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PDBsum entry 3fz6

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
3fz6
Jmol
Contents
Protein chains
(+ 0 more) 455 a.a.
Ligands
PMP ×6
Metals
_XE ×6
Waters ×363
HEADER    LYASE                                   23-JAN-09   3FZ6
TITLE     CRYSTAL STRUCTURE OF GLUTAMATE DECARBOXYLASE BETA FROM ESCHERICHIA
TITLE    2 COLI: COMPLEX WITH XENON
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, PMP FORM, XENON, 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 3FZ6    1       VERSN
REVDAT   1   03-FEB-09 3FZ6    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: COMPLEX WITH XENON
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.82 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) : 2.82
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.85
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8
REMARK   3   NUMBER OF REFLECTIONS             : 75035
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) : 0.138
REMARK   3   R VALUE            (WORKING SET) : 0.135
REMARK   3   FREE R VALUE                     : 0.203
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 3768
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) : 2.82
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.89
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4696
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.77
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2810
REMARK   3   BIN FREE R VALUE SET COUNT          : 261
REMARK   3   BIN FREE R VALUE                    : 0.3570
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          : 102
REMARK   3   SOLVENT ATOMS            : 363
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) : 16.76
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.02000
REMARK   3    B22 (A**2) : 0.02000
REMARK   3    B33 (A**2) : -0.03000
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): 0.328
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.219
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.017
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.909
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 22552 ; 0.015 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 30590 ; 1.646 ; 1.956
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2751 ; 6.167 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1097 ;34.944 ;23.956
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3723 ;18.873 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   152 ;19.254 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3190 ; 0.104 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 17551 ; 0.007 ; 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): 13687 ; 1.322 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 21985 ; 5.347 ;20.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  8865 ;10.736 ;20.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  8601 ; 4.908 ; 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):   3613 ; 0.260 ; 5.000
REMARK   3   TIGHT POSITIONAL   1    B    (A):   3613 ; 0.240 ; 5.000
REMARK   3   TIGHT POSITIONAL   1    C    (A):   3613 ; 0.260 ; 5.000
REMARK   3   TIGHT POSITIONAL   1    D    (A):   3613 ; 0.250 ; 5.000
REMARK   3   TIGHT POSITIONAL   1    E    (A):   3613 ; 0.390 ; 5.000
REMARK   3   TIGHT POSITIONAL   1    F    (A):   3613 ; 0.230 ; 5.000
REMARK   3   TIGHT THERMAL      1    A (A**2):   3613 ; 3.320 ;10.000
REMARK   3   TIGHT THERMAL      1    B (A**2):   3613 ; 3.290 ;10.000
REMARK   3   TIGHT THERMAL      1    C (A**2):   3613 ; 3.660 ;10.000
REMARK   3   TIGHT THERMAL      1    D (A**2):   3613 ; 3.510 ;10.000
REMARK   3   TIGHT THERMAL      1    E (A**2):   3613 ; 3.880 ;10.000
REMARK   3   TIGHT THERMAL      1    F (A**2):   3613 ; 3.110 ;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   501
REMARK   3    ORIGIN FOR THE GROUP (A):  30.3926 -17.8234  -5.6146
