Header list of 2a3d.pdb file
Complete list - 6 20 Bytes
HEADER THREE-HELIX BUNDLE 01-APR-99 2A3D TITLE SOLUTION STRUCTURE OF A DE NOVO DESIGNED SINGLE CHAIN THREE-HELIX TITLE 2 BUNDLE (A3D) CAVEAT 2A3D ILE A 14 HAS WRONG CHIRALITY AT ATOM CB ILE A 35 HAS WRONG CAVEAT 2 2A3D CHIRALITY AT ATOM CB COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (DE NOVO THREE-HELIX BUNDLE); COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 3 ORGANISM_TAXID: 32630; SOURCE 4 STRAIN: BL21(DE3); SOURCE 5 CELLULAR_LOCATION: CYTOPLASM; 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: ESCHERICHIA COLI; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-16B; SOURCE 11 EXPRESSION_SYSTEM_GENE: A3D; SOURCE 12 OTHER_DETAILS: SYNTHETIC GENE KEYWDS THREE-HELIX BUNDLE EXPDTA SOLUTION NMR AUTHOR S.T.R.WALSH,H.CHENG,J.W.BRYSON,H.RODER,W.F.DEGRADO REVDAT 4 06-NOV-19 2A3D 1 CAVEAT REMARK REVDAT 3 24-FEB-09 2A3D 1 VERSN REVDAT 2 01-APR-03 2A3D 1 JRNL REVDAT 1 05-MAY-99 2A3D 0 JRNL AUTH S.T.WALSH,H.CHENG,J.W.BRYSON,H.RODER,W.F.DEGRADO JRNL TITL SOLUTION STRUCTURE AND DYNAMICS OF A DE NOVO DESIGNED JRNL TITL 2 THREE-HELIX BUNDLE PROTEIN. JRNL REF PROC.NATL.ACAD.SCI.USA V. 96 5486 1999 JRNL REFN ISSN 0027-8424 JRNL PMID 10318910 JRNL DOI 10.1073/PNAS.96.10.5486 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE REMARK 3 PNAS CITATION REMARK 4 REMARK 4 2A3D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-APR-99. REMARK 100 THE DEPOSITION ID IS D_1000000779. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 5.0 REMARK 210 IONIC STRENGTH : 50 MM SODIUM ACETATE REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 92% WATER/8% D2O AND 99.9% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : TRIPLE RESONANCE REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : DMX; INOVA REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 60 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: LOWEST ENERGY. THE STRUCTURE WAS DETERMINED USING TRIPLE- REMARK 210 RESONANCE NMR SPECTROSCOPY ON 15N, 13C LABELED A3D 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: 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 ALA A 20 -74.62 -97.65 REMARK 500 SER A 24 -82.73 47.07 REMARK 500 GLU A 27 -73.80 -95.52 REMARK 500 LYS A 46 -158.87 -158.89 REMARK 500 LYS A 48 54.26 169.73 REMARK 500 HIS A 72 53.56 -144.77 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG A 10 0.30 SIDE CHAIN REMARK 500 ARG A 17 0.29 SIDE CHAIN REMARK 500 ARG A 57 0.30 SIDE CHAIN REMARK 500 ARG A 64 0.22 SIDE CHAIN REMARK 500 ARG A 71 0.22 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 2A3D A 1 73 PDB 2A3D 2A3D 1 73 SEQRES 1 A 73 MET GLY SER TRP ALA GLU PHE LYS GLN ARG LEU ALA ALA SEQRES 2 A 73 ILE LYS THR ARG LEU GLN ALA LEU GLY GLY SER GLU ALA SEQRES 3 A 73 GLU LEU ALA ALA PHE GLU LYS GLU ILE ALA ALA PHE GLU SEQRES 4 A 73 SER GLU LEU GLN ALA TYR LYS GLY LYS GLY ASN PRO GLU SEQRES 5 A 73 VAL GLU ALA LEU ARG LYS GLU ALA ALA ALA ILE ARG ASP SEQRES 6 A 73 GLU LEU GLN ALA TYR ARG HIS ASN HELIX 1 1 GLY A 2 ALA A 20 1 19 HELIX 2 2 SER A 24 ALA A 26 5 3 HELIX 3 3 LEU A 28 ALA A 44 1 17 HELIX 4 4 VAL A 53 TYR A 70 5 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 - 6 20 Bytes