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PDBsum entry 2kyx

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Isomerase PDB id
2kyx
Jmol
Contents
Protein chain
83 a.a.
HEADER    ISOMERASE                               09-JUN-10   2KYX
TITLE     SOLUTION STRUCTURE OF THE RRM DOMAIN OF CYP33
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE E;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: UNP RESIDUES 3-83;
COMPND   5 SYNONYM: PPIASE E, ROTAMASE E, CYCLOPHILIN E, CYCLOPHILIN-33;
COMPND   6 EC: 5.2.1.8;
COMPND   7 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: PPIE, CYP33;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PGEX 4T
KEYWDS    CYP33, RRM, ISOMERASE
EXPDTA    SOLUTION NMR
NUMMDL    10
AUTHOR    S.PARK,J.H.BUSHWELLER
REVDAT   1   25-AUG-10 2KYX    0
JRNL        AUTH   S.PARK,U.OSMERS,G.RAMAN,R.H.SCHWANTES,M.O.DIAZ,
JRNL        AUTH 2 J.H.BUSHWELLER
JRNL        TITL   THE PHD3 DOMAIN OF MLL ACTS AS A CYP33-REGULATED SWITCH
JRNL        TITL 2 BETWEEN MLL-MEDIATED ACTIVATION AND REPRESSION .
JRNL        REF    BIOCHEMISTRY                  V.  49  6576 2010
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   20677832
JRNL        DOI    10.1021/BI1009387
REMARK   2
REMARK   2 RESOLUTION. NOT APPLICABLE.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS
REMARK   3   AUTHORS     : BRUNGER, ADAMS, CLORE, GROS, NILGES AND READ
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2KYX COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUN-10.
REMARK 100 THE RCSB ID CODE IS RCSB101747.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210  EXPERIMENT TYPE                : NMR
REMARK 210  TEMPERATURE           (KELVIN) : 303
REMARK 210  PH                             : 6.9
REMARK 210  IONIC STRENGTH                 : NULL
REMARK 210  PRESSURE                       : AMBIENT
REMARK 210  SAMPLE CONTENTS                : 25 MM POTASSIUM PHOSPHATE, 50 MM
REMARK 210                                   SODIUM CHLORIDE, 1 MM DTT, 1 MM
REMARK 210                                   SODIUM AZIDE, 95% H2O/5% D2O
REMARK 210
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 2D 1H-15N HSQC; 2D 1H-13C HSQC;
REMARK 210                                   3D CBCA(CO)NH; 3D C(CO)NH; 3D
REMARK 210                                   HNCO; 3D HNCAB; 3D H(CCO)NH; 3D
REMARK 210                                   HCCH-TOCSY; 3D 1H-13C NOESY; 3D
REMARK 210                                   1H-15N NOESY; 3D TROSY_HNCO
REMARK 210  SPECTROMETER FIELD STRENGTH    : 600 MHZ
REMARK 210  SPECTROMETER MODEL             : INOVA
REMARK 210  SPECTROMETER MANUFACTURER      : VARIAN
REMARK 210
REMARK 210  STRUCTURE DETERMINATION.
