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PDBsum entry 3s42

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
3s42
Jmol
Contents
Protein chains
260 a.a.
Ligands
MLA ×2
DMS ×6
IMD
BO3
Metals
_NI
Waters ×599
HEADER    LYASE                                   18-MAY-11   3S42
TITLE     CRYSTAL STRUCTURE OF THE 3-DEHYDROQUINATE DEHYDRATASE (AROD) FROM
TITLE    2 SALMONELLA ENTERICA TYPHIMURIUM LT2 WITH MALONATE AND BORIC ACID AT
TITLE    3 THE ACTIVE SITE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: 3-DEHYDROQUINATE DEHYDRATASE;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: 3-DEHYDROQUINASE, TYPE I DHQASE;
COMPND   5 EC: 4.2.1.10;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR
SOURCE   3 TYPHIMURIUM;
SOURCE   4 ORGANISM_TAXID: 90371;
SOURCE   5 STRAIN: LT2;
SOURCE   6 GENE: AROD, STM1358;
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: MCSG7
KEYWDS    STRUCTURAL GENOMICS, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS
KEYWDS   2 DISEASES, CSGID, TIM BARREL, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.H.LIGHT,G.MINASOV,M-E.DUBAN,A.S.HALAVATY,S.N.KRISHNA,L.SHUVALOVA,
AUTHOR   2 K.KWON,W.F.ANDERSON,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS
AUTHOR   3 DISEASES (CSGID)
REVDAT   1   01-JUN-11 3S42    0
JRNL        AUTH   S.H.LIGHT,G.MINASOV,M-E.DUBAN,A.S.HALAVATY,S.N.KRISHNA,
JRNL        AUTH 2 L.SHUVALOVA,K.KWON,W.F.ANDERSON,
JRNL        AUTH 3 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
JRNL        AUTH 4 (CSGID)
JRNL        TITL   CRYSTAL STRUCTURE OF THE 3-DEHYDROQUINATE DEHYDRATASE (AROD)
JRNL        TITL 2 FROM SALMONELLA ENTERICA TYPHIMURIUM LT2 WITH MALONATE AND
JRNL        TITL 3 BORIC ACID AT THE ACTIVE SITE
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    1.45 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0109
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) : 1.45
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.56
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6
REMARK   3   NUMBER OF REFLECTIONS             : 77604
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) : 0.145
REMARK   3   R VALUE            (WORKING SET) : 0.144
REMARK   3   FREE R VALUE                     : 0.175
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 4091
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) : 1.45
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.49
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5399
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.02
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1790
REMARK   3   BIN FREE R VALUE SET COUNT          : 289
REMARK   3   BIN FREE R VALUE                    : 0.2010
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4026
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 48
REMARK   3   SOLVENT ATOMS            : 563
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.75
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.50000
REMARK   3    B22 (A**2) : 1.49000
REMARK   3    B33 (A**2) : -0.99000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.065
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.067
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.037
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.035
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.972
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.960
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4759 ; 0.025 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  3119 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6494 ; 2.200 ; 1.963
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7704 ; 1.056 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   643 ; 3.612 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   200 ;37.531 ;24.650
