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PDBsum entry 3ctq

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Transferase PDB id
3ctq
Jmol
Contents
Protein chain
336 a.a.
Ligands
337
Waters ×143
HEADER    TRANSFERASE                             14-APR-08   3CTQ
TITLE     STRUCTURE OF MAP KINASE P38 IN COMPLEX WITH A 1-O-TOLYL-1,2,
TITLE    2 3-TRIAZOLE-4-CARBOXAMIDE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 14;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: MITOGEN-ACTIVATED PROTEIN KINASE P38 ALPHA, MAP
COMPND   5 KINASE P38 ALPHA, CYTOKINE SUPPRESSIVE ANTI-INFLAMMATORY
COMPND   6 DRUG-BINDING PROTEIN, CSAID-BINDING PROTEIN, CSBP, MAX-
COMPND   7 INTERACTING PROTEIN 2, MAP KINASE MXI2, SAPK2A;
COMPND   8 EC: 2.7.11.24;
COMPND   9 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: MAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: MAPK14, CSBP, CSBP1, CSBP2, CSPB1, MXI2;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI
KEYWDS    TWO LOBE KINASE FOLD, N-TERMINAL BETA-SHEET, C-TERMINAL
KEYWDS   2 ALPHA-HELIX, ALTERNATIVE SPLICING, ATP-BINDING, CYTOPLASM,
KEYWDS   3 KINASE, NUCLEOTIDE-BINDING, NUCLEUS, PHOSPHOPROTEIN,
KEYWDS   4 POLYMORPHISM, SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.QIAN
REVDAT   3   24-FEB-09 3CTQ    1       VERSN
REVDAT   2   17-JUN-08 3CTQ    1       JRNL
REVDAT   1   27-MAY-08 3CTQ    0
JRNL        AUTH   D.A.COGAN,R.AUNGST,E.C.BREINLINGER,T.FADRA,
JRNL        AUTH 2 D.R.GOLDBERG,M.H.HAO,R.KROE,N.MOSS,C.PARGELLIS,
JRNL        AUTH 3 K.C.QIAN,A.D.SWINAMER
JRNL        TITL   STRUCTURE-BASED DESIGN AND SUBSEQUENT OPTIMIZATION
JRNL        TITL 2 OF 2-TOLYL-(1,2,3-TRIAZOL-1-YL-4-CARBOXAMIDE)
JRNL        TITL 3 INHIBITORS OF P38 MAP KINASE.
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  18  3251 2008
JRNL        REFN                   ISSN 0960-894X
JRNL        PMID   18462940
JRNL        DOI    10.1016/J.BMCL.2008.04.043
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 88.0
REMARK   3   NUMBER OF REFLECTIONS             : 23633
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.230
REMARK   3   FREE R VALUE                     : 0.269
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.700
REMARK   3   FREE R VALUE TEST SET COUNT      : 2337
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2705
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 42
REMARK   3   SOLVENT ATOMS            : 143
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.99
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.01300
REMARK   3    B22 (A**2) : 0.05500
REMARK   3    B33 (A**2) : -0.04200
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 COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.492 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.420 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.102 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.953 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  4  : ION.PARAM
REMARK   3  PARAMETER FILE  5  : BIRB2371.PAR
REMARK   3  PARAMETER FILE  6  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3  TOPOLOGY FILE  5   : NULL
REMARK   3  TOPOLOGY FILE  6   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3CTQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAY-08.
