Header list of 2cu1.pdb file
Complete list - v 10 2 Bytes
HEADER TRANSFERASE 24-MAY-05 2CU1
TITLE SOLUTION STRUCTURE OF THE PB1 DOMAIN OF HUMAN PROTEIN KINASE MEKK2B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PB1 DOMAIN;
COMPND 5 SYNONYM: MAPK/ERK KINASE KINASE 2, MEK KINASE 2, MEKK 2;
COMPND 6 EC: 2.7.1.37;
COMPND 7 ENGINEERED: YES;
COMPND 8 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: MAP3K2, MAPKKK2, MEKK2;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050207-07;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS PB1 DOMAIN, MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 2,
KEYWDS 2 MAPK/ERK KINASE KINASE 2, MEK KINASE 2, MEKK 2, SIGNALING PROTEIN,
KEYWDS 3 STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL
KEYWDS 4 AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 5 INITIATIVE, RSGI, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.INOUE,T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 10-NOV-21 2CU1 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CU1 1 VERSN
REVDAT 1 24-NOV-05 2CU1 0
JRNL AUTH K.INOUE,T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE PB1 DOMAIN OF HUMAN PROTEIN KINASE
JRNL TITL 2 MEKK2B
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, CYANA 2.0.17
REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CU1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024617.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.53MM U-15N,13C-LABELED
REMARK 210 PROTEIN; 20MM D-TRIS-HCL; 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9296, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION, STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY, STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
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: 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 6 96.11 -62.47
REMARK 500 1 ASN A 52 -66.98 -132.12
REMARK 500 1 LEU A 58 96.54 -59.62
REMARK 500 1 ASN A 87 -60.99 -128.86
REMARK 500 1 THR A 93 -19.82 -48.39
REMARK 500 1 PRO A 97 -174.13 -69.73
REMARK 500 1 PRO A 100 94.61 -69.77
REMARK 500 1 SER A 101 128.94 -171.58
REMARK 500 2 ARG A 16 28.01 39.13
REMARK 500 2 ASN A 52 -63.56 -133.35
REMARK 500 2 LEU A 58 98.48 -61.91
REMARK 500 2 SER A 74 90.06 -67.32
REMARK 500 2 MET A 77 108.45 -54.82
REMARK 500 2 GLU A 96 54.57 35.07
REMARK 500 2 SER A 101 96.47 -51.46
REMARK 500 3 SER A 3 99.25 -68.32
REMARK 500 3 ASN A 51 -62.34 -91.61
REMARK 500 3 ASN A 52 -67.51 -131.72
REMARK 500 3 LEU A 58 102.29 -59.85
REMARK 500 3 GLU A 96 149.72 -174.77
REMARK 500 4 SER A 2 43.00 34.81
REMARK 500 4 ASN A 52 -59.25 -134.25
REMARK 500 4 GLU A 53 -31.24 -130.35
REMARK 500 4 THR A 93 93.85 -69.91
REMARK 500 4 ASN A 94 122.37 -172.95
REMARK 500 5 ARG A 16 53.61 38.96
REMARK 500 5 SER A 44 36.44 -83.76
REMARK 500 5 ASN A 51 -75.24 -86.54
REMARK 500 5 ASN A 52 -75.47 -108.44
REMARK 500 5 LEU A 58 95.01 -64.26
REMARK 500 5 THR A 90 131.47 -174.94
REMARK 500 6 SER A 5 150.49 -40.66
REMARK 500 6 SER A 6 117.53 -173.25
REMARK 500 6 ASN A 51 -72.29 -87.55
REMARK 500 6 ASN A 52 -68.18 -120.37
