Header list of 2ase.pdb file
Complete list - t 20 2 Bytes
HEADER SIGNALING PROTEIN 23-AUG-05 2ASE
TITLE NMR STRUCTURE OF THE F28L MUTANT OF CDC42HS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELL DIVISION CONTROL PROTEIN 42 HOMOLOG;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: G25K GTP-BINDING PROTEIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 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: CDC42;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-CDC42HSF28L
KEYWDS GTP BINDING PROTEIN, G-PROTEIN, CELL SIGNALLING, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR P.D.ADAMS,R.E.OSWALD
REVDAT 5 20-OCT-21 2ASE 1 REMARK SEQADV
REVDAT 4 24-FEB-09 2ASE 1 VERSN
REVDAT 3 07-MAR-06 2ASE 1 JRNL
REVDAT 2 07-MAR-06 2ASE 1 JRNL
REVDAT 1 21-FEB-06 2ASE 0
JRNL AUTH P.D.ADAMS,R.E.OSWALD
JRNL TITL SOLUTION STRUCTURE OF AN ONCOGENIC MUTANT OF CDC42HS
JRNL REF BIOCHEMISTRY V. 45 2577 2006
JRNL REFN ISSN 0006-2960
JRNL PMID 16489751
JRNL DOI 10.1021/BI051686G
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XPLOR-NIH 2.9.0
REMARK 3 AUTHORS : C.D.SCHWIETERS,J.J.KUSZEWSKI,N.TJANDRA,G.M.CLORE
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE WAS DETERMINED USING 978
REMARK 3 DISTANCE RESTRAINTS.
REMARK 4
REMARK 4 2ASE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JAN-06.
REMARK 100 THE DEPOSITION ID IS D_1000034258.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 30 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : U-15N CDC42HS, 25 MM PHOSPHATE
REMARK 210 BUFFER, 5 MM MGCL2, PH 5.5, 90%
REMARK 210 H2O, 10% D2O; U-15N CDC42HS, 25
REMARK 210 MM PHOSPHATE BUFFER, 5 MM MGCL2,
REMARK 210 PH 5.5, 100% D2O; CDC42HS, 25 MM
REMARK 210 PHOSPHATE BUFFER, 5 MM MGCL2, PH
REMARK 210 5.5, 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_TOCSY; 15N-HSQC; 2D
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 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 H GLY A 15 HG1 THR A 115 1.21
REMARK 500 O THR A 161 H LYS A 163 1.48
REMARK 500 O ILE A 21 HG1 THR A 24 1.55
REMARK 500 O SER A 22 H THR A 25 1.57
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 THR A 3 142.19 -39.93
REMARK 500 1 THR A 17 -55.94 -130.37
REMARK 500 1 CYS A 18 -28.58 -34.84
REMARK 500 1 SER A 22 -77.83 -39.85
REMARK 500 1 TYR A 23 -34.72 -39.93
REMARK 500 1 THR A 24 -14.29 -45.95
REMARK 500 1 LYS A 27 131.87 57.84
REMARK 500 1 PRO A 29 -15.86 -38.64
REMARK 500 1 VAL A 33 50.73 -178.18
REMARK 500 1 TYR A 40 19.60 -167.13
REMARK 500 1 ASP A 57 -162.38 -162.33
REMARK 500 1 THR A 58 -112.43 -8.25
REMARK 500 1 ALA A 59 83.83 39.81
REMARK 500 1 ASP A 63 45.48 176.58
REMARK 500 1 TYR A 72 71.17 91.39
REMARK 500 1 VAL A 84 4.24 -63.64
REMARK 500 1 SER A 86 92.16 83.65
REMARK 500 1 PRO A 87 -0.15 -48.11
REMARK 500 1 GLU A 95 -63.24 -106.11