REMARK 100 THE RCSB ID CODE IS RCSB047198.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
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          : RIGAKU RU300
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24353
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.0
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) : 1.95
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 50.00
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.0
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 45.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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       32.72500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.07000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.94500
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       37.07000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.72500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.94500
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 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     LEU A   171
REMARK 465     ALA A   172
REMARK 465     ARG A   173
REMARK 465     HIS A   174
REMARK 465     THR A   175
REMARK 465     ASP A   176
REMARK 465     ASP A   177
REMARK 465     GLU A   178
REMARK 465     MET A   179
REMARK 465     THR A   180
REMARK 465     GLY A   181
REMARK 465     TYR A   182
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ALA A  14      -97.33     68.49
REMARK 500    SER A  56     -101.04    -45.94
REMARK 500    ARG A  57       66.50   -114.66
REMARK 500    PHE A  99      105.23    -59.01
REMARK 500    CYS A 119     -114.10    -75.89
REMARK 500    ARG A 149       -7.58     77.14
REMARK 500    ASP A 150       40.47   -144.89
REMARK 500    MET A 198      100.01     36.10
REMARK 500    HIS A 199       28.96    148.20
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 337 A 1
DBREF  3CTQ A    5   352  UNP    Q16539   MK14_HUMAN       5    352
SEQADV 3CTQ ALA A   14  UNP  Q16539    ASN    14 CONFLICT
SEQADV 3CTQ HIS A   48  UNP  Q16539    LEU    48 CONFLICT
SEQADV 3CTQ ALA A  120  UNP  Q16539    GLN   120 CONFLICT
SEQADV 3CTQ ALA A  263  UNP  Q16539    THR   263 CONFLICT
SEQRES   1 A  348  ARG PRO THR PHE TYR ARG GLN GLU LEU ALA LYS THR ILE
SEQRES   2 A  348  TRP GLU VAL PRO GLU ARG TYR GLN ASN LEU SER PRO VAL
SEQRES   3 A  348  GLY SER GLY ALA TYR GLY SER VAL CYS ALA ALA PHE ASP
SEQRES   4 A  348  THR LYS THR GLY HIS ARG VAL ALA VAL LYS LYS LEU SER
SEQRES   5 A  348  ARG PRO PHE GLN SER ILE ILE HIS ALA LYS ARG THR TYR
SEQRES   6 A  348  ARG GLU LEU ARG LEU LEU LYS HIS MET LYS HIS GLU ASN
SEQRES   7 A  348  VAL ILE GLY LEU LEU ASP VAL PHE THR PRO ALA ARG SER
SEQRES   8 A  348  LEU GLU GLU PHE ASN ASP VAL TYR LEU VAL THR HIS LEU
SEQRES   9 A  348  MET GLY ALA ASP LEU ASN ASN ILE VAL LYS CYS ALA LYS
SEQRES  10 A  348  LEU THR ASP ASP HIS VAL GLN PHE LEU ILE TYR GLN ILE
SEQRES  11 A  348  LEU ARG GLY LEU LYS TYR ILE HIS SER ALA ASP ILE ILE
SEQRES  12 A  348  HIS ARG ASP LEU LYS PRO SER ASN LEU ALA VAL ASN GLU
SEQRES  13 A  348  ASP CYS GLU LEU LYS ILE LEU ASP PHE GLY LEU ALA ARG
SEQRES  14 A  348  HIS THR ASP ASP GLU MET THR GLY TYR VAL ALA THR ARG
SEQRES  15 A  348  TRP TYR ARG ALA PRO GLU ILE MET LEU ASN TRP MET HIS
SEQRES  16 A  348  TYR ASN GLN THR VAL ASP ILE TRP SER VAL GLY CYS ILE
SEQRES  17 A  348  MET ALA GLU LEU LEU THR GLY ARG THR LEU PHE PRO GLY
SEQRES  18 A  348  THR ASP HIS ILE ASP GLN LEU LYS LEU ILE LEU ARG LEU
