Header list of 1zit.pdb file
Complete list - r 25 2 Bytes
HEADER TRANSCRIPTION REGULATOR 27-APR-05 1ZIT TITLE STRUCTURE OF THE RECEIVER DOMAIN OF NTRC4 FROM AQUIFEX AEOLICUS COMPND MOL_ID: 1; COMPND 2 MOLECULE: TRANSCRIPTIONAL REGULATOR (NTRC FAMILY); COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RECEIVER DOMAIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS; SOURCE 3 ORGANISM_TAXID: 224324; SOURCE 4 STRAIN: VF5; SOURCE 5 GENE: AQ_164; 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: PET21A KEYWDS (BETA/ALPHA)5, TRANSCRIPTION REGULATOR EXPDTA SOLUTION NMR NUMMDL 38 AUTHOR K.MATSUBARA,J.G.PELTON,D.E.WEMMER REVDAT 3 13-JUL-11 1ZIT 1 VERSN REVDAT 2 24-FEB-09 1ZIT 1 VERSN REVDAT 1 09-MAY-06 1ZIT 0 JRNL AUTH K.MATSUBARA,J.G.PELTON,D.E.WEMMER JRNL TITL STRUCTURE AND CONSEQUENCES OF ACTIVIATION OF THE RECEIVER JRNL TITL 2 DOMAIN OF NTRC4 FROM AQUIFEX AEOLICUS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 1.5 REMARK 3 AUTHORS : GUNTERT REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 1155 NOE REMARK 3 RESTRAINTS, 19 HYDROGEN BONDS (38 RESTRAINTS), 57 PHI DIHEDRAL REMARK 3 RESTRAINTS, 11 CHI1 RESTRAINTS, AND 24 1H-15N RESIDUAL DIPOLAR REMARK 3 COUPLING RESTRAINTS. REMARK 4 REMARK 4 1ZIT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAY-05. REMARK 100 THE RCSB ID CODE IS RCSB032761. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 323 REMARK 210 PH : 7 REMARK 210 IONIC STRENGTH : 40 MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM NTRC4R U-15N,13C 10 MM REMARK 210 PHOSPHATE BUFFER PH 7.0. REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C- REMARK 210 SEPARATED_NOESY; HNHA; 2D NOESY; REMARK 210 15N-IPAP-HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CNS 1.1, NMRPIPE LINUX, NMRVIEW REMARK 210 5.0, DYANA 1.5 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 38 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON- REMARK 210 BOND ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 11 REMARK 210 REMARK 210 REMARK: NULL 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 ASP A 9 51.69 -97.32 REMARK 500 1 GLU A 10 127.77 -173.58 REMARK 500 1 GLU A 11 160.26 58.82 REMARK 500 1 SER A 16 -14.31 78.77 REMARK 500 1 ALA A 31 -164.37 -108.48 REMARK 500 1 THR A 33 -172.27 -170.36 REMARK 500 1 GLU A 43 -49.82 -136.96 REMARK 500 1 VAL A 53 42.78 -149.52 REMARK 500 1 TRP A 54 -90.05 -49.90 REMARK 500 1 MET A 55 50.84 -149.60 REMARK 500 1 PRO A 56 -168.29 -75.95 REMARK 500 1 ASP A 57 39.77 -145.40 REMARK 500 1 ASP A 59 -159.52 62.07 REMARK 500 1 SER