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PDBsum entry 3pg3

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Transferase/transferase inhibitor PDB id
3pg3
Jmol
Contents
Protein chain
337 a.a.
Ligands
BOG
DG7
Waters ×99
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       29-OCT-10   3PG3
TITLE     HUMAN P38 MAP KINASE IN COMPLEX WITH RL182
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 14;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: MAP KINASE 14, MAPK 14, CYTOKINE SUPPRESSIVE ANTI-
COMPND   5 INFLAMMATORY DRUG-BINDING PROTEIN, CSAID-BINDING PROTEIN, CSBP, MAP
COMPND   6 KINASE MXI2, MAX-INTERACTING PROTEIN 2, MITOGEN-ACTIVATED PROTEIN
COMPND   7 KINASE P38 ALPHA, MAP KINASE P38 ALPHA, SAPK2A;
COMPND   8 EC: 2.7.11.24;
COMPND   9 ENGINEERED: YES;
COMPND  10 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: MAPK14, CSBP, CSBP1, CSBP2, CSPB1, MXI2;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX 6P-1
KEYWDS    DFG-OUT, SAR, KINASE DOMAIN, THIAZOLE-UREA, TRANSFERASE-TRANSFERASE
KEYWDS   2 INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    C.GRUETTER,J.R.SIMARD,M.GETLIK,D.RAUH
REVDAT   1   02-NOV-11 3PG3    0
JRNL        AUTH   M.GETLIK,C.GRUETTER,J.R.SIMARD,W.VAN OTTERLO,A.ROBUBI,
JRNL        AUTH 2 B.AUST,D.RAUH
JRNL        TITL   STRUCTURE-BASED DESIGN AND SYNTHESIS OF CELL ACTIVE
JRNL        TITL 2 N-PYRAZOLE, N-THIAZOLE UREA INHIBITORS OF THE MAP KINASE
JRNL        TITL 3 P38ALPHA
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0102
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) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 24717
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) : 0.221
REMARK   3   R VALUE            (WORKING SET) : 0.220
REMARK   3   FREE R VALUE                     : 0.261
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 989
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) : 2.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1713
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2820
REMARK   3   BIN FREE R VALUE SET COUNT          : 71
REMARK   3   BIN FREE R VALUE                    : 0.3200
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2714
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 55
REMARK   3   SOLVENT ATOMS            : 99
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 34.57
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.30
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 1.14000
REMARK   3    B22 (A**2) : -0.83000
REMARK   3    B33 (A**2) : -0.31000
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): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.184
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.131
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.603
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.940
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):  2844 ; 0.009 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3863 ; 1.176 ; 1.988
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   337 ; 4.993 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   130 ;33.174 ;23.923
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   487 ;15.345 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;17.034 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   433 ; 0.074 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2136 ; 0.005 ; 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):  1690 ; 0.612 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2742 ; 1.141 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1154 ; 1.601 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1120 ; 2.711 ; 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  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK   4
REMARK   4 3PG3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-NOV-10.
