Header list of 1z1v.pdb file
Complete list - 2 20 Bytes
HEADER CELL CYCLE 06-MAR-05 1Z1V
TITLE NMR STRUCTURE OF THE SACCHAROMYCES CEREVISIAE STE50 SAM DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STE50 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: STE50 SAM DOMAIN (RESIDUES 32-107);
COMPND 5 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: STE50;
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: PET15B;
SOURCE 11 OTHER_DETAILS: THIS PROTEIN FRAGMENT WAS CLONED INTO THE NDEI AND
SOURCE 12 BAMHI SITES OF PET15B CREATING AN AMINOTERMINAL HEXAHISTIDINE TAGGED
SOURCE 13 PROTEIN WITH AN INTERVENING THROMBIN PROTEASE CLEAVAGE SITE. AFTER
SOURCE 14 THROMBIN TREATMENT, THE NON-NATIVE RESIDUES GSH REMAINED AMINO
SOURCE 15 TERMINAL TO THE NATIVE STE50 SEQUENCE
KEYWDS ALL HELIX PROTEIN, SAM DOMAIN, CELL CYCLE
EXPDTA SOLUTION NMR
AUTHOR J.J.KWAN,N.WARNER,J.MAINI,T.PAWSON,L.W.DONALDSON
REVDAT 3 02-MAR-22 1Z1V 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1Z1V 1 VERSN
REVDAT 1 14-FEB-06 1Z1V 0
JRNL AUTH J.J.KWAN,N.WARNER,J.MAINI,K.W.CHAN TUNG,H.ZAKARIA,T.PAWSON,
JRNL AUTH 2 L.W.DONALDSON
JRNL TITL SACCHAROMYCES CEREVISIAE STE50 BINDS THE MAPKKK STE11
JRNL TITL 2 THROUGH A HEAD-TO-TAIL SAM DOMAIN INTERACTION.
JRNL REF J.MOL.BIOL. V. 356 142 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16337230
JRNL DOI 10.1016/J.JMB.2005.11.012
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, XPLOR-NIH 2.9.9
REMARK 3 AUTHORS : DELAGIO (NMRPIPE),
REMARK 3 C.D.SCHWIETERS,J.J.KUSZEWSKI,N.TJANDRA,G.M.CLORE
REMARK 3 (XPLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 EXPERIMENTAL OBSERVATIONS: 615 INTERMOLECULAR NOE DISTANCE
REMARK 3 RESTRAINTS, 328 SHORT RANGE NOE DISTANCE RESTRAINTS, 163 MEDIUM
REMARK 3 RANGE NOE DISTANCE RESTRAINTS, 149 LONG RANGE NOE RESTRAINTS, 42
REMARK 3 PAIRS OF HYDROGEN BOND DISTANCE RESTRAINTS AND 69 PAIRS OF PHI/PSI
REMARK 3 DIHEDRAL ANGLE RESTRAINTS.
REMARK 3 AN INITIAL ENSEMBLE OF 500 STRUCTURES WERE CALCULATED WITH CYANA
REMARK 3 2.0. THE TOP 25 STRUCTURES WITH MINIMUM RESTRAINT VIOLATIONS WERE
REMARK 3 REFINED IN WATER USING XPLOR-NIH AND A PROTOCOL BY C. SPRONK. ALL
REMARK 3 25 WATER REFINED STRUCTURES HAD NO NOE VIOLATIONS > 0.5 A AND NO
REMARK 3 DIHEDRAL VIOLATIONS > 5 DEGREES. FOR RESIDUES 35-100, THE BACKBONE
REMARK 3 RMSD OF THE ENSEMBLE IS 0.75 +/- 0.14 A.
REMARK 3 RESIDUES 28-32 AND 101-107 ARE DISORDERED.
REMARK 4
REMARK 4 1Z1V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032192.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.8
REMARK 210 IONIC STRENGTH : 150 MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.8 MM STE50 SAM U-15N,13C, 20
REMARK 210 MM SODIUM PHOSPHATE BUFFER, PH
REMARK 210 7.8, 150 MM SODIUM CHLORIDE,
REMARK 210 0.02 % SODIUM AZIDE, 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 5.2, CYANA 2.0
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 3D
REMARK 210 HETERONUCLEAR TECHNIQUES
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 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 RES C SSSEQI
REMARK 465 GLY A 28
REMARK 465 SER A 29
REMARK 465 HIS A 30
REMARK 465 MET A 31
REMARK 465 PHE A 32
REMARK 465 LYS A 103
REMARK 465 LEU A 104
REMARK 465 GLU A 105
REMARK 465 TRP A 106
REMARK 465 LYS A 107
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 GLN A 34 70.84 35.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1UQV RELATED DB: PDB
REMARK 900 SIMILAR TO GRIMSHAW SJ ET AL. (2004). J.BIOL.CHEM. 279(3) :2192-2201
DBREF 1Z1V A 32 107 UNP P25344 ST50_YEAST 32 107
SEQADV 1Z1V GLY A 28 UNP P25344 CLONING ARTIFACT
SEQADV 1Z1V SER A 29 UNP P25344 CLONING ARTIFACT
SEQADV 1Z1V HIS A 30 UNP P25344 CLONING ARTIFACT
SEQADV 1Z1V MET A 31 UNP P25344 CLONING ARTIFACT
SEQRES 1 A 80 GLY SER HIS MET PHE SER GLN TRP SER VAL ASP ASP VAL
SEQRES 2 A 80 ILE THR TRP CYS ILE SER THR LEU GLU VAL GLU GLU THR
SEQRES 3 A 80 ASP PRO LEU CYS GLN ARG LEU ARG GLU ASN ASP ILE VAL
SEQRES 4 A 80 GLY ASP LEU LEU PRO GLU LEU CYS LEU GLN ASP CYS GLN
SEQRES 5 A 80 ASP LEU CYS ASP GLY ASP LEU ASN LYS ALA ILE LYS PHE
SEQRES 6 A 80 LYS ILE LEU ILE ASN LYS MET ARG ASP SER LYS LEU GLU
SEQRES 7 A 80 TRP LYS
HELIX 1 1 SER A 36 GLU A 49 1 14
HELIX 2 2 ASP A 54 ASN A 63 1 10
HELIX 3 3 LEU A 69 LEU A 73 5 5
HELIX 4 4 CYS A 74 CYS A 82 1 9
HELIX 5 5 ASP A 85 SER A 102 1 18
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
Complete list - 2 20 Bytes