REMARK   3    T TENSOR
REMARK   3      T11:   0.0270 T22:   0.0288
REMARK   3      T33:   0.0582 T12:   0.0200
REMARK   3      T13:  -0.0209 T23:  -0.0381
REMARK   3    L TENSOR
REMARK   3      L11:   0.3549 L22:   0.6745
REMARK   3      L33:   0.5172 L12:  -0.0981
REMARK   3      L13:  -0.1478 L23:   0.2346
REMARK   3    S TENSOR
REMARK   3      S11:   0.0229 S12:   0.0123 S13:  -0.0163
REMARK   3      S21:  -0.0294 S22:   0.0717 S23:  -0.1365
REMARK   3      S31:   0.0590 S32:   0.0924 S33:  -0.0946
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   501
REMARK   3    ORIGIN FOR THE GROUP (A):  12.5431 -29.7796  12.6742
REMARK   3    T TENSOR
REMARK   3      T11:   0.1128 T22:   0.0172
REMARK   3      T33:   0.0319 T12:   0.0186
REMARK   3      T13:  -0.0495 T23:   0.0037
REMARK   3    L TENSOR
REMARK   3      L11:   0.5348 L22:   0.3001
REMARK   3      L33:   0.6637 L12:  -0.0138
REMARK   3      L13:   0.1612 L23:  -0.0890
REMARK   3    S TENSOR
REMARK   3      S11:   0.0570 S12:  -0.0676 S13:  -0.0945
REMARK   3      S21:   0.0889 S22:   0.0101 S23:  -0.0414
REMARK   3      S31:   0.1663 S32:   0.0470 S33:  -0.0670
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   501
REMARK   3    ORIGIN FOR THE GROUP (A): -24.8134 -14.6972 -12.5202
REMARK   3    T TENSOR
REMARK   3      T11:   0.0060 T22:   0.0231
REMARK   3      T33:   0.0024 T12:  -0.0083
REMARK   3      T13:   0.0023 T23:  -0.0020
REMARK   3    L TENSOR
REMARK   3      L11:   0.2867 L22:   0.4932
REMARK   3      L33:   0.5692 L12:  -0.0324
REMARK   3      L13:   0.0881 L23:   0.1936
REMARK   3    S TENSOR
REMARK   3      S11:   0.0258 S12:  -0.0491 S13:  -0.0063
REMARK   3      S21:   0.0398 S22:  -0.0385 S23:   0.0339
REMARK   3      S31:   0.0259 S32:  -0.1035 S33:   0.0126
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   501
REMARK   3    ORIGIN FOR THE GROUP (A): -30.5347   4.5589   8.0715
REMARK   3    T TENSOR
REMARK   3      T11:   0.0156 T22:   0.0697
REMARK   3      T33:   0.0227 T12:  -0.0185
REMARK   3      T13:   0.0183 T23:  -0.0144
REMARK   3    L TENSOR
REMARK   3      L11:   0.6703 L22:   0.5323
REMARK   3      L33:   0.4363 L12:   0.2928
REMARK   3      L13:  -0.2065 L23:   0.1481
REMARK   3    S TENSOR
REMARK   3      S11:   0.0615 S12:  -0.0253 S13:   0.0852
REMARK   3      S21:   0.0883 S22:  -0.0763 S23:   0.1065
REMARK   3      S31:   0.0299 S32:  -0.1470 S33:   0.0148
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   501
REMARK   3    RESIDUE RANGE :   E   467        E   831
REMARK   3    ORIGIN FOR THE GROUP (A):   5.3785  31.7658  -7.7922
REMARK   3    T TENSOR
REMARK   3      T11:   0.0112 T22:   0.0027
REMARK   3      T33:   0.0006 T12:  -0.0027
REMARK   3      T13:   0.0006 T23:   0.0008
REMARK   3    L TENSOR
REMARK   3      L11:   0.4961 L22:   0.4561
REMARK   3      L33:   0.4409 L12:   0.1848
REMARK   3      L13:   0.0481 L23:  -0.0594
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0121 S12:   0.0325 S13:   0.0155
REMARK   3      S21:  -0.0431 S22:   0.0149 S23:   0.0022
REMARK   3      S31:  -0.0357 S32:   0.0175 S33:  -0.0028
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   501
REMARK   3    ORIGIN FOR THE GROUP (A):  20.8084  25.2567  14.6376
REMARK   3    T TENSOR
REMARK   3      T11:   0.0072 T22:   0.0182
REMARK   3      T33:   0.0165 T12:  -0.0086
REMARK   3      T13:   0.0054 T23:  -0.0120
REMARK   3    L TENSOR
REMARK   3      L11:   0.3799 L22:   0.5897
REMARK   3      L33:   0.5112 L12:  -0.0642
REMARK   3      L13:   0.1442 L23:   0.1589
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0142 S12:  -0.0244 S13:   0.0018
REMARK   3      S21:  -0.0162 S22:   0.0585 S23:  -0.0951
REMARK   3      S31:  -0.0520 S32:   0.0738 S33:  -0.0443
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 3FZ6 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 RCSB051220.