REMARK 100 THE RCSB ID CODE IS RCSB062334.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 22-AUG-10
REMARK 200  TEMPERATURE           (KELVIN) : 90
REMARK 200  PH                             : 6.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SLS
REMARK 200  BEAMLINE                       : X10SA
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.040000
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : DYNAMIC BENDABLE MIRROR
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XSCALE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24719
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7
REMARK 200  DATA REDUNDANCY                : 4.360
REMARK 200  R MERGE                    (I) : 0.06000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 19.8200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.3
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.55
REMARK 200  R MERGE FOR SHELL          (I) : 0.41700
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 4.900
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: 1ZYJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 43.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES, 20-30% PEG4000, 50 MM N-
REMARK 280  BOG, PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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       34.55500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.26500
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.98500
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       37.26500
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.55500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.98500
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: MONOMERIC
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     GLY A     1
REMARK 465     SER A     2
REMARK 465     GLN A     3
REMARK 465     LEU A   171
REMARK 465     CYS 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 465     VAL A   183
REMARK 465     ASP A   354
REMARK 465     GLN A   355
REMARK 465     GLU A   356
REMARK 465     GLU A   357
REMARK 465     MET A   358
REMARK 465     GLU A   359
REMARK 465     SER A   360
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     GLU A   4    CG   CD   OE1  OE2
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    SER A  32      -45.64     75.23
REMARK 500    ASP A 145       33.77     71.01
REMARK 500    ARG A 149      -17.87     80.78
REMARK 500    MET A 198      -12.09     86.33
REMARK 500    HIS A 199       60.92   -117.27
REMARK 500    PHE A 274       70.78   -116.49
REMARK 500    LEU A 289       59.97    -95.62
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    MET A 198        24.9      L          L   OUTSIDE RANGE
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 BOG A 361
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DG7 A 362
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3IW8   RELATED DB: PDB
DBREF  3PG3 A    2   360  UNP    Q16539   MK14_HUMAN       2    360
SEQADV 3PG3 GLY A    1  UNP  Q16539              EXPRESSION TAG
SEQADV 3PG3 SER A  119  UNP  Q16539    CYS   119 ENGINEERED MUTATION
SEQADV 3PG3 SER A  162  UNP  Q16539    CYS   162 ENGINEERED MUTATION
SEQADV 3PG3 CYS A  172  UNP  Q16539    ALA   172 ENGINEERED MUTATION
SEQADV 3PG3 LEU A  327  UNP  Q16539    PHE   327 ENGINEERED MUTATION
SEQRES   1 A  360  GLY SER GLN GLU ARG PRO THR PHE TYR ARG GLN GLU LEU
SEQRES   2 A  360  ASN LYS THR ILE TRP GLU VAL PRO GLU ARG TYR GLN ASN
SEQRES   3 A  360  LEU SER PRO VAL GLY SER GLY ALA TYR GLY SER VAL CYS
SEQRES   4 A  360  ALA ALA PHE ASP THR LYS THR GLY LEU ARG VAL ALA VAL
SEQRES   5 A  360  LYS LYS LEU SER ARG PRO PHE GLN SER ILE ILE HIS ALA
SEQRES   6 A  360  LYS ARG THR TYR ARG GLU LEU ARG LEU LEU LYS HIS MET
SEQRES   7 A  360  LYS HIS GLU ASN VAL ILE GLY LEU LEU ASP VAL PHE THR
SEQRES   8 A  360  PRO ALA ARG SER LEU GLU GLU PHE ASN ASP VAL TYR LEU
SEQRES   9 A  360  VAL THR HIS LEU MET GLY ALA ASP LEU ASN ASN ILE VAL
SEQRES  10 A  360  LYS SER GLN LYS LEU THR ASP ASP HIS VAL GLN PHE LEU
