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PDBsum entry 3p7c

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Transferase/transferase inhibitor PDB id
3p7c
Jmol
Contents
Protein chain
332 a.a.
Ligands
BOG
P7C
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       12-OCT-10   3P7C
TITLE     P38 INHIBITOR-BOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 14;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: MAP KINASE 14, MAPK 14, CRK1, MITOGEN-ACTIVATED PROTEIN
COMPND   5 KINASE P38 ALPHA, MAP KINASE P38 ALPHA;
COMPND   6 EC: 2.7.11.24;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE   3 ORGANISM_COMMON: MOUSE;
SOURCE   4 ORGANISM_TAXID: 10090;
SOURCE   5 GENE: MAPK14, CRK1, CSBP1, CSBP2;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    KINASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.K.MOFFETT,H.NAMBOODIRI
REVDAT   3   25-JAN-12 3P7C    1       JRNL
REVDAT   2   09-NOV-11 3P7C    1       JRNL
REVDAT   1   12-OCT-11 3P7C    0
JRNL        AUTH   K.MOFFETT,Z.KONTEATIS,D.NGUYEN,R.SHETTY,J.LUDINGTON,
JRNL        AUTH 2 T.FUJIMOTO,K.J.LEE,X.CHAI,H.NAMBOODIRI,M.KARPUSAS,B.DORSEY,
JRNL        AUTH 3 F.GUARNIERI,M.BUKHTIYAROVA,E.SPRINGMAN,E.MICHELOTTI
JRNL        TITL   DISCOVERY OF A NOVEL CLASS OF NON-ATP SITE DFG-OUT STATE P38
JRNL        TITL 2 INHIBITORS UTILIZING COMPUTATIONALLY ASSISTED VIRTUAL
JRNL        TITL 3 FRAGMENT-BASED DRUG DESIGN (VFBDD).
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  21  7155 2011
JRNL        REFN                   ISSN 0960-894X
JRNL        PMID   22014550
JRNL        DOI    10.1016/J.BMCL.2011.09.078
REMARK   2
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0110
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) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.09
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.1
REMARK   3   NUMBER OF REFLECTIONS             : 14762
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) : 0.239
REMARK   3   R VALUE            (WORKING SET) : 0.234
REMARK   3   FREE R VALUE                     : 0.292
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1279
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) : 2.19
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.25
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1023
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.32
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2740
REMARK   3   BIN FREE R VALUE SET COUNT          : 109
REMARK   3   BIN FREE R VALUE                    : 0.3950
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2683
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 56
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.92
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.94000
REMARK   3    B22 (A**2) : -0.03000
REMARK   3    B33 (A**2) : -0.91000
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): 0.475
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.301
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.186
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.142
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.917
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.875
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2803 ; 0.020 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3804 ; 1.905 ; 1.983
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   329 ; 6.985 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   130 ;35.981 ;23.923
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   480 ;21.452 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;19.656 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   423 ; 0.121 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2092 ; 0.009 ; 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):  1661 ; 1.039 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2694 ; 1.841 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1142 ; 2.645 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1110 ; 4.036 ; 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
REMARK   4
REMARK   4 3P7C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-OCT-10.
