Header list of 1x9x.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSFERASE 24-AUG-04 1X9X
TITLE SOLUTION STRUCTURE OF DIMERIC SAM DOMAIN FROM MAPKKK STE11
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE STE11;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: SAM DOMAIN (RESIDUES 37-104);
COMPND 5 EC: 2.7.1.37;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: STE11;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
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: PET14B
KEYWDS SAM DOMAIN, MAP KINASE, STE11, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 8
AUTHOR S.BHATTACHARJYA,P.XU,R.GINGRAS,R.SHAYKHUTDINOV,C.WU,M.WHITEWAY,F.NI
REVDAT 3 02-MAR-22 1X9X 1 REMARK
REVDAT 2 24-FEB-09 1X9X 1 VERSN
REVDAT 1 30-AUG-05 1X9X 0
JRNL AUTH S.BHATTACHARJYA,P.XU,R.GINGRAS,R.SHAYKHUTDINOV,C.WU,
JRNL AUTH 2 M.WHITEWAY,F.NI
JRNL TITL SOLUTION STRUCTURE OF THE DIMERIC SAM DOMAIN OF MAPKKK STE11
JRNL TITL 2 AND ITS INTERACTIONS WITH THE ADAPTOR PROTEIN STE50 FROM THE
JRNL TITL 3 BUDDING YEAST: IMPLICATIONS FOR STE11 ACTIVATION AND SIGNAL
JRNL TITL 4 TRANSMISSION THROUGH THE STE50-STE11 COMPLEX.
JRNL REF J.MOL.BIOL. V. 344 1071 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15544813
JRNL DOI 10.1016/J.JMB.2004.09.018
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 1.0.6, CYANA 1.0.6
REMARK 3 AUTHORS : GUENTERT (CYANA), GUENTERT (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: TOTAL DISTANT CONSTRAINTS USED, 1, 140,
REMARK 3 INTER-SUBNUINT NOE: 40, INTRA-SUBUNIT NOE:1134, DIHEDRAL ANGLE:60
REMARK 4
REMARK 4 1X9X COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-AUG-04.
REMARK 100 THE DEPOSITION ID IS D_1000030123.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288
REMARK 210 PH : 5.8
REMARK 210 IONIC STRENGTH : 300 MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8 MM STE11 SAM, U-15N, 13C,
REMARK 210 10MM PHOSPHATE BUFFER, 300 MM
REMARK 210 NACL, 90% H2O, 10% D2O; 0.8MM
REMARK 210 STE11 SAM U-15N, 13C MIXED WITH
REMARK 210 UNLABELLED STE11 SAM, 90% H2O,
REMARK 210 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; FILTERED
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANT GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 8
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: STRUCTURE HAS BEEN DETERMINED BY 3-D NMR
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-8
REMARK 465 RES C SSSEQI
REMARK 465 ASP A 1
REMARK 465 GLU A 2
REMARK 465 LYS A 3
REMARK 465 THR A 4
REMARK 465 ASN A 5
REMARK 465 ASP A 6
REMARK 465 ASP B 84
REMARK 465 GLU B 85
REMARK 465 LYS B 86
REMARK 465 THR B 87
REMARK 465 ASN B 88
REMARK 465 ASP B 89
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 10 H LEU A 14 1.45
REMARK 500 O GLY B 137 H LEU B 140 1.48
REMARK 500 O PHE B 109 H ASN B 113 1.48
REMARK 500 O PHE A 26 H ASN A 30 1.50
REMARK 500 O ILE B 142 H SER B 146 1.53
REMARK 500 O GLY A 54 H LEU A 57 1.54
REMARK 500 O TYR A 22 H PHE A 26 1.55
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 PHE A 9 40.72 -150.53
REMARK 500 1 ASN A 30 61.89 100.36
REMARK 500 1 GLU A 34 35.14 -87.35
