Header list of 1z8s.pdb file
Complete list - t 20 2 Bytes
HEADER TRANSFERASE 31-MAR-05 1Z8S TITLE DNAB BINDING DOMAIN OF DNAG (P16) FROM BACILLUS STEAROTHERMOPHILUS TITLE 2 (RESIDUES 452-597) COMPND MOL_ID: 1; COMPND 2 MOLECULE: DNA PRIMASE; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: P16, RESIDUES 451-597; COMPND 5 EC: 2.7.7.-; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACILLUS STEAROTHERMOPHILUS; SOURCE 3 ORGANISM_TAXID: 1422; SOURCE 4 GENE: DNAG; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21D KEYWDS TWO ALPHA HELICAL SUB-DOMAINS, TRANSFERASE EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR K.SYSON,J.THIRLWAY,A.M.HOUNSLOW,P.SOULTANAS,J.P.WALTHO REVDAT 3 20-OCT-21 1Z8S 1 REMARK SEQADV REVDAT 2 24-FEB-09 1Z8S 1 VERSN REVDAT 1 04-OCT-05 1Z8S 0 JRNL AUTH K.SYSON,J.THIRLWAY,A.M.HOUNSLOW,P.SOULTANAS,J.P.WALTHO JRNL TITL SOLUTION STRUCTURE OF THE HELICASE-INTERACTION DOMAIN OF THE JRNL TITL 2 PRIMASE DNAG: A MODEL FOR HELICASE ACTIVATION JRNL REF STRUCTURE V. 13 609 2005 JRNL REFN ISSN 0969-2126 JRNL PMID 15837199 JRNL DOI 10.1016/J.STR.2005.01.0220.1016 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, CNS 1.1 REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER, ET AL. (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: TOTAL OF 1707 EXPERIMENTALLY DETERMINED REMARK 3 RESTRAINTS, 1439 NOE-DERIVED DISTANCE CONSTRAINTS, 200 DIHEDRAL REMARK 3 ANGLE RESTRAINTS, 68 HYDROGEN BOND DISTANCE RESTRAINTS REMARK 4 REMARK 4 1Z8S COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAY-05. REMARK 100 THE DEPOSITION ID IS D_1000032441. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298; 298; 298 REMARK 210 PH : 6.8; 6.8; 6.8 REMARK 210 IONIC STRENGTH : 20MM POTASSIUM PHOSPHATE, 200MM REMARK 210 SODIUM CHLORIDE; 20MM POTASSIUM REMARK 210 PHOSPHATE, 200MM SODIUM CHLORIDE; REMARK 210 20MM POTASSIUM PHOSPHATE, 200MM REMARK 210 SODIUM CHLORIDE REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM U-15N P16; 1MM U-15N U13C REMARK 210 P16; 0.5MM U-15N P16 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : SIMULTANEOUSLY ACQUIRED 15N- AND REMARK 210 13C-EDITED 3D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX 2000, CNS 1.1 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS FOLLOWED REMARK 210 BY CARTESIAN SLOW-COOL ANNEALING REMARK 210 ENERGY MINIMISATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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: 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 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 LYS A 454 46.14 -105.34 REMARK 500 1 LEU A 456 -75.95 -61.13 REMARK 500 1 LEU A 457 79.62 -163.68 REMARK 500 1 ALA A 459 146.87 -177.88 REMARK 500 1 PHE A 460 48.36 -92.70 REMARK 500 1 ARG A 473 -62.39 -91.15 REMARK 500 1 ILE A 485 -51.28 -143.71 REMARK 500 1 ARG A 488 102.16 -175.80 REMARK 500 1 ASN A 490 47.44 -89.58 REMARK 500 1 GLU A 507 -71.04 -66.53 REMARK 500 1 GLU A 510 118.55 -166.60 REMARK 500 1 ALA A 