REMARK 210   SOFTWARE USED                 : CNS
REMARK 210   METHOD USED                   : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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    VAL A    21     H    ALA A    25              1.59
REMARK 500   H    LEU A     8     O    VAL A    52              1.59
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  1 SER A  -1       90.86     58.26
REMARK 500  1 THR A   4       70.16     50.72
REMARK 500  1 HIS A  46     -168.38    -68.45
REMARK 500  1 SER A  70     -166.23   -102.70
REMARK 500  2 ARG A   6      -24.89    165.58
REMARK 500  2 ASP A  31      105.92    -54.39
REMARK 500  2 PRO A  38       77.12    -69.35
REMARK 500  2 HIS A  46     -169.05    -79.65
REMARK 500  2 SER A  70     -161.57   -113.68
REMARK 500  2 LEU A  81       35.65    -84.42
REMARK 500  2 ALA A  82      167.84     58.13
REMARK 500  3 LYS A   5      -93.47     49.73
REMARK 500  3 ARG A   6      -35.95    173.43
REMARK 500  3 ASP A  31      109.54    -59.85
REMARK 500  3 GLU A  69       30.05     70.82
REMARK 500  3 ALA A  82      160.81     59.12
REMARK 500  4 SER A  -1      159.68     62.91
REMARK 500  4 THR A   3      -77.20   -128.12
REMARK 500  4 THR A   4       92.76     59.09
REMARK 500  4 ASP A  31      105.07    -59.58
REMARK 500  4 GLU A  44       38.69     37.19
REMARK 500  4 HIS A  46     -179.89    -64.88
REMARK 500  4 SER A  70     -168.17   -106.09
REMARK 500  4 ALA A  82     -165.07   -102.73
REMARK 500  5 THR A   3      158.38     59.09
REMARK 500  5 ASP A  31      106.20    -58.25
REMARK 500  5 LEU A  39     -169.18   -122.79
REMARK 500  5 TYR A  41       43.12    -88.36
REMARK 500  5 GLU A  42      -40.83   -170.43
REMARK 500  5 HIS A  46     -178.94    -57.26
REMARK 500  5 SER A  70     -166.57   -122.82
REMARK 500  6 THR A   4       46.02    -94.27
REMARK 500  6 LYS A   5      159.56     61.43
REMARK 500  6 ARG A   6       18.01   -147.66
REMARK 500  6 GLU A  44       49.88     34.72
REMARK 500  6 GLU A  69       52.85     72.03
REMARK 500  7 THR A   3       90.95   -172.36
REMARK 500  7 THR A   4       80.14     57.23
REMARK 500  7 ARG A   6       61.95   -159.49
REMARK 500  7 LEU A  39     -164.14   -102.88
REMARK 500  7 TYR A  41      -47.87     81.39
REMARK 500  7 HIS A  46     -175.71    -66.33
REMARK 500  7 SER A  70     -166.38   -120.64
REMARK 500  8 SER A  -1      -53.17   -131.55
REMARK 500  8 THR A   4      -74.24   -126.13
REMARK 500  8 ARG A   6      -34.06    174.14
REMARK 500  8 TYR A  41      -48.70     82.81
REMARK 500  8 GLU A  44       32.31     39.41
REMARK 500  8 HIS A  46      175.51    -57.90
REMARK 500  8 SER A  70     -165.08   -105.39
REMARK 500
REMARK 500 THIS ENTRY HAS      67 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 16989   RELATED DB: BMRB
DBREF  2KYX A    3    83  UNP    Q9UNP9   PPIE_HUMAN       3     83
SEQADV 2KYX GLY A   -2  UNP  Q9UNP9              EXPRESSION TAG
SEQADV 2KYX SER A   -1  UNP  Q9UNP9              EXPRESSION TAG
SEQRES   1 A   83  GLY SER THR THR LYS ARG VAL LEU TYR VAL GLY GLY LEU
SEQRES   2 A   83  ALA GLU GLU VAL ASP ASP LYS VAL LEU HIS ALA ALA PHE
SEQRES   3 A   83  ILE PRO PHE GLY ASP ILE THR ASP ILE GLN ILE PRO LEU
SEQRES   4 A   83  ASP TYR GLU THR GLU LYS HIS ARG GLY PHE ALA PHE VAL
SEQRES   5 A   83  GLU PHE GLU LEU ALA GLU ASP ALA ALA ALA ALA ILE ASP
SEQRES   6 A   83  ASN MET ASN GLU SER GLU LEU PHE GLY ARG THR ILE ARG
SEQRES   7 A   83  VAL ASN LEU ALA LYS
HELIX    1   1 ASP A   18  ILE A   27  1                                  10
HELIX    2   2 LEU A   56  ASN A   68  1                                  13
SHEET    1   A 5 ILE A  32  GLN A  36  0
SHEET    2   A 5 PHE A  49  PHE A  54 -1  O  GLU A  53   N  THR A  33
SHEET    3   A 5 LEU A   8  GLY A  11 -1  N  LEU A   8   O  VAL A  52
SHEET    4   A 5 ARG A  75  LEU A  81 -1  O  ARG A  78   N  GLY A  11
SHEET    5   A 5 SER A  70  LEU A  72 -1  N  LEU A  72   O  ARG A  75
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1
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      1.000000  0.000000  0.000000        0.00000
SCALE2      0.000000  1.000000  0.000000        0.00000
SCALE3      0.000000  0.000000  1.000000        0.00000
      
PROCHECK
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