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   857 ;10.533 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    29 ;16.884 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   764 ; 0.134 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5486 ; 0.011 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):   927 ; 0.002 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3026 ; 1.494 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1220 ; 0.550 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4943 ; 2.293 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1733 ; 3.397 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1545 ; 5.225 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 8
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    -7        A    44
REMARK   3    ORIGIN FOR THE GROUP (A):   7.1237   9.3073   5.3344
REMARK   3    T TENSOR
REMARK   3      T11:   0.0184 T22:   0.0160
REMARK   3      T33:   0.0379 T12:  -0.0011
REMARK   3      T13:  -0.0003 T23:  -0.0084
REMARK   3    L TENSOR
REMARK   3      L11:   0.5054 L22:   0.4458
REMARK   3      L33:   0.5066 L12:   0.1563
REMARK   3      L13:   0.2338 L23:   0.0601
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0423 S12:   0.0374 S13:   0.0693
REMARK   3      S21:  -0.0227 S22:  -0.0107 S23:   0.0299
REMARK   3      S31:  -0.0789 S32:  -0.0079 S33:   0.0530
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    45        A   102
REMARK   3    ORIGIN FOR THE GROUP (A):  17.0242   4.5535  14.4212
REMARK   3    T TENSOR
REMARK   3      T11:   0.0064 T22:   0.0326
REMARK   3      T33:   0.0278 T12:  -0.0023
REMARK   3      T13:  -0.0008 T23:  -0.0069
REMARK   3    L TENSOR
REMARK   3      L11:   0.8298 L22:   1.2801
REMARK   3      L33:   0.9283 L12:  -0.1858
REMARK   3      L13:   0.0057 L23:   0.1241
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0318 S12:  -0.0772 S13:   0.0063
REMARK   3      S21:   0.0605 S22:   0.0521 S23:  -0.0234
REMARK   3      S31:  -0.0287 S32:   0.0703 S33:  -0.0204
REMARK   3
REMARK   3   TLS GROUP : 3
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   103        A   208
REMARK   3    ORIGIN FOR THE GROUP (A):   9.7103  -8.1138   2.4793
REMARK   3    T TENSOR
REMARK   3      T11:   0.0077 T22:   0.0002
REMARK   3      T33:   0.0235 T12:   0.0008
REMARK   3      T13:  -0.0002 T23:  -0.0006
REMARK   3    L TENSOR
REMARK   3      L11:   0.3575 L22:   0.3304
REMARK   3      L33:   0.8425 L12:  -0.1005
REMARK   3      L13:  -0.1453 L23:   0.1741
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0051 S12:  -0.0018 S13:  -0.0095
REMARK   3      S21:   0.0273 S22:   0.0013 S23:  -0.0063
REMARK   3      S31:   0.0737 S32:   0.0083 S33:   0.0038
REMARK   3
REMARK   3   TLS GROUP : 4
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   209        A   252
REMARK   3    ORIGIN FOR THE GROUP (A):  10.9607   6.3723  -8.3592
REMARK   3    T TENSOR
REMARK   3      T11:   0.0254 T22:   0.0091
REMARK   3      T33:   0.0360 T12:   0.0093
REMARK   3      T13:   0.0049 T23:  -0.0020
REMARK   3    L TENSOR
REMARK   3      L11:   0.7445 L22:   1.6782
REMARK   3      L33:   1.3908 L12:   0.2750
REMARK   3      L13:   0.0828 L23:  -0.2388
REMARK   3    S TENSOR
REMARK   3      S11:   0.0384 S12:   0.0424 S13:   0.0298
REMARK   3      S21:  -0.0232 S22:  -0.0417 S23:  -0.0898
REMARK   3      S31:  -0.0377 S32:   0.0409 S33:   0.0033
REMARK   3
REMARK   3   TLS GROUP : 5
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   -23        B    47
REMARK   3    ORIGIN FOR THE GROUP (A):  12.1291   7.0148 -41.4054
REMARK   3    T TENSOR
REMARK   3      T11:   0.0945 T22:   0.0741
REMARK   3      T33:   0.0926 T12:  -0.0001
REMARK   3      T13:   0.0145 T23:   0.0015
REMARK   3    L TENSOR
REMARK   3      L11:   0.5948 L22:   0.2398
REMARK   3      L33:   0.9165 L12:   0.1765
REMARK   3      L13:   0.2125 L23:  -0.2469
REMARK   3    S TENSOR
REMARK   3      S11:   0.0221 S12:  -0.0515 S13:   0.1081
REMARK   3      S21:   0.0466 S22:  -0.0274 S23:   0.0054
REMARK   3      S31:  -0.1077 S32:   0.1155 S33:   0.0053