REMARK 100 THE RCSB ID CODE IS RCSB062047.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 17-AUG-04
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : NSLS
REMARK 200  BEAMLINE                       : X4A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97931
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17097
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.090
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5
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: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-20% PEG4000    0.1M CACODYLIC ACID,
REMARK 280  50 MM N-OCTYL-BETA-D-GLUCOSIDE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 293K, PH 6.0
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       33.43000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       38.06500
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.38500
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       38.06500
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.43000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.38500
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     MET A    -5
REMARK 465     ALA A    -4
REMARK 465     HIS A    -3
REMARK 465     HIS A    -2
REMARK 465     HIS A    -1
REMARK 465     HIS A     0
REMARK 465     HIS A     1
REMARK 465     SER A     2
REMARK 465     GLN A     3
REMARK 465     GLU A     4
REMARK 465     GLY A    33
REMARK 465     ALA A    34
REMARK 465     TYR A    35
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 465     VAL A   183
REMARK 465     LEU A   353
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 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    CYS A 162   CB    CYS A 162   SG      0.189
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 A 151   CA  -  CB  -  CG  ANGL. DEV. =  15.8 DEGREES
REMARK 500    CYS A 162   CB  -  CA  -  C   ANGL. DEV. =   8.0 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    LYS A  15      -13.12     79.04
REMARK 500    ALA A  93      121.64    -26.87
REMARK 500    ASN A 100       11.14   -157.35
REMARK 500    ASP A 145       30.04     78.74
REMARK 500    ARG A 149      -19.89     78.91
REMARK 500    MET A 198      -44.06    102.94
REMARK 500    TYR A 200      120.07     74.56
REMARK 500    SER A 252       99.99    -67.44
REMARK 500    GLU A 253      -47.74    -26.64
REMARK 500    SER A 254      -90.27    -34.87
REMARK 500    PHE A 274       43.54   -108.95
REMARK 500    ILE A 275     -102.36     -7.81
REMARK 500    ASP A 292       94.81    -57.69
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        24.0      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 P7C A 362
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3P5K   RELATED DB: PDB
REMARK 900 RELATED ID: 3P78   RELATED DB: PDB
REMARK 900 RELATED ID: 3P79   RELATED DB: PDB
REMARK 900 RELATED ID: 3P7B   RELATED DB: PDB
REMARK 900 RELATED ID: 3P7A   RELATED DB: PDB
DBREF  3P7C A    2   360  UNP    P47811   MK14_MOUSE       2    360
SEQADV 3P7C MET A   -5  UNP  P47811              EXPRESSION TAG
SEQADV 3P7C ALA A   -4  UNP  P47811              EXPRESSION TAG
SEQADV 3P7C HIS A   -3  UNP  P47811              EXPRESSION TAG
SEQADV 3P7C HIS A   -2  UNP  P47811              EXPRESSION TAG
SEQADV 3P7C HIS A   -1  UNP  P47811              EXPRESSION TAG
SEQADV 3P7C HIS A    0  UNP  P47811              EXPRESSION TAG
SEQADV 3P7C HIS A    1  UNP  P47811              EXPRESSION TAG
SEQRES   1 A  366  MET ALA HIS HIS HIS HIS HIS SER GLN GLU ARG PRO THR
SEQRES   2 A  366  PHE TYR ARG GLN GLU LEU ASN LYS THR ILE TRP GLU VAL
SEQRES   3 A  366  PRO GLU ARG TYR GLN ASN LEU SER PRO VAL GLY SER GLY
SEQRES   4 A  366  ALA TYR GLY SER VAL CYS ALA ALA PHE ASP THR LYS THR
SEQRES   5 A  366  GLY HIS ARG VAL ALA VAL LYS LYS LEU SER ARG PRO PHE
SEQRES   6 A  366  GLN SER ILE ILE HIS ALA LYS ARG THR TYR ARG GLU LEU
