Header list of 1abz.pdb file
Complete list - b 16 2 Bytes
HEADER DE NOVO DESIGN 31-JAN-97 1ABZ TITLE ALPHA-T-ALPHA, A DE NOVO DESIGNED PEPTIDE, NMR, 23 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: ALPHA-T-ALPHA; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ATA; COMPND 5 ENGINEERED: YES; COMPND 6 OTHER_DETAILS: DE NOVO DESIGNED PEPTIDE SOURCE MOL_ID: 1 KEYWDS DE NOVO DESIGN, HELIX-TURN-HELIX EXPDTA SOLUTION NMR NUMMDL 23 AUTHOR Y.FEZOUI,P.J.CONNOLLY,J.J.OSTERHOUT REVDAT 4 16-FEB-22 1ABZ 1 REMARK LINK REVDAT 3 19-MAY-09 1ABZ 1 REMARK REVDAT 2 24-FEB-09 1ABZ 1 VERSN REVDAT 1 04-FEB-98 1ABZ 0 JRNL AUTH Y.FEZOUI,P.J.CONNOLLY,J.J.OSTERHOUT JRNL TITL SOLUTION STRUCTURE OF ALPHA T ALPHA, A HELICAL HAIRPIN JRNL TITL 2 PEPTIDE OF DE NOVO DESIGN. JRNL REF PROTEIN SCI. V. 6 1869 1997 JRNL REFN ISSN 0961-8368 JRNL PMID 9300486 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH Y.FEZOUI,D.L.WEAVER,J.J.OSTERHOUT REMARK 1 TITL DE NOVO DESIGN AND STRUCTURAL CHARACTERIZATION OF AN REMARK 1 TITL 2 ALPHA-HELICAL HAIRPIN PEPTIDE: A MODEL SYSTEM FOR THE STUDY REMARK 1 TITL 3 OF PROTEIN FOLDING INTERMEDIATES REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 91 3675 1994 REMARK 1 REFN ISSN 0027-8424 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: THE FAMILY OF 23 STRUCTURES IS REMARK 3 SUPERIMPOSED OVER THE WELL-DEFINED HELICAL REGION ENCOMPASSING REMARK 3 RESIDUES 4 - 16 AND 24 - 34. THE AVERAGE RMSD'S BETWEEN THE 23 REMARK 3 REFINED STRUCTURES AND AVERAGE STRUCTURE ARE AS FOLLOWS: 0.81 REMARK 3 (RESIDUES 4 - 16 AND 24 - 34, BACKBONE ATOMS) 1.48 (RESIDUES 4 - REMARK 3 16 AND 24 - 34, HEAVY ATOMS) 1.08 (ALL BACKBONE ATOMS) 1.77 (ALL REMARK 3 HEAVY ATOMS). REMARK 4 REMARK 4 1ABZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000170637. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 3.6 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY; TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 400 MHZ REMARK 210 SPECTROMETER MODEL : UNITYPLUS REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR REMARK 210 METHOD USED : HYBRID DISTANCE GEOMETRY REMARK 210 DYNAMICAL SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 23 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING HOMONUCLEAR TWO REMARK 210 -DIMENSIONAL NMR 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: 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 19 44.75 -101.42 REMARK 500 1 ASP A 20 55.97 -161.44 REMARK 500 1 SER A 21 36.21 -165.45 REMARK 500 1 LEU A 32 -70.80 -48.09 REMARK 500 1 GLN A 37 42.15 -85.39 REMARK 500 2 ARG A 17 22.73 -143.54 REMARK 500 2 SER A 21 -157.09 -165.95 REMARK 500 2 ALA A 23 -53.75 -143.11 REMARK 500 3 ARG A 17 41.47 -87.45 REMARK 500 4 ARG A 17 67.33 -153.25 REMARK 500 4 THR A 19 81.36 72.80 REMARK 500 5 SER A 21 30.90 -177.40 REMARK 500 6 ALA A 23 -43.55 -130.95 REMARK 500 7 THR A 19 89.81 170.15 REMARK 500 7 ASP A 20 63.85 62.65 REMARK 500 7 SER A 21 41.86 -177.67 REMARK 500 8 VAL A 7 -72.31 -90.39 REMARK 500 8 ALA A 16 -80.57 -53.45 REMARK 500 8 ARG A 17 27.59 48.50 REMARK 500 8 THR A 19 61.36 -108.50 REMARK 500 8 SER A 21 38.40 167.36 REMARK 500 9 THR A 19 51.13 76.63 REMARK 500 9 GLN A 37 -72.07 -54.07 REMARK 500 10 ARG A 17 65.77 -156.77 REMARK 500 10 THR A 19 75.66 47.64 REMARK 500 10 ASP A 20 52.84 75.91 REMARK 500 11 ARG A 17 77.78 176.00 REMARK 500 11 THR A 19 93.73 179.50 REMARK 500 12 ARG A 17 51.04 -101.05 REMARK 500 12 ASP A 20 51.88 -165.04 REMARK 500 