REMARK   3
REMARK   3   TLS GROUP : 6
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B    48        B    91
REMARK   3    ORIGIN FOR THE GROUP (A):   1.6531   5.4063 -46.3481
REMARK   3    T TENSOR
REMARK   3      T11:   0.0287 T22:   0.0476
REMARK   3      T33:   0.0276 T12:   0.0281
REMARK   3      T13:   0.0175 T23:   0.0149
REMARK   3    L TENSOR
REMARK   3      L11:   1.6481 L22:   0.9057
REMARK   3      L33:   1.2228 L12:  -0.1401
REMARK   3      L13:   0.3445 L23:  -0.1212
REMARK   3    S TENSOR
REMARK   3      S11:   0.0330 S12:   0.1544 S13:   0.0611
REMARK   3      S21:   0.0104 S22:  -0.0007 S23:   0.0574
REMARK   3      S31:  -0.0506 S32:  -0.0932 S33:  -0.0323
REMARK   3
REMARK   3   TLS GROUP : 7
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B    92        B   228
REMARK   3    ORIGIN FOR THE GROUP (A):   8.3455  -6.9902 -35.3454
REMARK   3    T TENSOR
REMARK   3      T11:   0.0187 T22:   0.0053
REMARK   3      T33:   0.0125 T12:  -0.0055
REMARK   3      T13:  -0.0022 T23:   0.0030
REMARK   3    L TENSOR
REMARK   3      L11:   0.4249 L22:   0.1765
REMARK   3      L33:   1.4781 L12:  -0.0057
REMARK   3      L13:  -0.0151 L23:  -0.1843
REMARK   3    S TENSOR
REMARK   3      S11:   0.0342 S12:  -0.0366 S13:  -0.0249
REMARK   3      S21:  -0.0290 S22:  -0.0035 S23:  -0.0099
REMARK   3      S31:   0.1283 S32:  -0.0040 S33:  -0.0307
REMARK   3
REMARK   3   TLS GROUP : 8
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   229        B   252
REMARK   3    ORIGIN FOR THE GROUP (A):   7.2843   9.5866 -24.4425
REMARK   3    T TENSOR
REMARK   3      T11:   0.0674 T22:   0.0254
REMARK   3      T33:   0.0385 T12:   0.0114
REMARK   3      T13:   0.0145 T23:  -0.0088
REMARK   3    L TENSOR
REMARK   3      L11:   2.6359 L22:   1.5102
REMARK   3      L33:   3.5379 L12:   0.4220
REMARK   3      L13:   1.3772 L23:   0.1932
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0869 S12:   0.0043 S13:  -0.0535
REMARK   3      S21:  -0.0666 S22:   0.0959 S23:   0.0611
REMARK   3      S31:  -0.3686 S32:  -0.0631 S33:  -0.0089
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3S42 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAY-11.
REMARK 100 THE RCSB ID CODE IS RCSB065734.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 21-APR-11
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 21-ID-G
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97856
REMARK 200  MONOCHROMATOR                  : DIAMOND
REMARK 200  OPTICS                         : BERYLLIUM LENS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 81850
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.450
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6
REMARK 200  DATA REDUNDANCY                : 5.600
REMARK 200  R MERGE                    (I) : 0.06800
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 20.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.48
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40
REMARK 200  R MERGE FOR SHELL          (I) : 0.27600
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 4.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3L20
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 34.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5 M SODIUM CHLORIDE,     0.010 M
REMARK 280  TRIS-HCL, QIAGEN PACT B2, 0.1 M MIB BUFFER (CONTAINING 0.025 M
REMARK 280  SODIUM MALONATE, 0.037 M BORIC ACID, 0.025 M IMIDAZOLE), 25% (W/
REMARK 280  V) PEG 1500, PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280  300K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       18.28100
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       85.67650
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.28450
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       85.67650
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       18.28100
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.28450
