Header list of 1rhw.pdb file
Complete list - r 2 2 Bytes
HEADER CONTRACTILE PROTEIN 14-NOV-03 1RHW TITLE THE SOLUTION STRUCTURE OF THE PH-INDUCED MONOMER OF DYNEIN LIGHT CHAIN TITLE 2 LC8 FROM DROSOPHILA COMPND MOL_ID: 1; COMPND 2 MOLECULE: DYNEIN LIGHT CHAIN 1, CYTOPLASMIC; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: 8 KDA DYNEIN LIGHT CHAIN, CUT UP PROTEIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER; SOURCE 3 ORGANISM_COMMON: FRUIT FLY; SOURCE 4 ORGANISM_TAXID: 7227; SOURCE 5 GENE: CTP, CDLC1, DDLC1, CG6998; 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: PET-15DA KEYWDS DOMAIN SWAPPED, DIMER INTERFACE, CONTRACTILE PROTEIN EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR M.MAKOKHA,Y.J.HUANG,G.MONTELIONE,A.S.EDISON,E.BARBAR REVDAT 3 02-MAR-22 1RHW 1 REMARK REVDAT 2 24-FEB-09 1RHW 1 VERSN REVDAT 1 27-APR-04 1RHW 0 JRNL AUTH M.MAKOKHA,Y.J.HUANG,G.MONTELIONE,A.S.EDISON,E.BARBAR JRNL TITL THE SOLUTION STRUCTURE OF THE PH-INDUCED MONOMER OF DYNEIN JRNL TITL 2 LIGHT-CHAIN LC8 FROM DROSOPHILA. JRNL REF PROTEIN SCI. V. 13 727 2004 JRNL REFN ISSN 0961-8368 JRNL PMID 14767079 JRNL DOI 10.1110/PS.03462204 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : FELIX 97, AUTOSTRUCTURE 1.1.2, DYANA 1.5 REMARK 3 AUTHORS : ACCELERYS (FELIX), HUANG, MONTELIONE REMARK 3 (AUTOSTRUCTURE), GUNTERT (DYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 1129 RESTRAINTS, 939 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 122 REMARK 3 DIHEDRAL ANGLE RESTRAINTS,68 (2 PER HYDROGEN BOND) DISTANCE REMARK 3 RESTRAINTS FROM HYDROGEN BONDS. STRUCTURE DETERMINATION WAS REMARK 3 PERFORMED ITERATIVELY USING AUTOSTRUCTURE WITH DYANA. REMARK 4 REMARK 4 1RHW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-NOV-03. REMARK 100 THE DEPOSITION ID IS D_1000020755. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 3.0 REMARK 210 IONIC STRENGTH : 50MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.8-1.4MM LC8 PROTEIN REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 15N-NOESY, 13C-NOESY; H/D REMARK 210 EXCHANGE; HNHA; 2D TOCSY, NOESY, REMARK 210 COSY AND CT-HSQC; BACKBONE TR REMARK 210 EXPERIMENTS; 3D TOCSYS REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : DMX; INOVA REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2.1, AUTOASSIGN 1.9 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS, REMARK 210 SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 56 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY 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 O ALA A 28 H TYR A 32 1.49 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 ASP A 3 -167.38 -57.51 REMARK 500 1 ARG A 4 -86.21 -143.46 REMARK 500 1 LYS A 5 -154.98 -175.13 REMARK 500 1 LYS A 9 -84.06 -89.85 REMARK 500 1 ALA A 11 -48.62 -144.68 REMARK 500 1 ASP A 12 73.93 43.72 REMARK 