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PDBsum entry 3mgy

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Transferase PDB id
3mgy
Jmol
Contents
Protein chain
329 a.a.
Ligands
BOG
Waters ×53
HEADER    TRANSFERASE                             07-APR-10   3MGY
TITLE     MUTAGENESIS OF P38 MAP KINASE ESHTABLISHES KEY ROLES OF PHE169 IN
TITLE    2 FUNCTION AND STRUCTURAL DYNAMICS AND REVEALS A NOVEL DFG-OUT STATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 14;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: MAP KINASE 14, MAPK 14, MITOGEN-ACTIVATED PROTEIN KINASE P38
COMPND   5 ALPHA, MAP KINASE P38 ALPHA, CYTOKINE SUPPRESSIVE ANTI-INFLAMMATORY
COMPND   6 DRUG-BINDING PROTEIN, CSAID-BINDING PROTEIN, CSBP, MAX-INTERACTING
COMPND   7 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: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: CSBP, CSBP1, CSBP2, CSPB1, MAPK14, MXI2;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: DE3
KEYWDS    TRANSFERASE, SIGNALING PROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    H.V.NAMBOODIRI,M.KARPUSAS,M.BUKHTIYAROVA,E.B.SPRINGMAN
REVDAT   2   22-DEC-10 3MGY    1       AUTHOR
REVDAT   1   21-APR-10 3MGY    0
SPRSDE     21-APR-10 3MGY      2PV5
JRNL        AUTH   M.BUKHTIYAROVA,M.KARPUSAS,K.NORTHROP,H.V.NAMBOODIRI,
JRNL        AUTH 2 E.B.SPRINGMAN
JRNL        TITL   MUTAGENESIS OF P38ALPHA MAP KINASE ESTABLISHES KEY ROLES OF
JRNL        TITL 2 PHE169 IN FUNCTION AND STRUCTURAL DYNAMICS AND REVEALS A
JRNL        TITL 3 NOVEL DFG-OUT STATE.
JRNL        REF    BIOCHEMISTRY                  V.  46  5687 2007
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   17441692
JRNL        DOI    10.1021/BI0622221
REMARK   2
REMARK   2 RESOLUTION.    2.10 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 : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.96
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.6
REMARK   3   NUMBER OF REFLECTIONS             : 18644
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 SET) : 0.239
REMARK   3   FREE R VALUE                     : 0.291
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.900
REMARK   3   FREE R VALUE TEST SET COUNT      : 1593
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           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.07
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1248
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2930
REMARK   3   BIN FREE R VALUE                    : 0.3760
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 106
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            : 2664
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 20
REMARK   3   SOLVENT ATOMS            : 53
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.14
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 1.73000
REMARK   3    B22 (A**2) : -0.50000
REMARK   3    B33 (A**2) : -1.24000
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) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : MASK
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  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3MGY COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-APR-10.
REMARK 100 THE RCSB ID CODE IS RCSB058532.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 16-AUG-04
REMARK 200  TEMPERATURE           (KELVIN) : 93
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) : 0.98
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21427
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.7
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.09500
REMARK 200  R SYM                      (I) : 0.07300
REMARK 200   FOR THE DATA SET  : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.26
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.41100
REMARK 200  R SYM FOR SHELL            (I) : 0.41000
REMARK 200   FOR SHELL         : 2.500
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: PDB ENTRY 1ZYJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-20% PEG 4000, 0.1 M CACODYLIC ACID,
REMARK 280  50 MM N-OCTYL-BETA-D-GLUCOSIDE, PH 6.0, VAPOR DIFFUSION, SITTING
REMARK 280  DROP, TEMPERATURE 295K
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       33.89500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.89000
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       37.89000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.89500
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     1
REMARK 465     SER A     2
REMARK 465     GLN A     3
REMARK 465     GLU A     4
REMARK 465     SER A    32
REMARK 465     GLY A    33
REMARK 465     ALA A    34
REMARK 465     TYR A    35
REMARK 465     GLY A   170
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     ALA A   184
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 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     ASP A 168    CB   CG   OD1  OD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    ALA A   255     O    ASN A   257              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   OE1  GLN A    25     OG   SER A   254     2664     2.05
REMARK 500
REMARK 500 REMARK: NULL
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      0.225
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    ARG A 136   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    CYS A 162   CB  -  CA  -  C   ANGL. DEV. =  13.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ASN A  14      -96.87     53.84
REMARK 500    SER A  56      -94.24    -47.68
REMARK 500    ARG A  57       69.97   -116.16
REMARK 500    SER A  95      143.83     61.47
REMARK 500    ASN A 100      -13.31   -146.61
REMARK 500    ARG A 149        0.61     85.85
REMARK 500    ASP A 150       39.46   -147.15
REMARK 500    ASN A 159     -163.66   -102.20
REMARK 500    ASP A 168      -87.53    144.18
REMARK 500    MET A 198      175.55     81.28
REMARK 500    HIS A 199       74.38     15.83
REMARK 500    THR A 203        3.96    -68.85
REMARK 500    SER A 254      -81.35    -73.34
REMARK 500    TYR A 258      -50.65     73.49
REMARK 500    THR A 263      104.30    -50.42
REMARK 500    GLN A 264       89.10    -62.75
REMARK 500    LEU A 289       54.42    -93.59
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    ARG A 330        24.8      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 367        DISTANCE =  7.30 ANGSTROMS
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 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3MH0   RELATED DB: PDB
REMARK 900 RELATED ID: 3MH1   RELATED DB: PDB
REMARK 900 RELATED ID: 3MH2   RELATED DB: PDB
REMARK 900 RELATED ID: 3MH3   RELATED DB: PDB
DBREF  3MGY A    1   360  UNP    Q16539   MK14_HUMAN       1    360
SEQRES   1 A  360  MET 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 CYS 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 CYS GLU LEU LYS ILE LEU ASP PHE
SEQRES  14 A  360  GLY LEU ALA 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 PHE 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
HETNAM     BOG B-OCTYLGLUCOSIDE
FORMUL   2  BOG    C14 H28 O6
FORMUL   3  HOH   *53(H2 O)
HELIX    1   1 SER A   61  MET A   78  1                                  18
HELIX    2   2 ARG A   94  PHE A   99  1                                   6
HELIX    3   3 ASP A  112  GLN A  120  1                                   9
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  190  LEU A  195  1                                   6
HELIX    7   7 GLN A  202  GLY A  219  1                                  18
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  GLN A  260  1                                   9
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 ASP A  292  ARG A  296  5                                   5
HELIX   14  14 THR A  298  ALA A  304  1                                   7
HELIX   15  15 HIS A  305  ALA A  309  5                                   5
HELIX   16  16 GLN A  325  ARG A  330  5                                   6
HELIX   17  17 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  ALA A  40   N  SER A  28
SHEET    3   B 5 ARG A  49  LYS A  54 -1  O  VAL A  50   N  ALA A  41
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 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 10 LEU A 195  TRP A 197  MET A 198  HIS A 199
SITE     2 AC1 10 LEU A 246  LYS A 249  LEU A 291  ASP A 292
SITE     3 AC1 10 SER A 293  ASP A 294
CRYST1   67.790   70.770   75.780  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      0.014751  0.000000  0.000000        0.00000
SCALE2      0.000000  0.014130  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013196        0.00000
      
PROCHECK
Go to PROCHECK summary
 References