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 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     HIS B   -17
REMARK 465     SER B   -16
REMARK 465     SER B   -15
REMARK 465     GLY B   -14
REMARK 465     VAL B   -13
REMARK 465     ASP B   -12
REMARK 465     LEU B   -11
REMARK 465     GLY B   -10
REMARK 465     THR B    -9
REMARK 465     GLU B    -8
REMARK 465     MET A   -23
REMARK 465     HIS A   -22
REMARK 465     HIS A   -21
REMARK 465     HIS A   -20
REMARK 465     HIS A   -19
REMARK 465     HIS A   -18
REMARK 465     HIS A   -17
REMARK 465     SER A   -16
REMARK 465     SER A   -15
REMARK 465     GLY A   -14
REMARK 465     VAL A   -13
REMARK 465     ASP A   -12
REMARK 465     LEU A   -11
REMARK 465     GLY A   -10
REMARK 465     THR A    -9
REMARK 465     GLU A    -8
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    GLN B 162   CB    GLN B 162   CG     -0.180
REMARK 500    GLU A 163   CG    GLU A 163   CD      0.099
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 B  85   CB  -  CA  -  C   ANGL. DEV. = -13.9 DEGREES
REMARK 500    GLU B  89   N   -  CA  -  C   ANGL. DEV. =  18.5 DEGREES
REMARK 500    ASP B 121   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES
REMARK 500    ARG B 157   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES
REMARK 500    ARG B 157   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    ARG A 157   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ARG A 157   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES
REMARK 500    ARG A 243   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 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    ASP B   8       -1.06     68.00
REMARK 500    ASN B  54       47.91    -97.45
REMARK 500    SER B 206      167.33     77.13
REMARK 500    ASN A  54       48.35   -102.85
REMARK 500    SER A 206      167.33     75.94
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    PHE B 219        25.0      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NI B 589  NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B -22   NE2
REMARK 620 2 IMD B 253   N1  177.1
REMARK 620 3 HIS B 134   NE2  89.8  91.6
REMARK 620 4 HIS B -20   NE2  90.0  92.5  91.9
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLA B 583
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 591
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 592
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 593
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 594
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 589
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD B 253
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLA A 586
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 590
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 595
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO3 A 253
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3L2I   RELATED DB: PDB
REMARK 900 STRUCTURE OF UNLIGANDED ENZYME
REMARK 900 RELATED ID: 3LB0   RELATED DB: PDB
REMARK 900 STRUCTURE OF ENZYME WITH CITRATE BOUND AT ACTIVE SITE
REMARK 900 RELATED ID: 3OEX   RELATED DB: PDB
REMARK 900 STRUCTURE OF ENZYME WITH CHLORIDE BOUND AT ACTIVE SITE
REMARK 900 RELATED ID: 3NNT   RELATED DB: PDB
REMARK 900 STRUCTURE OF THE K170M MUTANT IN NON-COVALENT COMPLEX WITH
REMARK 900 SUBSTRATE
REMARK 900 RELATED ID: 3M7W   RELATED DB: PDB
REMARK 900 STRUCTURE OF ENZYME IN COVALENT COMPLEX WITH SUBSTRATE
REMARK 900 RELATED ID: IDP90922   RELATED DB: TARGETDB
DBREF  3S42 B    1   252  UNP    P58687   AROD_SALTY       1    252
DBREF  3S42 A    1   252  UNP    P58687   AROD_SALTY       1    252