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) : 294
REMARK 200  PH                             : 7.6
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : ELLIOTT GX-20
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54178
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   : 76681
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8
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: XENON DERIVATIVE WAS PRODUCED BY APPLYING 9 BAR XENON GAS
REMARK 200  PRESSURE TO THE CRYSTAL MOUNTED IN THE QUARTZ X-RAY CAPILLARY.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 52.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      138.94867
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       69.47433
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: 47200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 87700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -241.0 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 B   352     OE1  GLU B   435              2.03
REMARK 500   ND1  HIS C   465     O    HOH E   799              2.04
REMARK 500   NE   ARG D   402     O    HOH E   757              2.10
REMARK 500   ND1  HIS E   465     O    HOH E   804              2.11
REMARK 500   O    ASN A    59     NH2  ARG A   426              2.12
REMARK 500   OH   TYR F   352     OE1  GLU F   435              2.14
REMARK 500   O    THR B   368     NH2  ARG B   370              2.18
REMARK 500   OE2  GLU C   292     O    HOH E   534              2.19
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    LEU B 157   CA  -  CB  -  CG  ANGL. DEV. =  14.8 DEGREES
REMARK 500    ARG B 422   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES
REMARK 500    ASP C  40   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES
REMARK 500    LEU E 157   CA  -  CB  -  CG  ANGL. DEV. =  15.6 DEGREES
REMARK 500    LEU E 436   CA  -  CB  -  CG  ANGL. DEV. =  14.9 DEGREES
REMARK 500    ARG F 290   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 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    GLU A  28       42.91     72.79
REMARK 500    ALA A  56       -4.07     67.13
REMARK 500    PRO A 161       78.71    -65.03
REMARK 500    LEU A 250      -63.17   -123.13
REMARK 500    ALA A 255       57.57   -154.89
REMARK 500    ASP A 261     -144.46   -106.16
REMARK 500    LYS A 276     -114.48    -96.75
REMARK 500    LEU A 279       -1.53     82.78
REMARK 500    PHE A 317      -97.75   -124.43
REMARK 500    GLN A 459       21.33   -146.32
REMARK 500    SER B  11       43.94   -101.53
REMARK 500    GLU B  28       14.47     92.93
REMARK 500    GLN B 186       85.78   -158.22
REMARK 500    ALA B 245      -50.78    -26.18
REMARK 500    ALA B 255       62.41   -152.17
REMARK 500    TRP B 260      -12.23   -140.13
REMARK 500    ASP B 261     -150.79   -111.54
REMARK 500    LYS B 276     -123.87   -102.35
REMARK 500    LEU B 282      135.95    -38.89
REMARK 500    PHE B 317      -98.59   -112.15
REMARK 500    THR B 416       -8.86    -55.18
REMARK 500    GLN B 459       28.66   -153.72
REMARK 500    PHE B 463      118.29    -34.54
REMARK 500    GLU C  28       46.95    -81.60
REMARK 500    TYR C  90       64.16   -111.17
REMARK 500    HIS C 109       34.63     72.36
REMARK 500    PRO C 161       69.46    -68.69
REMARK 500    GLN C 186       69.42   -155.44
REMARK 500    LEU C 250      -65.01   -102.35
REMARK 500    ALA C 255       57.53   -148.00
REMARK 500    ASP C 261     -149.26   -113.37
REMARK 500    LYS C 276     -108.77    -94.31
REMARK 500    PHE C 317     -109.64   -111.40
REMARK 500    ARG C 319      145.93    172.57
REMARK 500    PRO C 376       84.56    -67.54
REMARK 500    GLN C 459       23.65   -145.41
REMARK 500    ALA D  56       -7.42     69.32