REMARK 500 6 PRO A 57 94.59 -69.75
REMARK 500 6 LEU A 58 98.69 -55.93
REMARK 500 6 GLN A 91 40.97 -98.17
REMARK 500 6 LEU A 95 134.57 -171.66
REMARK 500 6 PRO A 97 -172.06 -69.80
REMARK 500 7 ASN A 51 -66.05 -95.79
REMARK 500 7 ASN A 52 -69.92 -128.46
REMARK 500 7 PRO A 57 97.45 -69.72
REMARK 500 7 LEU A 58 98.70 -56.73
REMARK 500 7 MET A 77 96.37 -67.52
REMARK 500 7 ILE A 86 108.40 -48.67
REMARK 500 7 SER A 102 142.73 -174.49
REMARK 500 8 ASN A 52 -75.78 -125.80
REMARK 500 8 LEU A 58 91.85 -61.96
REMARK 500 8 ILE A 75 -71.53 -73.57
REMARK 500
REMARK 500 THIS ENTRY HAS 120 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSO002001045.1 RELATED DB: TARGETDB
DBREF 2CU1 A 8 97 UNP Q9Y2U5 M3K2_HUMAN 43 132
SEQADV 2CU1 GLY A 1 UNP Q9Y2U5 CLONING ARTIFACT
SEQADV 2CU1 SER A 2 UNP Q9Y2U5 CLONING ARTIFACT
SEQADV 2CU1 SER A 3 UNP Q9Y2U5 CLONING ARTIFACT
SEQADV 2CU1 GLY A 4 UNP Q9Y2U5 CLONING ARTIFACT
SEQADV 2CU1 SER A 5 UNP Q9Y2U5 CLONING ARTIFACT
SEQADV 2CU1 SER A 6 UNP Q9Y2U5 CLONING ARTIFACT
SEQADV 2CU1 GLY A 7 UNP Q9Y2U5 CLONING ARTIFACT
SEQADV 2CU1 VAL A 68 UNP Q9Y2U5 LEU 103 ENGINEERED MUTATION
SEQADV 2CU1 SER A 98 UNP Q9Y2U5 CLONING ARTIFACT
SEQADV 2CU1 GLY A 99 UNP Q9Y2U5 CLONING ARTIFACT
SEQADV 2CU1 PRO A 100 UNP Q9Y2U5 CLONING ARTIFACT
SEQADV 2CU1 SER A 101 UNP Q9Y2U5 CLONING ARTIFACT
SEQADV 2CU1 SER A 102 UNP Q9Y2U5 CLONING ARTIFACT
SEQADV 2CU1 GLY A 103 UNP Q9Y2U5 CLONING ARTIFACT
SEQRES 1 A 103 GLY SER SER GLY SER SER GLY ASP VAL ARG VAL LYS PHE
SEQRES 2 A 103 GLU HIS ARG GLY GLU LYS ARG ILE LEU GLN PHE PRO ARG
SEQRES 3 A 103 PRO VAL LYS LEU GLU ASP LEU ARG SER LYS ALA LYS ILE
SEQRES 4 A 103 ALA PHE GLY GLN SER MET ASP LEU HIS TYR THR ASN ASN
SEQRES 5 A 103 GLU LEU VAL ILE PRO LEU THR THR GLN ASP ASP LEU ASP
SEQRES 6 A 103 LYS ALA VAL GLU LEU LEU ASP ARG SER ILE HIS MET LYS
SEQRES 7 A 103 SER LEU LYS ILE LEU LEU VAL ILE ASN GLY SER THR GLN
SEQRES 8 A 103 ALA THR ASN LEU GLU PRO SER GLY PRO SER SER GLY
HELIX 1 1 LYS A 29 GLY A 42 1 14
HELIX 2 2 THR A 60 SER A 74 1 15
SHEET 1 A 5 GLU A 18 PRO A 25 0
SHEET 2 A 5 ASP A 8 HIS A 15 -1 N HIS A 15 O GLU A 18
SHEET 3 A 5 LEU A 80 ILE A 86 1 O ILE A 82 N LYS A 12
SHEET 4 A 5 MET A 45 TYR A 49 -1 N ASP A 46 O VAL A 85
SHEET 5 A 5 ILE A 56 PRO A 57 -1 O ILE A 56 N TYR A 49
CISPEP 1 ARG A 26 PRO A 27 1 0.03
CISPEP 2 ARG A 26 PRO A 27 2 -0.01
CISPEP 3 ARG A 26 PRO A 27 3 -0.03
CISPEP 4 ARG A 26 PRO A 27 4 -0.04
CISPEP 5 ARG A 26 PRO A 27 5 -0.08
CISPEP 6 ARG A 26 PRO A 27 6 -0.04
CISPEP 7 ARG A 26 PRO A 27 7 0.03
CISPEP 8 ARG A 26 PRO A 27 8 0.09
CISPEP 9 ARG A 26 PRO A 27 9 -0.02
CISPEP 10 ARG A 26 PRO A 27 10 0.00
CISPEP 11 ARG A 26 PRO A 27 11 -0.02
CISPEP 12 ARG A 26 PRO A 27 12 0.03
CISPEP 13 ARG A 26 PRO A 27 13 -0.07
CISPEP 14 ARG A 26 PRO A 27 14 0.02
CISPEP 15 ARG A 26 PRO A 27 15 0.05
CISPEP 16 ARG A 26 PRO A 27 16 -0.04
CISPEP 17 ARG A 26 PRO A 27 17 -0.03
CISPEP 18 ARG A 26 PRO A 27 18 0.05
CISPEP 19 ARG A 26 PRO A 27 19 -0.07
CISPEP 20 ARG A 26 PRO A 27 20 -0.08
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
MODEL 1
Complete list - v 10 2 Bytes