SEQADV 3S42 MET B  -23  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 HIS B  -22  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 HIS B  -21  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 HIS B  -20  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 HIS B  -19  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 HIS B  -18  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 HIS B  -17  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 SER B  -16  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 SER B  -15  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 GLY B  -14  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 VAL B  -13  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 ASP B  -12  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 LEU B  -11  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 GLY B  -10  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 THR B   -9  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 GLU B   -8  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 ASN B   -7  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 LEU B   -6  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 TYR B   -5  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 PHE B   -4  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 GLN B   -3  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 SER B   -2  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 ASN B   -1  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 ALA B    0  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 MET A  -23  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 HIS A  -22  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 HIS A  -21  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 HIS A  -20  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 HIS A  -19  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 HIS A  -18  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 HIS A  -17  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 SER A  -16  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 SER A  -15  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 GLY A  -14  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 VAL A  -13  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 ASP A  -12  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 LEU A  -11  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 GLY A  -10  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 THR A   -9  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 GLU A   -8  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 ASN A   -7  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 LEU A   -6  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 TYR A   -5  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 PHE A   -4  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 GLN A   -3  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 SER A   -2  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 ASN A   -1  UNP  P58687              EXPRESSION TAG
SEQADV 3S42 ALA A    0  UNP  P58687              EXPRESSION TAG
SEQRES   1 A  276  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES   2 A  276  GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET LYS
SEQRES   3 A  276  THR VAL THR VAL ARG ASP LEU VAL VAL GLY GLU GLY ALA
SEQRES   4 A  276  PRO LYS ILE ILE VAL SER LEU MET GLY LYS THR ILE THR
SEQRES   5 A  276  ASP VAL LYS SER GLU ALA LEU ALA TYR ARG GLU ALA ASP
SEQRES   6 A  276  PHE ASP ILE LEU GLU TRP ARG VAL ASP HIS PHE ALA ASN
SEQRES   7 A  276  VAL THR THR ALA GLU SER VAL LEU GLU ALA ALA GLY ALA
SEQRES   8 A  276  ILE ARG GLU ILE ILE THR ASP LYS PRO LEU LEU PHE THR
SEQRES   9 A  276  PHE ARG SER ALA LYS GLU GLY GLY GLU GLN ALA LEU THR
SEQRES  10 A  276  THR GLY GLN TYR ILE ASP LEU ASN ARG ALA ALA VAL ASP
SEQRES  11 A  276  SER GLY LEU VAL ASP MET ILE ASP LEU GLU LEU PHE THR
SEQRES  12 A  276  GLY ASP ASP GLU VAL LYS ALA THR VAL GLY TYR ALA HIS
SEQRES  13 A  276  GLN HIS ASN VAL ALA VAL ILE MET SER ASN HIS ASP PHE
SEQRES  14 A  276  HIS LYS THR PRO ALA ALA GLU GLU ILE VAL GLN ARG LEU
SEQRES  15 A  276  ARG LYS MET GLN GLU LEU GLY ALA ASP ILE PRO LYS ILE
