Header list of 1rrb.pdb file
Complete list - 2 20 Bytes
HEADER TRANSFERASE 26-MAR-98 1RRB TITLE THE RAS-BINDING DOMAIN OF RAF-1 FROM RAT, NMR, 1 STRUCTURE COMPND MOL_ID: 1; COMPND 2 MOLECULE: RAF PROTO-ONCOGENE SERINE/THREONINE-PROTEIN KINASE; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RAS-BINDING DOMAIN, RESIDUES 56-131; COMPND 5 SYNONYM: RAF-1 RBD; COMPND 6 EC: 2.7.1.-; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: NORWAY RAT; SOURCE 4 ORGANISM_TAXID: 10116; SOURCE 5 CELL_LINE: BL21; 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_PLASMID: PET-RID KEYWDS RAF-1, RAS-BINDING DOMAIN, TRANSFERASE, SERINE/THREONINE-PROTEIN KEYWDS 2 KINASE, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, KEYWDS 3 STRUCTURAL GENOMICS EXPDTA SOLUTION NMR AUTHOR T.TERADA,Y.ITO,M.SHIROUZU,M.TATENO,K.HASHIMOTO,T.KIGAWA,T.EBISUZAKI, AUTHOR 2 K.TAKIO,T.SHIBATA,S.YOKOYAMA,B.O.SMITH,E.D.LAUE,J.A.COOPER,RIKEN AUTHOR 3 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1RRB 1 REMARK REVDAT 2 24-FEB-09 1RRB 1 VERSN REVDAT 1 30-MAR-99 1RRB 0 JRNL AUTH T.TERADA,Y.ITO,M.SHIROUZU,M.TATENO,K.HASHIMOTO,T.KIGAWA, JRNL AUTH 2 T.EBISUZAKI,K.TAKIO,T.SHIBATA,S.YOKOYAMA,B.O.SMITH,E.D.LAUE, JRNL AUTH 3 J.A.COOPER JRNL TITL NUCLEAR MAGNETIC RESONANCE AND MOLECULAR DYNAMICS STUDIES ON JRNL TITL 2 THE INTERACTIONS OF THE RAS-BINDING DOMAIN OF RAF-1 WITH JRNL TITL 3 WILD-TYPE AND MUTANT RAS PROTEINS. JRNL REF J.MOL.BIOL. V. 286 219 1999 JRNL REFN ISSN 0022-2836 JRNL PMID 9931261 JRNL DOI 10.1006/JMBI.1998.2472 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: SIMULATED ANNEALING REFINEMENT FOR NMR REMARK 3 STRUCTURE DETERMINATION REMARK 4 REMARK 4 1RRB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000176186. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 5 MM MGCL2 REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 20 MM SODIUM PHOSPHATE BUFFER REMARK 210 (PH 6.5) REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 1H-1H NOESY; 1H-15N HSQC; 3D 15N REMARK 210 -EDITED NOESY; 3D 15N-EDITED REMARK 210 TOCSY; HMQC-J; 3D HNCA; 3D HCCH- REMARK 210 TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : AMX600 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX 2.3, AZARA 1.0, X-PLOR 3.1 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 80 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : CLOSEST TO THE AVERAGE OF 20 REMARK 210 LEAST ENERGY STRUCTURES REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY ON 13C/15N-LABELED RAF-1 RBD 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 ALA A 38 REMARK 465 SER A 39 REMARK 465 MET A 40 REMARK 465 THR A 41 REMARK 465 GLY A 42 REMARK 465 GLY A 43 REMARK 465 GLN A 44 REMARK 465 GLN A 45 REMARK 465 MET A 46 REMARK 465 GLY A 47 REMARK 465 ARG A 48 REMARK 465 GLY A 49 REMARK 465 SER A 50 REMARK 465 SER A 51 REMARK 465 SER A 52 REMARK 465 LYS A 53 REMARK 465 THR A 54 REMARK 465 SER A 55 REMARK 465 LYS A 132 REMARK 465 LEU A 133 REMARK 465 ALA A 134 REMARK 465 ALA A 135 REMARK 465 ALA A 136 REMARK 465 LEU A 137 REMARK 465 GLU A 138 REMARK 465 HIS A 139 REMARK 465 HIS A 140 REMARK 465 HIS A 141 REMARK 465 HIS A 142 REMARK 465 HIS A 143 REMARK 465 HIS A 144 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 PRO A 63 -177.86 -66.93 REMARK 500 ASN A 64 -85.66 57.61 REMARK 500 LYS A 65 76.13 -170.55 REMARK 500 VAL A 72 66.96 -118.99 REMARK 500 ASN A 74 -85.63 56.51 REMARK 500 MET A 76 89.13 -58.68 REMARK 500 LEU A 91 -153.66 -89.99 REMARK 500 LEU A 102 103.44 -56.17 REMARK 500 HIS A 105 -157.26 -118.38 REMARK 500 LYS A 106 -76.00 -63.88 REMARK 500 TRP A 114 33.86 -96.12 REMARK 500 ASN A 115 23.20 -157.26 REMARK 500 GLU A 124 -166.40 -100.07 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: MY_001000014.1 RELATED DB: TARGETDB DBREF 1RRB A 51 131 UNP P11345 RAF1_RAT 51 131 SEQRES 1 A 107 ALA SER MET THR GLY GLY GLN GLN MET GLY ARG GLY SER SEQRES 2 A 107 SER SER LYS THR SER ASN THR ILE ARG VAL PHE LEU PRO SEQRES 3 A 107 ASN LYS GLN ARG THR VAL VAL ASN VAL ARG ASN GLY MET SEQRES 4 A 107 SER LEU HIS ASP CYS LEU MET LYS ALA LEU LYS VAL ARG SEQRES 5 A 107 GLY LEU GLN PRO GLU CYS CYS ALA VAL PHE ARG LEU LEU SEQRES 6 A 107 GLN GLU HIS LYS GLY LYS LYS ALA ARG LEU ASP TRP ASN SEQRES 7 A 107 THR ASP ALA ALA SER LEU ILE GLY GLU GLU LEU GLN VAL SEQRES 8 A 107 ASP PHE LEU LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS SEQRES 9 A 107 HIS HIS HIS HELIX 1 H1 LEU A 78 ARG A 89 1 12 HELIX 2 H2 ALA A 118 LEU A 121 1 4 SHEET 1 S 5 GLN A 66 ASN A 71 0 SHEET 2 S 5 THR A 57 LEU A 62 -1 N LEU A 62 O GLN A 66 SHEET 3 S 5 GLU A 125 ASP A 129 1 N LEU A 126 O ARG A 59 SHEET 4 S 5 CYS A 96 LEU A 101 -1 N PHE A 99 O GLN A 127 SHEET 5 S 5 LYS A 109 LEU A 112 -1 N ALA A 110 O ARG A 100 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