AC 4 ALA F 408  THR F 410 -1  N  PHE F 409   O  VAL F 420
LINK         NZ  LYS A 276                 C4A PLR A 500     1555   1555  1.60
LINK         NZ  LYS B 276                 C4A PLR B 500     1555   1555  1.50
LINK         NZ  LYS C 276                 C4A PLR C 500     1555   1555  1.50
LINK         NZ  LYS D 276                 C4A PLR D 500     1555   1555  1.54
LINK         NZ  LYS E 276                 C4A PLR E 500     1555   1555  1.51
LINK         NZ  LYS F 276                 C4A PLR F 500     1555   1555  1.54
SITE     1 AC1 15 SER A 126  SER A 127  GLN A 163  THR A 208
SITE     2 AC1 15 GLY A 210  THR A 212  ASP A 243  ALA A 245
SITE     3 AC1 15 SER A 273  HIS A 275  LYS A 276  HIS A 465
SITE     4 AC1 15 THR A 466  PHE B 317  SER B 318
SITE     1 AC2 14 PHE A 317  SER A 318  GLY B 125  SER B 126
SITE     2 AC2 14 SER B 127  GLN B 163  THR B 208  THR B 212
SITE     3 AC2 14 ASP B 243  ALA B 245  SER B 273  HIS B 275
SITE     4 AC2 14 LYS B 276  THR B 466
SITE     1 AC3 15 SER C 126  SER C 127  GLN C 163  THR C 208
SITE     2 AC3 15 GLY C 210  THR C 212  ASP C 243  ALA C 245
SITE     3 AC3 15 SER C 273  HIS C 275  LYS C 276  HIS C 465
SITE     4 AC3 15 THR C 466  PHE D 317  SER D 318
SITE     1 AC4 15 PHE C 317  SER C 318  GLY D 125  SER D 126
SITE     2 AC4 15 SER D 127  GLN D 163  THR D 208  THR D 212
SITE     3 AC4 15 ASP D 243  ALA D 245  SER D 273  HIS D 275
SITE     4 AC4 15 LYS D 276  HIS D 465  THR D 466
SITE     1 AC5 15 GLY E 125  SER E 126  SER E 127  GLN E 163
SITE     2 AC5 15 THR E 208  GLY E 210  THR E 212  ASP E 243
SITE     3 AC5 15 ALA E 245  SER E 273  HIS E 275  LYS E 276
SITE     4 AC5 15 THR E 466  PHE F 317  SER F 318
SITE     1 AC6 14 PHE E 317  SER E 318  GLY F 125  SER F 126
SITE     2 AC6 14 SER F 127  GLN F 163  GLY F 210  THR F 212
SITE     3 AC6 14 ASP F 243  ALA F 245  SER F 273  HIS F 275
SITE     4 AC6 14 LYS F 276  THR F 466
CRYST1  116.896  116.894  208.586  90.00  90.00 120.00 P 32         18
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      0.008555  0.004939  0.000000        0.00000
SCALE2      0.000000  0.009878  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004794        0.00000
      
PROCHECK
Go to PROCHECK summary
 References