SEQRES  16 A  276  ALA VAL MET PRO GLN THR LYS ALA ASP VAL LEU THR LEU
SEQRES  17 A  276  LEU THR ALA THR VAL GLU MET GLN GLU ARG TYR ALA ASP
SEQRES  18 A  276  ARG PRO ILE ILE THR MET SER MET SER LYS THR GLY VAL
SEQRES  19 A  276  ILE SER ARG LEU ALA GLY GLU VAL PHE GLY SER ALA ALA
SEQRES  20 A  276  THR PHE GLY ALA VAL LYS LYS ALA SER ALA PRO GLY GLN
SEQRES  21 A  276  ILE SER VAL ALA ASP LEU ARG THR VAL LEU THR ILE LEU
SEQRES  22 A  276  HIS GLN ALA
SEQRES   1 B  276  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES   2 B  276  GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET LYS
SEQRES   3 B  276  THR VAL THR VAL ARG ASP LEU VAL VAL GLY GLU GLY ALA
SEQRES   4 B  276  PRO LYS ILE ILE VAL SER LEU MET GLY LYS THR ILE THR
SEQRES   5 B  276  ASP VAL LYS SER GLU ALA LEU ALA TYR ARG GLU ALA ASP
SEQRES   6 B  276  PHE ASP ILE LEU GLU TRP ARG VAL ASP HIS PHE ALA ASN
SEQRES   7 B  276  VAL THR THR ALA GLU SER VAL LEU GLU ALA ALA GLY ALA
SEQRES   8 B  276  ILE ARG GLU ILE ILE THR ASP LYS PRO LEU LEU PHE THR
SEQRES   9 B  276  PHE ARG SER ALA LYS GLU GLY GLY GLU GLN ALA LEU THR
SEQRES  10 B  276  THR GLY GLN TYR ILE ASP LEU ASN ARG ALA ALA VAL ASP
SEQRES  11 B  276  SER GLY LEU VAL ASP MET ILE ASP LEU GLU LEU PHE THR
SEQRES  12 B  276  GLY ASP ASP GLU VAL LYS ALA THR VAL GLY TYR ALA HIS
SEQRES  13 B  276  GLN HIS ASN VAL ALA VAL ILE MET SER ASN HIS ASP PHE
SEQRES  14 B  276  HIS LYS THR PRO ALA ALA GLU GLU ILE VAL GLN ARG LEU
SEQRES  15 B  276  ARG LYS MET GLN GLU LEU GLY ALA ASP ILE PRO LYS ILE
SEQRES  16 B  276  ALA VAL MET PRO GLN THR LYS ALA ASP VAL LEU THR LEU
SEQRES  17 B  276  LEU THR ALA THR VAL GLU MET GLN GLU ARG TYR ALA ASP
SEQRES  18 B  276  ARG PRO ILE ILE THR MET SER MET SER LYS THR GLY VAL
SEQRES  19 B  276  ILE SER ARG LEU ALA GLY GLU VAL PHE GLY SER ALA ALA
SEQRES  20 B  276  THR PHE GLY ALA VAL LYS LYS ALA SER ALA PRO GLY GLN
SEQRES  21 B  276  ILE SER VAL ALA ASP LEU ARG THR VAL LEU THR ILE LEU
SEQRES  22 B  276  HIS GLN ALA
HET    MLA  B 583       7
HET    DMS  A 592       4
HET    DMS  B 591       4
HET    DMS  B 593       4
HET    DMS  B 594       4
HET     NI  B 589       1
HET    IMD  B 253       5
HET    MLA  A 586       7
HET    DMS  A 590       4
HET    DMS  A 595       4
HET    BO3  A 253       4
HETNAM     MLA MALONIC ACID
HETNAM     DMS DIMETHYL SULFOXIDE
HETNAM      NI NICKEL (II) ION
HETNAM     IMD IMIDAZOLE
HETNAM     BO3 BORIC ACID
HETSYN     MLA DICARBOXYLIC ACID C3; PROPANEDIOLIC ACID;
HETSYN   2 MLA  METAHNEDICARBOXYLIC ACID
FORMUL   3  MLA    2(C3 H4 O4)
FORMUL   4  DMS    6(C2 H6 O S)
FORMUL   8   NI    NI 2+
FORMUL   9  IMD    C3 H5 N2 1+
FORMUL  13  BO3    B H3 O3
FORMUL  14  HOH   *563(H2 O)
HELIX    1  12 THR B   26  GLU B   39  1                                  14
HELIX    2  13 ASP B   50  PHE B   52  5                                   3
HELIX    3  14 THR B   57  ILE B   72  1                                  16
HELIX    4  15 SER B   83  GLY B   87  5                                   5
HELIX    5  16 THR B   93  GLY B  108  1                                  16
HELIX    6  17 GLY B  120  HIS B  134  1                                  15
HELIX    7  18 ALA B  150  LEU B  164  1                                  15
HELIX    8  19 THR B  177  TYR B  195  1                                  19
HELIX    9  20 SER B  206  GLY B  209  5                                   4
HELIX   10  21 VAL B  210  ALA B  215  1                                   6
HELIX   11  22 ALA B  215  GLY B  220  1                                   6
HELIX   12  23 SER B  238  GLN B  251  1                                  14
HELIX   13   1 THR A   26  ARG A   38  1                                  13
HELIX   14   2 ASP A   50  PHE A   52  5                                   3
HELIX   15   3 THR A   57  ILE A   72  1                                  16
HELIX   16   4 SER A   83  GLY A   87  5                                   5
HELIX   17   5 THR A   93  GLY A  108  1                                  16