REMARK 500 1 PRO A 106 -76.62 -43.34
REMARK 500 1 GLN A 116 31.04 34.16
REMARK 500 1 ILE A 117 -138.40 24.84
REMARK 500 1 LEU A 119 91.42 66.10
REMARK 500 1 ARG A 120 62.39 5.72
REMARK 500 1 ASP A 121 -96.26 168.54
REMARK 500 1 ASP A 122 -43.50 108.08
REMARK 500 1 ALA A 130 130.60 109.08
REMARK 500 1 LYS A 135 59.94 26.71
REMARK 500 1 THR A 138 -65.29 -133.23
REMARK 500 1 PRO A 139 -73.46 -20.54
REMARK 500 1 LEU A 149 -117.67 -123.48
REMARK 500 1 LYS A 150 69.99 -177.46
REMARK 500 1 ALA A 151 -121.94 -53.13
REMARK 500 1 VAL A 152 -61.16 -155.02
REMARK 500 1 TYR A 154 95.50 -170.03
REMARK 500 1 VAL A 155 -167.28 -171.92
REMARK 500 1 CYS A 157 121.13 -171.76
REMARK 500 1 SER A 158 92.74 -173.88
REMARK 500 1 ALA A 159 31.25 31.34
REMARK 500 1 LEU A 160 -77.45 -164.76
REMARK 500 1 THR A 161 3.45 -58.98
REMARK 500 1 GLN A 162 30.38 -64.80
REMARK 500 1 LEU A 165 -14.09 -41.03
REMARK 500 2 GLN A 2 -148.65 49.68
REMARK 500 2 THR A 3 135.07 -36.83
REMARK 500 2 SER A 22 -80.01 -42.21
REMARK 500 2 THR A 25 -12.53 -151.90
REMARK 500 2 ASN A 26 119.73 53.98
REMARK 500 2 LYS A 27 62.87 61.08
REMARK 500 2 PRO A 29 158.91 -49.05
REMARK 500
REMARK 500 THIS ENTRY HAS 573 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2ASE A 1 178 UNP P60953 CDC42_HUMAN 1 178
SEQADV 2ASE LEU A 28 UNP P60953 PHE 28 ENGINEERED MUTATION
SEQADV 2ASE LYS A 163 UNP P60953 ARG 163 VARIANT
SEQRES 1 A 178 MET GLN THR ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA
SEQRES 2 A 178 VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN
SEQRES 3 A 178 LYS LEU PRO SER GLU TYR VAL PRO THR VAL PHE ASP ASN
SEQRES 4 A 178 TYR ALA VAL THR VAL MET ILE GLY GLY GLU PRO TYR THR
SEQRES 5 A 178 LEU GLY LEU PHE ASP THR ALA GLY GLN GLU ASP TYR ASP
SEQRES 6 A 178 ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE
SEQRES 7 A 178 LEU VAL CYS PHE SER VAL VAL SER PRO SER SER PHE GLU
SEQRES 8 A 178 ASN VAL LYS GLU LYS TRP VAL PRO GLU ILE THR HIS HIS
SEQRES 9 A 178 CYS PRO LYS THR PRO PHE LEU LEU VAL GLY THR GLN ILE
SEQRES 10 A 178 ASP LEU ARG ASP ASP PRO SER THR ILE GLU LYS LEU ALA
SEQRES 11 A 178 LYS ASN LYS GLN LYS PRO ILE THR PRO GLU THR ALA GLU
SEQRES 12 A 178 LYS LEU ALA ARG ASP LEU LYS ALA VAL LYS TYR VAL GLU
SEQRES 13 A 178 CYS SER ALA LEU THR GLN LYS GLY LEU LYS ASN VAL PHE
SEQRES 14 A 178 ASP GLU ALA ILE LEU ALA ALA LEU GLU
HELIX 1 1 SER A 86 LYS A 94 1 9
HELIX 2 2 LYS A 96 CYS A 105 1 10
HELIX 3 3 THR A 125 ALA A 130 1 6
HELIX 4 4 GLU A 140 LEU A 149 1 10
HELIX 5 5 GLY A 164 GLU A 178 1 15
SHEET 1 A 5 VAL A 42 MET A 45 0
SHEET 2 A 5 PRO A 50 GLY A 54 -1 O LEU A 53 N VAL A 42
SHEET 3 A 5 ILE A 4 GLY A 10 1 N ILE A 4 O THR A 52
SHEET 4 A 5 VAL A 77 SER A 83 1 O LEU A 79 N VAL A 9
SHEET 5 A 5 PHE A 110 THR A 115 1 O LEU A 111 N PHE A 78
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 - t 20 2 Bytes