A 71 65.38 -154.63 REMARK 500 1 VAL A 78 101.14 54.99 REMARK 500 1 LYS A 90 39.92 -89.75 REMARK 500 1 ALA A 91 -42.26 -170.24 REMARK 500 1 GLU A 98 141.02 79.29 REMARK 500 1 LYS A 102 58.70 -179.49 REMARK 500 1 SER A 105 -28.58 171.70 REMARK 500 1 VAL A 106 28.35 41.12 REMARK 500 1 TYR A 120 24.72 -140.83 REMARK 500 2 LYS A 2 -170.13 59.66 REMARK 500 2 ARG A 3 108.81 64.64 REMARK 500 2 ASP A 9 -70.67 -64.04 REMARK 500 2 GLU A 11 69.38 -114.18 REMARK 500 2 THR A 30 122.07 4.33 REMARK 500 2 ALA A 31 -164.17 -102.83 REMARK 500 2 GLU A 43 -58.65 -124.37 REMARK 500 2 VAL A 53 66.92 -67.31 REMARK 500 2 TRP A 54 -96.64 -69.86 REMARK 500 2 SER A 71 75.60 -169.91 REMARK 500 2 VAL A 78 97.35 54.21 REMARK 500 2 THR A 80 114.25 74.98 REMARK 500 2 SER A 84 86.25 -178.13 REMARK 500 2 LYS A 93 -44.01 74.31 REMARK 500 2 ALA A 96 -178.70 -59.56 REMARK 500 2 GLU A 98 157.43 86.65 REMARK 500 2 GLU A 101 -169.84 -65.17 REMARK 500 2 SER A 105 -169.53 66.75 REMARK 500 2 GLU A 119 42.38 -92.59 REMARK 500 2 TYR A 120 31.20 -168.26 REMARK 500 3 ASP A 9 48.83 -88.76 REMARK 500 3 GLU A 10 167.40 179.89 REMARK 500 3 GLU A 11 54.12 -106.35 REMARK 500 3 SER A 16 -63.03 -97.24 REMARK 500 3 GLU A 24 -70.72 -76.49 REMARK 500 3 TYR A 26 -169.31 -129.84 REMARK 500 3 THR A 30 123.64 0.83 REMARK 500 3 ALA A 31 -165.69 -107.77 REMARK 500 REMARK 500 THIS ENTRY HAS 829 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1ZIT A 1 121 UNP O66551 O66551_AQUAE 1 121 SEQRES 1 A 121 MET LYS ARG VAL LEU VAL VAL ASP ASP GLU GLU SER ILE SEQRES 2 A 121 THR SER SER LEU SER ALA ILE LEU GLU GLU GLU GLY TYR SEQRES 3 A 121 HIS PRO ASP THR ALA LYS THR LEU ARG GLU ALA GLU LYS SEQRES 4 A 121 LYS ILE LYS GLU LEU PHE PHE PRO VAL ILE VAL LEU ASP SEQRES 5 A 121 VAL TRP MET PRO ASP GLY ASP GLY VAL ASN PHE ILE ASP SEQRES 6 A 121 PHE ILE LYS GLU ASN SER PRO ASP SER VAL VAL ILE VAL SEQRES 7 A 121 ILE THR GLY HIS GLY SER VAL ASP THR ALA VAL LYS ALA SEQRES 8 A 121 ILE LYS LYS GLY ALA TYR GLU PHE LEU GLU LYS PRO PHE SEQRES 9 A 121 SER VAL GLU ARG PHE LEU LEU THR ILE LYS HIS ALA PHE SEQRES 10 A 121 GLU GLU TYR SER HELIX 1 1 SER A 16 GLY A 25 1 10 HELIX 2 2 THR A 33 LYS A 42 1 10 HELIX 3 3 ASN A 62 SER A 71 1 10 HELIX 4 4 SER A 84 LYS A 93 1 10 HELIX 5 5 VAL A 106 GLU A 118 1 13 HELIX 6 6 GLU A 119 SER A 121 5 3 SHEET 1 A 4 ASP A 29 THR A 30 0 SHEET 2 A 4 VAL A 4 VAL A 7 1 N VAL A 6 O ASP A 29 SHEET 3 A 4 VAL A 48 LEU A 51 1 O VAL A 50 N VAL A 7 SHEET 4 A 4 VAL A 75 VAL A 76 1 O VAL A 75 N ILE A 49 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 25 2 Bytes