500 1 ALA A 25 -72.13 -65.68 REMARK 500 1 ASP A 47 -33.96 -35.89 REMARK 500 1 LYS A 48 -77.25 -34.99 REMARK 500 1 TYR A 50 -67.69 -141.79 REMARK 500 1 ASN A 51 72.59 -176.05 REMARK 500 1 ARG A 60 -42.40 -155.09 REMARK 500 1 SER A 64 -80.32 -141.16 REMARK 500 1 TYR A 65 -76.34 57.81 REMARK 500 1 THR A 67 -65.68 -155.44 REMARK 500 1 GLU A 69 152.81 -35.96 REMARK 500 1 THR A 70 -145.34 -138.69 REMARK 500 1 ILE A 74 119.14 -160.79 REMARK 500 1 GLN A 80 28.54 -148.14 REMARK 500 2 SER A 2 133.73 72.94 REMARK 500 2 ASP A 3 -159.49 -72.26 REMARK 500 2 ARG A 4 -70.18 -143.23 REMARK 500 2 LYS A 5 -166.83 -172.54 REMARK 500 2 ALA A 6 89.20 -64.76 REMARK 500 2 VAL A 7 159.52 -40.15 REMARK 500 2 LYS A 9 -75.10 -111.00 REMARK 500 2 ALA A 11 -58.72 -148.18 REMARK 500 2 ASP A 12 81.59 55.69 REMARK 500 2 MET A 13 -169.17 -170.29 REMARK 500 2 ALA A 21 -71.66 -67.87 REMARK 500 2 VAL A 22 -34.38 -37.21 REMARK 500 2 LYS A 48 -93.95 -52.41 REMARK 500 2 TYR A 50 -66.58 -137.79 REMARK 500 2 ASN A 51 66.46 -175.54 REMARK 500 2 ARG A 60 -43.47 -155.63 REMARK 500 2 PHE A 62 -142.71 -104.13 REMARK 500 2 TYR A 65 -43.41 -160.34 REMARK 500 2 VAL A 66 44.17 -89.85 REMARK 500 2 THR A 67 -53.52 -153.64 REMARK 500 2 GLU A 69 162.45 64.91 REMARK 500 2 ARG A 71 -70.47 -32.86 REMARK 500 3 SER A 2 -147.92 -101.96 REMARK 500 3 ASP A 3 -155.19 50.31 REMARK 500 3 ALA A 6 -71.24 70.18 REMARK 500 3 VAL A 7 168.72 69.61 REMARK 500 3 LYS A 9 -70.25 -91.54 REMARK 500 3 ALA A 11 -48.20 -150.95 REMARK 500 3 ALA A 25 -72.14 -63.72 REMARK 500 3 LYS A 31 -44.07 -139.94 REMARK 500 3 PHE A 46 -70.10 -75.33 REMARK 500 REMARK 500 THIS ENTRY HAS 212 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1RHW A 1 89 UNP Q24117 DYL1_DROME 1 89 SEQRES 1 A 89 MET SER ASP ARG LYS ALA VAL ILE LYS ASN ALA ASP MET SEQRES 2 A 89 SER GLU GLU MET GLN GLN ASP ALA VAL ASP CYS ALA THR SEQRES 3 A 89 GLN ALA LEU GLU LYS TYR ASN ILE GLU LYS ASP ILE ALA SEQRES 4 A 89 ALA TYR ILE LYS LYS GLU PHE ASP LYS LYS TYR ASN PRO SEQRES 5 A 89 THR TRP HIS CYS ILE VAL GLY ARG ASN PHE GLY SER TYR SEQRES 6 A 89 VAL THR HIS GLU THR ARG HIS PHE ILE TYR PHE TYR LEU SEQRES 7 A 89 GLY GLN VAL ALA ILE LEU LEU PHE LYS SER GLY HELIX 1 1 SER A 14 GLU A 30 1 17 HELIX 2 2 ILE A 34 LYS A 49 1 16 SHEET 1 A 4 ILE A 8 ASN A 10 0 SHEET 2 A 4 PHE A 73 LEU A 78 -1 O TYR A 75 N ASN A 10 SHEET 3 A 4 VAL A 81 PHE A 86 -1 O LEU A 85 N ILE A 74 SHEET 4 A 4 HIS A 55 ILE A 57 -1 N HIS A 55 O PHE A 86 CISPEP 1 PRO A 52 THR A 53 1 0.04 CISPEP 2 PRO A 52 THR A 53 2 0.07 CISPEP 3 PRO A 52 THR A 53 3 -0.07 CISPEP 4 PRO A 52 THR A 53 4 0.06 CISPEP 5 PRO A 52 THR A 53 5 -0.08 CISPEP 6 PRO A 52 THR A 53 6 0.07 CISPEP 7 PRO A 52 THR A 53 7 0.03 CISPEP 8 PRO A 52 THR A 53 8 -0.08 CISPEP 9 PRO A 52 THR A 53 9 -0.06 CISPEP 10 PRO A 52 THR A 53 10 0.05 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