REMARK 500    LYS D 154       56.95   -119.03
REMARK 500    ALA D 255       55.29   -151.43
REMARK 500    TRP D 260      -12.73   -151.37
REMARK 500    ASP D 261     -153.60   -104.89
REMARK 500    LYS D 276     -122.36   -100.55
REMARK 500    LEU D 282      129.79    -39.79
REMARK 500    ASP D 291      172.86    179.24
REMARK 500    PHE D 317      -98.67   -106.36
REMARK 500    ALA D 415       34.70    -98.58
REMARK 500    GLN D 459       32.36   -147.16
REMARK 500    LYS E   4       23.97    -74.81
REMARK 500    ALA E  56       -0.23     71.01
REMARK 500    ASP E 261     -148.57   -115.05
REMARK 500
REMARK 500 THIS ENTRY HAS      63 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XE A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP C 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP D 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XE D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP E 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP F 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FZ7   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF APO GLUTAMATE DECARBOXYLASE BETA FROM
REMARK 900 ESCHERICHIA COLI
REMARK 900 RELATED ID: 3FZ8   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GLUTAMATE DECARBOXYLASE BETA FROM
REMARK 900 ESCHERICHIA COLI: REDUCED SCHIFF BASE WITH PLP
DBREF  3FZ6 A    1   466  UNP    P69910   DCEB_ECOLI       1    466
DBREF  3FZ6 B    1   466  UNP    P69910   DCEB_ECOLI       1    466
DBREF  3FZ6 C    1   466  UNP    P69910   DCEB_ECOLI       1    466
DBREF  3FZ6 D    1   466  UNP    P69910   DCEB_ECOLI       1    466
DBREF  3FZ6 E    1   466  UNP    P69910   DCEB_ECOLI       1    466
DBREF  3FZ6 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    PMP  A 500      16
HET     XE  A 501       1
HET    PMP  B 500      16
HET     XE  B 501       1
HET    PMP  C 500      16
HET     XE  C 501       1
HET    PMP  D 500      16
HET     XE  D 501       1
HET    PMP  E 500      16
HET     XE  E 501       1
HET    PMP  F 500      16
HET     XE  F 501       1
HETNAM     PMP 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE
HETNAM      XE XENON
HETSYN     PMP PYRIDOXAMINE-5'-PHOSPHATE
FORMUL   7  PMP    6(C8 H13 N2 O5 P)
FORMUL   8   XE    6(XE)
FORMUL  19  HOH   *363(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  CYS A  198  1                                   9
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  TYR B   51  1                                  14
HELIX   17  17 ASP B   69  ILE B   80  1                                  12
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  ARG B  402  1                                  12
HELIX   30  30 GLY B  412  THR B  416  5                                   5
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 ILE C   26  LYS C   30  5                                   5
HELIX   34  34 ARG C   38  TYR C   51  1                                  14
HELIX   35  35 ASP C   69  SER C   79  1                                  11
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  CYS C  198  1                                   9
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 GLY C  412  ASP C  417  5                                   6
HELIX   48  48 GLU C  430  HIS C  451  1                                  22
HELIX   49  49 PRO C  452  GLN C  455  5                                   4
HELIX   50  50 ARG D   38  LEU D   50  1                                  13
HELIX   51  51 TYR D   51  ASP D   53  5                                   3
HELIX   52  52 ASP D   69  SER D   79  1                                  11
HELIX   53  53 TYR D   90  TRP D  108  1                                  19
HELIX   54  54 GLY D  125  ALA D  148  1                                  24