SEQRES  19 A  348  VAL GLY THR PRO GLY ALA GLU LEU LEU LYS LYS ILE SER
SEQRES  20 A  348  SER GLU SER ALA ARG ASN TYR ILE GLN SER LEU ALA GLN
SEQRES  21 A  348  MET PRO LYS MET ASN PHE ALA ASN VAL PHE ILE GLY ALA
SEQRES  22 A  348  ASN PRO LEU ALA VAL ASP LEU LEU GLU LYS MET LEU VAL
SEQRES  23 A  348  LEU ASP SER ASP LYS ARG ILE THR ALA ALA GLN ALA LEU
SEQRES  24 A  348  ALA HIS ALA TYR PHE ALA GLN TYR HIS ASP PRO ASP ASP
SEQRES  25 A  348  GLU PRO VAL ALA ASP PRO TYR ASP GLN SER PHE GLU SER
SEQRES  26 A  348  ARG ASP LEU LEU ILE ASP GLU TRP LYS SER LEU THR TYR
SEQRES  27 A  348  ASP GLU VAL ILE SER PHE VAL PRO PRO PRO
HET    337  A   1      42
HETNAM     337 N-BENZYL-1-[5-({5-TERT-BUTYL-2-METHOXY-3-
HETNAM   2 337  [(METHYLSULFONYL)AMINO]PHENYL}CARBAMOYL)-2-
HETNAM   3 337  METHYLPHENYL]-1H-1,2,3-TRIAZOLE-4-CARBOXAMIDE
FORMUL   2  337    C30 H34 N6 O5 S
FORMUL   3  HOH   *143(H2 O)
HELIX    1   1 GLY A   31  ALA A   34  5                                   4
HELIX    2   2 SER A   61  MET A   78  1                                  18
HELIX    3   3 LEU A  113  LYS A  118  1                                   6
HELIX    4   4 THR A  123  ALA A  144  1                                  22
HELIX    5   5 LYS A  152  SER A  154  5                                   3
HELIX    6   6 ALA A  184  ARG A  189  5                                   6
HELIX    7   7 ALA A  190  LEU A  195  1                                   6
HELIX    8   8 THR A  203  GLY A  219  1                                  17
HELIX    9   9 ASP A  227  GLY A  240  1                                  14
HELIX   10  10 GLY A  243  LYS A  248  1                                   6
HELIX   11  11 SER A  252  LEU A  262  1                                  11
HELIX   12  12 ASN A  269  PHE A  274  1                                   6
HELIX   13  13 ASN A  278  LEU A  289  1                                  12
HELIX   14  14 ASP A  292  ARG A  296  5                                   5
HELIX   15  15 THR A  298  HIS A  305  1                                   8
HELIX   16  16 ALA A  306  ALA A  309  5                                   4
HELIX   17  17 GLN A  325  ARG A  330  5                                   6
HELIX   18  18 LEU A  333  SER A  347  1                                  15
SHEET    1   A 2 PHE A   8  LEU A  13  0
SHEET    2   A 2 THR A  16  PRO A  21 -1  O  TRP A  18   N  GLN A  11
SHEET    1   B 5 TYR A  24  PRO A  29  0
SHEET    2   B 5 VAL A  38  ASP A  43 -1  O  ALA A  40   N  SER A  28
SHEET    3   B 5 ARG A  49  LYS A  54 -1  O  VAL A  52   N  CYS A  39
SHEET    4   B 5 TYR A 103  HIS A 107 -1  O  THR A 106   N  ALA A  51
SHEET    5   B 5 ASP A  88  PHE A  90 -1  N  ASP A  88   O  VAL A 105
SHEET    1   C 3 ALA A 111  ASP A 112  0
SHEET    2   C 3 LEU A 156  VAL A 158 -1  O  VAL A 158   N  ALA A 111
SHEET    3   C 3 LEU A 164  ILE A 166 -1  O  LYS A 165   N  ALA A 157
SITE     1 AC1 19 TYR A  35  ALA A  51  LYS A  53  ARG A  70
SITE     2 AC1 19 GLU A  71  LEU A  75  MET A  78  ILE A  84
SITE     3 AC1 19 THR A 106  HIS A 107  LEU A 108  MET A 109
SITE     4 AC1 19 GLY A 110  ALA A 111  ASP A 112  LEU A 167
SITE     5 AC1 19 ASP A 168  GLY A 170  HOH A 451
CRYST1   65.450   73.890   74.140  90.00  90.00  90.00 P 21 21 21    4
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      0.015279  0.000000  0.000000        0.00000
SCALE2      0.000000  0.013534  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013488        0.00000
      
PROCHECK
Go to PROCHECK summary
 References