12 SER A 21 -169.75 -68.93 REMARK 500 12 ASN A 22 19.35 54.80 REMARK 500 12 ALA A 23 -43.57 -136.85 REMARK 500 13 SER A 21 27.98 -171.86 REMARK 500 14 ARG A 17 53.97 -170.86 REMARK 500 14 THR A 19 22.99 48.52 REMARK 500 14 ASP A 20 48.11 -143.06 REMARK 500 14 SER A 21 34.20 174.64 REMARK 500 14 LEU A 32 -70.42 -58.89 REMARK 500 14 GLN A 37 -76.13 -55.43 REMARK 500 15 THR A 19 74.04 39.64 REMARK 500 15 ASP A 20 54.23 75.63 REMARK 500 15 LEU A 32 -73.32 -74.84 REMARK 500 16 ARG A 17 58.54 -145.38 REMARK 500 16 ASP A 20 65.59 -156.77 REMARK 500 16 SER A 21 32.28 179.61 REMARK 500 16 GLU A 35 -64.62 -90.14 REMARK 500 17 SER A 21 -148.86 -148.14 REMARK 500 17 ALA A 23 -50.94 -145.02 REMARK 500 18 LEU A 14 -75.09 -75.37 REMARK 500 REMARK 500 THIS ENTRY HAS 69 RAMACHANDRAN OUTLIERS. 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 1 ARG A 6 0.30 SIDE CHAIN REMARK 500 1 ARG A 17 0.27 SIDE CHAIN REMARK 500 1 ARG A 26 0.32 SIDE CHAIN REMARK 500 2 ARG A 6 0.31 SIDE CHAIN REMARK 500 2 ARG A 17 0.28 SIDE CHAIN REMARK 500 2 ARG A 26 0.16 SIDE CHAIN REMARK 500 3 ARG A 6 0.22 SIDE CHAIN REMARK 500 3 ARG A 17 0.30 SIDE CHAIN REMARK 500 3 ARG A 26 0.30 SIDE CHAIN REMARK 500 4 ARG A 6 0.24 SIDE CHAIN REMARK 500 4 ARG A 17 0.26 SIDE CHAIN REMARK 500 4 ARG A 26 0.18 SIDE CHAIN REMARK 500 5 ARG A 6 0.24 SIDE CHAIN REMARK 500 5 ARG A 17 0.17 SIDE CHAIN REMARK 500 5 ARG A 26 0.21 SIDE CHAIN REMARK 500 6 ARG A 6 0.20 SIDE CHAIN REMARK 500 6 ARG A 17 0.32 SIDE CHAIN REMARK 500 6 ARG A 26 0.14 SIDE CHAIN REMARK 500 7 ARG A 6 0.27 SIDE CHAIN REMARK 500 7 ARG A 17 0.16 SIDE CHAIN REMARK 500 7 ARG A 26 0.29 SIDE CHAIN REMARK 500 8 ARG A 6 0.21 SIDE CHAIN REMARK 500 8 ARG A 17 0.24 SIDE CHAIN REMARK 500 8 ARG A 26 0.19 SIDE CHAIN REMARK 500 9 ARG A 6 0.10 SIDE CHAIN REMARK 500 9 ARG A 17 0.18 SIDE CHAIN REMARK 500 9 ARG A 26 0.09 SIDE CHAIN REMARK 500 10 ARG A 6 0.27 SIDE CHAIN REMARK 500 10 ARG A 17 0.27 SIDE CHAIN REMARK 500 11 ARG A 6 0.25 SIDE CHAIN REMARK 500 11 ARG A 17 0.31 SIDE CHAIN REMARK 500 12 ARG A 6 0.28 SIDE CHAIN REMARK 500 12 ARG A 17 0.24 SIDE CHAIN REMARK 500 12 ARG A 26 0.32 SIDE CHAIN REMARK 500 13 ARG A 17 0.09 SIDE CHAIN REMARK 500 13 ARG A 26 0.31 SIDE CHAIN REMARK 500 14 ARG A 6 0.29 SIDE CHAIN REMARK 500 14 ARG A 17 0.09 SIDE CHAIN REMARK 500 14 ARG A 26 0.22 SIDE CHAIN REMARK 500 15 ARG A 6 0.26 SIDE CHAIN REMARK 500 15 ARG A 17 0.19 SIDE CHAIN REMARK 500 15 ARG A 26 0.14 SIDE CHAIN REMARK 500 16 ARG A 6 0.32 SIDE CHAIN REMARK 500 16 ARG A 17 0.22 SIDE CHAIN REMARK 500 16 ARG A 26 0.31 SIDE CHAIN REMARK 500 17 ARG A 6 0.22 SIDE CHAIN REMARK 500 17 ARG A 17 0.28 SIDE CHAIN REMARK 500 17 ARG A 26 0.22 SIDE CHAIN REMARK 500 18 ARG A 6 0.30 SIDE CHAIN REMARK 500 18 ARG A 17 0.23 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 64 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 39 DBREF 1ABZ A 0 39 PDB 1ABZ 1ABZ 0 39 SEQRES 1 A 40 SIN ASP TRP LEU LYS ALA ARG VAL GLU GLN GLU LEU GLN SEQRES 2 A 40 ALA LEU GLU ALA ARG GLY THR ASP SER ASN ALA GLU LEU SEQRES 3 A 40 ARG ALA MET GLU ALA LYS LEU LYS ALA GLU ILE GLN LYS SEQRES 4 A 40 NH2 HET SIN A 0 11 HET NH2 A 39 3 HETNAM SIN SUCCINIC ACID HETNAM NH2 AMINO GROUP FORMUL 1 SIN C4 H6 O4 FORMUL 1 NH2 H2 N HELIX 1 1 ASP A 1 ARG A 17 1 17 HELIX 2 2 GLU A 24 GLN A 37 1 14 LINK C4 SIN A 0 N ASP A 1 1555 1555 1.31 LINK C LYS A 38 N NH2 A 39 1555 1555 1.30 SITE 1 AC1 2 GLU A 35 LYS A 38 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 - b 16 2 Bytes