HELIX   55  55 ILE D  164  TRP D  173  1                                  10
HELIX   56  56 ASP D  190  ALA D  197  1                                   8
HELIX   57  57 PHE D  219  GLY D  235  1                                  17
HELIX   58  58 SER D  246  PHE D  249  5                                   4
HELIX   59  59 LEU D  250  ALA D  255  1                                   6
HELIX   60  60 PRO D  296  VAL D  300  5                                   5
HELIX   61  61 ALA D  321  LYS D  359  1                                  39
HELIX   62  62 THR D  391  ARG D  402  1                                  12
HELIX   63  63 GLY D  412  THR D  416  5                                   5
HELIX   64  64 GLU D  430  HIS D  451  1                                  22
HELIX   65  65 PRO D  452  GLN D  455  5                                   4
HELIX   66  66 VAL E    6  ARG E   10  5                                   5
HELIX   67  67 ILE E   26  LYS E   30  5                                   5
HELIX   68  68 ARG E   38  LEU E   50  1                                  13
HELIX   69  69 TYR E   51  ASP E   53  5                                   3
HELIX   70  70 ASP E   69  SER E   79  1                                  11
HELIX   71  71 TYR E   90  TRP E  108  1                                  19
HELIX   72  72 GLY E  125  ALA E  148  1                                  24
HELIX   73  73 GLN E  163  TRP E  173  1                                  11
HELIX   74  74 ASP E  190  CYS E  198  1                                   9
HELIX   75  75 PHE E  219  GLY E  235  1                                  17
HELIX   76  76 SER E  246  PHE E  249  5                                   4
HELIX   77  77 LEU E  250  ALA E  255  1                                   6
HELIX   78  78 ASP E  291  LEU E  295  5                                   5
HELIX   79  79 PRO E  296  VAL E  300  5                                   5
HELIX   80  80 ALA E  321  ALA E  358  1                                  38
HELIX   81  81 THR E  391  ARG E  402  1                                  12
HELIX   82  82 GLY E  412  THR E  416  5                                   5
HELIX   83  83 GLU E  430  HIS E  451  1                                  22
HELIX   84  84 PRO E  452  GLN E  455  5                                   4
HELIX   85  85 ARG F   38  TYR F   51  1                                  14
HELIX   86  86 ASP F   69  SER F   79  1                                  11
HELIX   87  87 TYR F   90  TRP F  108  1                                  19
HELIX   88  88 GLY F  125  ALA F  148  1                                  24
HELIX   89  89 GLN F  163  ASP F  174  1                                  12
HELIX   90  90 ASP F  190  ALA F  197  1                                   8
HELIX   91  91 PHE F  219  GLY F  235  1                                  17
HELIX   92  92 SER F  246  PHE F  249  5                                   4
HELIX   93  93 LEU F  250  ALA F  255  1                                   6
HELIX   94  94 ASP F  291  LEU F  295  5                                   5
HELIX   95  95 PRO F  296  VAL F  300  5                                   5
HELIX   96  96 ALA F  321  LYS F  359  1                                  39
HELIX   97  97 THR F  391  ARG F  402  1                                  12
HELIX   98  98 GLY F  412  THR F  416  5                                   5
HELIX   99  99 GLU F  430  HIS F  451  1                                  22
HELIX  100 100 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  LYS A 381   N  GLU A 364
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  ILE C 270   O  ILE C 288
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  MET D 240   O  LYS D 268