HELIX   18   6 GLY A  120  HIS A  134  1                                  15
HELIX   19   7 ALA A  150  LEU A  164  1                                  15
HELIX   20   8 THR A  177  TYR A  195  1                                  19
HELIX   21   9 SER A  206  LEU A  214  5                                   9
HELIX   22  10 ALA A  215  GLY A  220  1                                   6
HELIX   23  11 SER A  238  ALA A  252  1                                  15
SHEET    1   A 3 PHE A  -4  SER A  -2  0
SHEET    2   A 3 THR A   3  VAL A   6 -1  O  THR A   3   N  SER A  -2
SHEET    3   A 3 LEU A   9  VAL A  11 -1  O  VAL A  11   N  VAL A   4
SHEET    1   B 8 ILE A 201  SER A 204  0
SHEET    2   B 8 ILE A 168  VAL A 173  1  N  PRO A 169   O  ILE A 201
SHEET    3   B 8 ALA A 137  ASP A 144  1  N  ASP A 144   O  ALA A 172
SHEET    4   B 8 MET A 112  GLU A 116  1  N  ILE A 113   O  ILE A 139
SHEET    5   B 8 LEU A  77  THR A  80  1  N  PHE A  79   O  MET A 112
SHEET    6   B 8 ILE A  44  ARG A  48  1  N  TRP A  47   O  LEU A  78
SHEET    7   B 8 LYS A  17  LEU A  22  1  N  LEU A  22   O  GLU A  46
SHEET    8   B 8 ALA A 223  PHE A 225  1  O  THR A 224   N  ILE A  19
SHEET    1   C 3 TYR B  -5  SER B  -2  0
SHEET    2   C 3 THR B   3  VAL B   6 -1  O  THR B   5   N  PHE B  -4
SHEET    3   C 3 LEU B   9  VAL B  11 -1  O  VAL B  11   N  VAL B   4
SHEET    1   D 8 ILE B 201  SER B 204  0
SHEET    2   D 8 ILE B 168  VAL B 173  1  N  PRO B 169   O  ILE B 201
SHEET    3   D 8 ALA B 137  ASP B 144  1  N  ASP B 144   O  ALA B 172
SHEET    4   D 8 MET B 112  GLU B 116  1  N  ILE B 113   O  ILE B 139
SHEET    5   D 8 LEU B  77  THR B  80  1  N  PHE B  79   O  MET B 112
SHEET    6   D 8 ILE B  44  ARG B  48  1  N  LEU B  45   O  LEU B  78
SHEET    7   D 8 LYS B  17  LEU B  22  1  N  VAL B  20   O  GLU B  46
SHEET    8   D 8 ALA B 223  PHE B 225  1  O  THR B 224   N  LYS B  17
LINK         NE2 HIS B -22                NI    NI B 589     1555   1555  2.09
LINK        NI    NI B 589                 N1  IMD B 253     1555   1555  2.09
LINK         NE2 HIS B 134                NI    NI B 589     1555   1555  2.10
LINK         NE2 HIS B -20                NI    NI B 589     1555   1555  2.10
SITE     1 AC1 10 HIS B 143  LYS B 170  ALA B 172  MET B 203
SITE     2 AC1 10 MET B 205  ARG B 213  PHE B 225  ALA B 233
SITE     3 AC1 10 GLN B 236  HOH B 409
SITE     1 AC2  7 LYS A 207  VAL A 210  HOH A 348  VAL B 218
SITE     2 AC2  7 LEU B 249  ALA B 252  HOH B 308
SITE     1 AC3  6 GLU A 217  VAL A 218  LEU A 249  HOH A 277
SITE     2 AC3  6 HOH A 300  LYS B 207
SITE     1 AC4  9 SER B  83  ALA B  84  LEU B  92  TYR B  97
SITE     2 AC4  9 GLU B 116  HOH B 378  HOH B 398  HOH B 455
SITE     3 AC4  9 HOH B 474
SITE     1 AC5  7 ASN B  -1  ALA B   0  LYS B  85  HIS B 143
SITE     2 AC5  7 ASP B 144  PHE B 145  HIS B 146
SITE     1 AC6  6 HIS A 134  HOH A 547  HIS B -22  HIS B -20
SITE     2 AC6  6 HIS B 134  IMD B 253
SITE     1 AC7  8 GLN A 133  HIS A 134  HOH A 547  HIS B -20
SITE     2 AC7  8 ASP B 106  HIS B 134  HOH B 466   NI B 589
SITE     1 AC8 10 HIS A 143  LYS A 170  ALA A 172  MET A 203
SITE     2 AC8 10 MET A 205  ARG A 213  PHE A 225  ALA A 233
SITE     3 AC8 10 GLN A 236  BO3 A 253
SITE     1 AC9  7 SER A  83  ALA A  84  ALA A  91  LEU A  92
SITE     2 AC9  7 TYR A  97  GLU A 116  HOH A 520
SITE     1 BC1  7 LYS A   2  HIS A 146  GLN A 156  GLU A 193
SITE     2 BC1  7 ARG A 194  TYR A 195  ALA A 196
SITE     1 BC2  9 SER A  21  GLU A  46  ARG A  48  ARG A  82
SITE     2 BC2  9 LYS A 170  HOH A 307  HOH A 374  HOH A 404
SITE     3 BC2  9 MLA A 586
CRYST1   36.562   72.569  171.353  90.00  90.00  90.00 P 21 21 21    8
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.027351  0.000000  0.000000        0.00000
SCALE2      0.000000  0.013780  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005836        0.00000
      
PROCHECK
Go to PROCHECK summary
 References