REMARK 500 1 GLU A 35 -44.08 -147.43
REMARK 500 1 LYS A 52 99.17 -48.28
REMARK 500 1 ASP A 55 -31.18 -37.67
REMARK 500 1 SER A 65 -17.23 -49.41
REMARK 500 1 PHE B 92 82.19 -155.27
REMARK 500 1 CYS B 102 45.54 -142.12
REMARK 500 1 ASN B 113 65.79 97.61
REMARK 500 1 GLU B 118 -44.48 -136.85
REMARK 500 1 VAL B 133 77.72 -119.73
REMARK 500 1 LYS B 135 90.87 -46.90
REMARK 500 1 ASP B 138 -34.40 -37.35
REMARK 500 2 PHE A 9 115.51 -160.21
REMARK 500 2 CYS A 19 37.95 -153.80
REMARK 500 2 ASN A 30 53.90 98.55
REMARK 500 2 GLU A 34 34.02 -91.29
REMARK 500 2 GLU A 35 -44.96 -148.13
REMARK 500 2 LYS A 52 98.70 -51.78
REMARK 500 2 ASP A 55 -30.51 -37.28
REMARK 500 2 GLN A 67 -81.64 -118.51
REMARK 500 2 PHE B 92 52.18 -149.43
REMARK 500 2 CYS B 102 40.71 -143.41
REMARK 500 2 ASN B 113 45.21 99.46
REMARK 500 2 GLU B 117 31.21 -89.89
REMARK 500 2 GLU B 118 -45.82 -139.25
REMARK 500 2 ASP B 124 -168.25 -122.38
REMARK 500 2 LYS B 135 91.68 -46.51
REMARK 500 2 SER B 148 -19.24 -46.62
REMARK 500 3 CYS A 19 32.72 -153.37
REMARK 500 3 ASN A 30 56.36 101.36
REMARK 500 3 GLU A 35 -44.42 -132.27
REMARK 500 3 ASP A 41 -160.21 -100.32
REMARK 500 3 LYS A 52 102.06 -51.30
REMARK 500 3 ASP A 55 -32.70 -35.24
REMARK 500 3 PRO B 91 -89.75 -74.87
REMARK 500 3 ASN B 113 63.83 96.52
REMARK 500 3 VAL B 115 51.08 -109.32
REMARK 500 3 GLU B 117 36.61 34.10
REMARK 500 3 GLU B 118 -44.78 -155.70
REMARK 500 3 LYS B 135 97.32 -54.68
REMARK 500 3 ASP B 138 -34.95 -36.59
REMARK 500 3 GLN B 150 -93.54 -37.26
REMARK 500 4 PHE A 9 59.92 -147.79
REMARK 500 4 CYS A 19 36.27 -146.65
REMARK 500 4 ASN A 30 55.19 95.09
REMARK 500 4 VAL A 32 37.97 -94.28
REMARK 500 4 GLU A 35 -46.86 -131.05
REMARK 500 4 LYS A 52 98.03 -48.75
REMARK 500
REMARK 500 THIS ENTRY HAS 125 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5933 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFTS
DBREF 1X9X A 1 68 UNP P23561 STE11_YEAST 37 104
DBREF 1X9X B 84 151 UNP P23561 STE11_YEAST 37 104
SEQRES 1 A 68 ASP GLU LYS THR ASN ASP LEU PRO PHE VAL GLN LEU PHE
SEQRES 2 A 68 LEU GLU GLU ILE GLY CYS THR GLN TYR LEU ASP SER PHE
SEQRES 3 A 68 ILE GLN CYS ASN LEU VAL THR GLU GLU GLU ILE LYS TYR
SEQRES 4 A 68 LEU ASP LYS ASP ILE LEU ILE ALA LEU GLY VAL ASN LYS
SEQRES 5 A 68 ILE GLY ASP ARG LEU LYS ILE LEU ARG LYS SER LYS SER
SEQRES 6 A 68 PHE GLN ARG
SEQRES 1 B 68 ASP GLU LYS THR ASN ASP LEU PRO PHE VAL GLN LEU PHE
SEQRES 2 B 68 LEU GLU GLU ILE GLY CYS THR GLN TYR LEU ASP SER PHE
SEQRES 3 B 68 ILE GLN CYS ASN LEU VAL THR GLU GLU GLU ILE LYS TYR
SEQRES 4 B 68 LEU ASP LYS ASP ILE LEU ILE ALA LEU GLY VAL ASN LYS
SEQRES 5 B 68 ILE GLY ASP ARG LEU LYS ILE LEU ARG LYS SER LYS SER
SEQRES 6 B 68 PHE GLN ARG
HELIX 1 1 PHE A 9 GLY A 18 1 10
HELIX 2 2 CYS A 19 GLN A 21 5 3
HELIX 3 3 TYR A 22 ASN A 30 1 9
HELIX 4 4 GLU A 35 LEU A 40 5 6
HELIX 5 5 ASP A 41 GLY A 49 1 9
HELIX 6 6 GLY A 54 SER A 65 1 12
HELIX 7 7 PHE B 92 GLU B 98 1 7
HELIX 8 8 CYS B 102 GLN B 104 5 3
HELIX 9 9 TYR B 105 ASN B 113 1 9
HELIX 10 10 LYS B 125 GLY B 132 1 8
HELIX 11 11 GLY B 137 SER B 148 1 12
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 - r 2 2 Bytes