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  ILE D 203   N  ASN D 156
SHEET    1   S 2 PHE D 301  VAL D 303  0
SHEET    2   S 2 ILE D 310  THR D 312 -1  O  ILE D 310   N  VAL D 303
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 2 LEU E  13  ASP E  15  0
SHEET    2   U 2 ALA E  20  SER E  22 -1  O  SER E  22   N  LEU E  13
SHEET    1   V 4 GLY E 120  THR E 123  0
SHEET    2   V 4 GLY E 285  TRP E 289 -1  O  GLY E 285   N  THR E 123
SHEET    3   V 4 VAL E 267  SER E 273 -1  N  ALA E 272   O  TRP E 286
SHEET    4   V 4 MET E 240  ASP E 243  1  N  MET E 240   O  LYS E 268
SHEET    1   W 3 GLU E 176  GLU E 179  0
SHEET    2   W 3 ASN E 156  CYS E 159  1  N  LEU E 157   O  ARG E 178
SHEET    3   W 3 THR E 202  VAL E 206  1  O  ILE E 203   N  ASN E 156
SHEET    1   X 2 PHE E 301  TYR E 305  0
SHEET    2   X 2 GLY E 308  THR E 312 -1  O  THR E 312   N  PHE E 301
SHEET    1   Y 4 TYR E 363  THR E 368  0
SHEET    2   Y 4 ALA E 377  LEU E 382 -1  O  LYS E 381   N  GLU E 364
SHEET    3   Y 4 VAL E 419  MET E 424 -1  O  ILE E 423   N  VAL E 378
SHEET    4   Y 4 ALA E 408  THR E 410 -1  N  PHE E 409   O  VAL E 420
SHEET    1   Z 2 LEU F  14  ASP F  15  0
SHEET    2   Z 2 ALA F  20  LYS F  21 -1  O  ALA F  20   N  ASP F  15
SHEET    1  AA 4 GLY F 120  THR F 123  0
SHEET    2  AA 4 GLY F 285  TRP F 289 -1  O  GLY F 285   N  THR F 123
SHEET    3  AA 4 VAL F 267  SER F 273 -1  N  ALA F 272   O  TRP F 286
SHEET    4  AA 4 MET F 240  ASP F 243  1  N  MET F 240   O  LYS F 268
SHEET    1  AB 3 GLU F 176  GLU F 179  0
SHEET    2  AB 3 ASN F 156  CYS F 159  1  N  LEU F 157   O  ARG F 178
SHEET    3  AB 3 THR F 202  VAL F 206  1  O  ILE F 203   N  ASN F 156
SHEET    1  AC 2 PHE F 301  TYR F 305  0
SHEET    2  AC 2 GLY F 308  THR F 312 -1  O  THR F 312   N  PHE F 301
SHEET    1  AD 4 TYR F 363  THR F 368  0
SHEET    2  AD 4 ALA F 377  LEU F 382 -1  O  CYS F 379   N  ILE F 366
SHEET    3  AD 4 VAL F 419  MET F 424 -1  O  ILE F 423   N  VAL F 378
SHEET    4  AD 4 ALA F 408  THR F 410 -1  N  PHE F 409   O  VAL F 420
SITE     1 AC1 15 SER A 126  SER A 127  GLN A 163  GLY A 210
SITE     2 AC1 15 THR A 212  ASP A 243  ALA A 245  SER A 273
SITE     3 AC1 15 HIS A 275  LYS A 276  HIS A 465  THR A 466
SITE     4 AC1 15 PHE B 317  SER B 318  HOH E 519
SITE     1 AC2  1 GLY A 120
SITE     1 AC3 14 PHE A 317  SER A 318  SER B 126  SER B 127
SITE     2 AC3 14 GLN B 163  THR B 208  THR B 212  ASP B 243
SITE     3 AC3 14 ALA B 245  SER B 273  HIS B 275  LYS B 276
SITE     4 AC3 14 HIS B 465  THR B 466
SITE     1 AC4 17 GLY C 125  SER C 126  SER C 127  GLN C 163
SITE     2 AC4 17 CYS C 165  THR C 208  THR C 212  ASP C 243
SITE     3 AC4 17 ALA C 245  SER C 273  HIS C 275  LYS C 276
SITE     4 AC4 17 HIS C 465  THR C 466  PHE D 317  SER D 318
SITE     5 AC4 17 HOH E 515
SITE     1 AC5 14 PHE C 317  SER C 318  SER D 126  SER D 127
SITE     2 AC5 14 GLN D 163  THR D 208  THR D 212  ASP D 243
SITE     3 AC5 14 ALA D 245  SER D 273  HIS D 275  LYS D 276
SITE     4 AC5 14 HIS D 465  THR D 466
SITE     1 AC6  1 GLY D 120
SITE     1 AC7 14 SER E 126  SER E 127  GLN E 163  THR E 208
SITE     2 AC7 14 THR E 212  ASP E 243  ALA E 245  SER E 273
SITE     3 AC7 14 HIS E 275  LYS E 276  HIS E 465  THR E 466
SITE     4 AC7 14 PHE F 317  SER F 318
SITE     1 AC8 15 PHE E 317  SER E 318  HOH E 467  GLY F 125
SITE     2 AC8 15 SER F 126  SER F 127  GLN F 163  THR F 212
SITE     3 AC8 15 ASP F 243  ALA F 245  SER F 273  HIS F 275
SITE     4 AC8 15 LYS F 276  HIS F 465  THR F 466
CRYST1  116.729  116.729  208.423  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      0.008567  0.004946  0.000000        0.00000
SCALE2      0.000000  0.009892  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004798        0.00000
      
PROCHECK
Go to PROCHECK summary
 References