SEQRES   7 A  366  ARG LEU LEU LYS HIS MET LYS HIS GLU ASN VAL ILE GLY
SEQRES   8 A  366  LEU LEU ASP VAL PHE THR PRO ALA ARG SER LEU GLU GLU
SEQRES   9 A  366  PHE ASN ASP VAL TYR LEU VAL THR HIS LEU MET GLY ALA
SEQRES  10 A  366  ASP LEU ASN ASN ILE VAL LYS CYS GLN LYS LEU THR ASP
SEQRES  11 A  366  ASP HIS VAL GLN PHE LEU ILE TYR GLN ILE LEU ARG GLY
SEQRES  12 A  366  LEU LYS TYR ILE HIS SER ALA ASP ILE ILE HIS ARG ASP
SEQRES  13 A  366  LEU LYS PRO SER ASN LEU ALA VAL ASN GLU ASP CYS GLU
SEQRES  14 A  366  LEU LYS ILE LEU ASP PHE GLY LEU ALA ARG HIS THR ASP
SEQRES  15 A  366  ASP GLU MET THR GLY TYR VAL ALA THR ARG TRP TYR ARG
SEQRES  16 A  366  ALA PRO GLU ILE MET LEU ASN TRP MET HIS TYR ASN GLN
SEQRES  17 A  366  THR VAL ASP ILE TRP SER VAL GLY CYS ILE MET ALA GLU
SEQRES  18 A  366  LEU LEU THR GLY ARG THR LEU PHE PRO GLY THR ASP HIS
SEQRES  19 A  366  ILE ASP GLN LEU LYS LEU ILE LEU ARG LEU VAL GLY THR
SEQRES  20 A  366  PRO GLY ALA GLU LEU LEU LYS LYS ILE SER SER GLU SER
SEQRES  21 A  366  ALA ARG ASN TYR ILE GLN SER LEU ALA GLN MET PRO LYS
SEQRES  22 A  366  MET ASN PHE ALA ASN VAL PHE ILE GLY ALA ASN PRO LEU
SEQRES  23 A  366  ALA VAL ASP LEU LEU GLU LYS MET LEU VAL LEU ASP SER
SEQRES  24 A  366  ASP LYS ARG ILE THR ALA ALA GLN ALA LEU ALA HIS ALA
SEQRES  25 A  366  TYR PHE ALA GLN TYR HIS ASP PRO ASP ASP GLU PRO VAL
SEQRES  26 A  366  ALA ASP PRO TYR ASP GLN SER PHE GLU SER ARG ASP LEU
SEQRES  27 A  366  LEU ILE ASP GLU TRP LYS SER LEU THR TYR ASP GLU VAL
SEQRES  28 A  366  ILE SER PHE VAL PRO PRO PRO LEU ASP GLN GLU GLU MET
SEQRES  29 A  366  GLU SER
HET    BOG  A 361      20
HET    P7C  A 362      36
HETNAM     BOG B-OCTYLGLUCOSIDE
HETNAM     P7C 1-[5-TERT-BUTYL-3-({4-[2-(DIMETHYLAMINO)ETHYL]-5-OXO-1,
HETNAM   2 P7C  4-DIAZEPAN-1-YL}CARBONYL)THIOPHEN-2-YL]-3-(2,3-
HETNAM   3 P7C  DICHLOROPHENYL)UREA
FORMUL   2  BOG    C14 H28 O6
FORMUL   3  P7C    C25 H33 CL2 N5 O3 S
HELIX    1   1 SER A   61  MET A   78  1                                  18
HELIX    2   2 LEU A  113  GLN A  120  1                                   8
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  184  ARG A  189  5                                   6
HELIX    6   6 ALA A  190  LEU A  195  1                                   6
HELIX    7   7 THR A  203  GLY A  219  1                                  17
HELIX    8   8 ASP A  227  GLY A  240  1                                  14
HELIX    9   9 GLY A  243  LYS A  248  1                                   6
HELIX   10  10 SER A  252  LEU A  262  1                                  11
HELIX   11  11 ASN A  269  PHE A  274  1                                   6
HELIX   12  12 ASN A  278  LEU A  289  1                                  12
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 GLN A  325  ARG A  330  5                                   6
HELIX   16  16 LEU A  333  PHE A  348  1                                  16
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  GLY A  31  0
SHEET    2   B 5 SER A  37  ASP A  43 -1  O  PHE A  42   N  GLN A  25
SHEET    3   B 5 ARG A  49  LYS A  54 -1  O  LYS A  54   N  SER A  37
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 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  9 GLU A 192  LEU A 195  TRP A 197  TYR A 200
SITE     2 AC1  9 LEU A 246  LEU A 291  ASP A 292  SER A 293
SITE     3 AC1  9 ASP A 294
SITE     1 AC2 15 ALA A  51  LYS A  53  ARG A  67  ARG A  70
SITE     2 AC2 15 GLU A  71  LEU A  74  LEU A  75  VAL A  83
SITE     3 AC2 15 ILE A  84  LEU A 104  THR A 106  HIS A 148
SITE     4 AC2 15 ARG A 149  LEU A 167  ASP A 168
CRYST1   66.860   70.770   76.130  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      0.014957  0.000000  0.000000        0.00000
SCALE2      0.000000  0.014130  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013135        0.00000
      
PROCHECK
Go to PROCHECK summary
 References