SEQRES  11 A  360  ILE TYR GLN ILE LEU ARG GLY LEU LYS TYR ILE HIS SER
SEQRES  12 A  360  ALA ASP ILE ILE HIS ARG ASP LEU LYS PRO SER ASN LEU
SEQRES  13 A  360  ALA VAL ASN GLU ASP SER GLU LEU LYS ILE LEU ASP PHE
SEQRES  14 A  360  GLY LEU CYS ARG HIS THR ASP ASP GLU MET THR GLY TYR
SEQRES  15 A  360  VAL ALA THR ARG TRP TYR ARG ALA PRO GLU ILE MET LEU
SEQRES  16 A  360  ASN TRP MET HIS TYR ASN GLN THR VAL ASP ILE TRP SER
SEQRES  17 A  360  VAL GLY CYS ILE MET ALA GLU LEU LEU THR GLY ARG THR
SEQRES  18 A  360  LEU PHE PRO GLY THR ASP HIS ILE ASP GLN LEU LYS LEU
SEQRES  19 A  360  ILE LEU ARG LEU VAL GLY THR PRO GLY ALA GLU LEU LEU
SEQRES  20 A  360  LYS LYS ILE SER SER GLU SER ALA ARG ASN TYR ILE GLN
SEQRES  21 A  360  SER LEU THR GLN MET PRO LYS MET ASN PHE ALA ASN VAL
SEQRES  22 A  360  PHE ILE GLY ALA ASN PRO LEU ALA VAL ASP LEU LEU GLU
SEQRES  23 A  360  LYS MET LEU VAL LEU ASP SER ASP LYS ARG ILE THR ALA
SEQRES  24 A  360  ALA GLN ALA LEU ALA HIS ALA TYR PHE ALA GLN TYR HIS
SEQRES  25 A  360  ASP PRO ASP ASP GLU PRO VAL ALA ASP PRO TYR ASP GLN
SEQRES  26 A  360  SER LEU GLU SER ARG ASP LEU LEU ILE ASP GLU TRP LYS
SEQRES  27 A  360  SER LEU THR TYR ASP GLU VAL ILE SER PHE VAL PRO PRO
SEQRES  28 A  360  PRO LEU ASP GLN GLU GLU MET GLU SER
HET    BOG  A 361      20
HET    DG7  A 362      35
HETNAM     BOG B-OCTYLGLUCOSIDE
HETNAM     DG7 1-[3-TERT-BUTYL-1-(4-METHYLPHENYL)-1H-PYRAZOL-5-YL]-3-
HETNAM   2 DG7  {4-[2-(PYRIDIN-3-YLMETHOXY)ETHYL]-1,3-THIAZOL-2-
HETNAM   3 DG7  YL}UREA
HETSYN     DG7 1-(3-TERT-BUTYL-1-P-TOLYL-1H-PYRAZOL-5-YL)-3-(4-(2-
HETSYN   2 DG7  (PYRIDIN-3-YLMETHOXY)ETHYL)THIAZOL-2-YL)UREA
FORMUL   2  BOG    C14 H28 O6
FORMUL   3  DG7    C26 H30 N6 O2 S
FORMUL   4  HOH   *99(H2 O)
HELIX    1   1 SER A   61  MET A   78  1                                  18
HELIX    2   2 ASP A  112  LYS A  118  1                                   7
HELIX    3   3 THR A  123  ALA A  144  1                                  22
HELIX    4   4 LYS A  152  SER A  154  5                                   3
HELIX    5   5 ALA A  190  LEU A  195  1                                   6
HELIX    6   6 THR A  203  GLY A  219  1                                  17
HELIX    7   7 ASP A  227  GLY A  240  1                                  14
HELIX    8   8 GLY A  243  LYS A  248  1                                   6
HELIX    9   9 SER A  252  SER A  261  1                                  10
HELIX   10  10 ASN A  269  VAL A  273  5                                   5
HELIX   11  11 ASN A  278  LEU A  289  1                                  12
HELIX   12  12 ASP A  292  ARG A  296  5                                   5
HELIX   13  13 THR A  298  ALA A  304  1                                   7
HELIX   14  14 HIS A  305  ALA A  309  5                                   5
HELIX   15  15 ASP A  313  GLU A  317  5                                   5
HELIX   16  16 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  THR A  16   N  LEU A  13
SHEET    1   B 5 TYR A  24  PRO A  29  0
SHEET    2   B 5 SER A  37  ASP A  43 -1  O  ALA A  40   N  SER A  28
SHEET    3   B 5 LEU A  48  LYS A  54 -1  O  LEU A  48   N  ASP A  43
SHEET    4   B 5 TYR A 103  HIS A 107 -1  O  LEU A 104   N  LYS A  53
SHEET    5   B 5 ASP A  88  PHE A  90 -1  N  ASP A  88   O  VAL A 105
SHEET    1   C 2 LEU A 156  VAL A 158  0
SHEET    2   C 2 LEU A 164  ILE A 166 -1  O  LYS A 165   N  ALA A 157
SITE     1 AC1 13 GLU A 192  TRP A 197  HIS A 199  TYR A 200
SITE     2 AC1 13 ASN A 201  LEU A 246  LYS A 249  LEU A 291
SITE     3 AC1 13 ASP A 292  SER A 293  ASP A 294  HOH A 387
SITE     4 AC1 13 HOH A 419
SITE     1 AC2 12 ALA A  51  ARG A  70  GLU A  71  LEU A  74
SITE     2 AC2 12 ILE A  84  HIS A 107  LEU A 108  MET A 109
SITE     3 AC2 12 HIS A 148  LEU A 167  ASP A 168  PHE A 169
CRYST1   69.110   69.970   74.530  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      0.014470  0.000000  0.000000        0.00000
SCALE2      0.000000  0.014292  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013417        0.00000
      
PROCHECK
Go to PROCHECK summary
 References