511 73.04 -65.98 REMARK 500 1 SER A 518 45.07 -101.65 REMARK 500 1 LEU A 533 44.21 -175.06 REMARK 500 1 LEU A 535 58.32 -141.98 REMARK 500 1 VAL A 540 -12.90 74.13 REMARK 500 1 SER A 541 90.32 64.92 REMARK 500 1 PRO A 556 62.09 -67.37 REMARK 500 1 LYS A 575 170.49 72.55 REMARK 500 1 PHE A 577 -79.42 -110.16 REMARK 500 2 LEU A 456 -176.72 62.19 REMARK 500 2 LEU A 457 -52.86 -172.37 REMARK 500 2 PRO A 458 -152.83 -76.61 REMARK 500 2 PHE A 460 -82.17 -124.14 REMARK 500 2 MET A 472 -7.59 -49.46 REMARK 500 2 PHE A 489 -165.81 -62.55 REMARK 500 2 ASN A 490 -68.66 69.41 REMARK 500 2 HIS A 509 34.36 -169.61 REMARK 500 2 GLU A 510 156.52 60.75 REMARK 500 2 ARG A 519 -38.62 -140.98 REMARK 500 2 LEU A 533 49.24 -158.37 REMARK 500 2 LEU A 535 64.83 -153.48 REMARK 500 2 VAL A 540 159.71 68.07 REMARK 500 2 ASN A 554 -166.90 167.60 REMARK 500 2 PRO A 556 159.35 -39.74 REMARK 500 2 LYS A 575 169.72 75.94 REMARK 500 2 PHE A 577 -46.47 178.74 REMARK 500 2 THR A 579 145.20 -178.11 REMARK 500 2 SER A 595 -168.87 51.36 REMARK 500 3 PRO A 458 -170.24 -57.67 REMARK 500 3 ALA A 459 -75.80 -88.05 REMARK 500 3 PHE A 460 44.65 -97.80 REMARK 500 3 MET A 472 -6.26 -58.14 REMARK 500 3 ARG A 473 -69.33 -134.12 REMARK 500 3 ARG A 488 -66.93 -136.53 REMARK 500 3 PHE A 489 -89.41 -162.93 REMARK 500 3 ASN A 490 -163.09 43.45 REMARK 500 3 HIS A 509 12.58 -143.11 REMARK 500 3 ALA A 511 -58.24 69.44 REMARK 500 3 ASP A 512 90.28 65.38 REMARK 500 REMARK 500 THIS ENTRY HAS 213 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 999 REMARK 999 SEQUENCE REMARK 999 ACCORDING TO AUTHORS, RESIDUE 530 IN THE ACTUAL SEQUENCE REMARK 999 IS A GLU AND 531 IS A LEU. THE INITIAL SEQUENCE REMARK 999 SUBMITTED IN THE DATABASE FOR THESE RESIDUES IS INCORRECT. DBREF 1Z8S A 452 597 UNP Q9X4D0 PRIM_BACST 451 597 SEQADV 1Z8S MET A 452 UNP Q9X4D0 LEU 452 ENGINEERED MUTATION SEQADV 1Z8S GLU A 530 UNP Q9X4D0 ASP 530 SEE REMARK 999 SEQADV 1Z8S LEU A 531 UNP Q9X4D0 VAL 531 SEE REMARK 999 SEQRES 1 A 146 MET ALA LYS LYS LEU LEU PRO ALA PHE GLN ASN ALA GLU SEQRES 2 A 146 ARG LEU LEU LEU ALA HIS MET MET ARG SER ARG ASP VAL SEQRES 3 A 146 ALA LEU VAL VAL GLN GLU ARG ILE GLY GLY ARG PHE ASN SEQRES 4 A 146 ILE GLU GLU HIS ARG ALA LEU ALA ALA TYR ILE TYR ALA SEQRES 5 A 146 PHE TYR GLU GLU GLY HIS GLU ALA ASP PRO GLY ALA LEU SEQRES 6 A 146 ILE SER ARG ILE PRO GLY GLU LEU GLN PRO LEU ALA SER SEQRES 7 A 146 GLU LEU SER LEU LEU LEU ILE ALA ASP ASP VAL SER GLU SEQRES 8 A 146 GLN GLU LEU GLU ASP TYR ILE ARG HIS VAL LEU ASN ARG SEQRES 9 A 146 PRO LYS TRP LEU MET LEU LYS VAL LYS GLU GLN GLU LYS SEQRES 10 A 146 THR GLU ALA GLU ARG ARG LYS ASP PHE LEU THR ALA ALA SEQRES 11 A 146 ARG ILE ALA LYS GLU MET ILE GLU MET LYS LYS MET LEU SEQRES 12 A 146 SER SER SER HELIX 1 1 PHE A 460 MET A 472 1 13 HELIX 2 2 SER A 474 ILE A 485 1 12 HELIX 3 3 ILE A 491 GLY A 508 1 18 HELIX 4 4 ASP A 512 ILE A 517 1 6 HELIX 5 5 SER A 518 ILE A 520 5 3 HELIX 6 6 GLU A 523 SER A 532 1 10 HELIX 7 7 SER A 541 ASN A 554 1 14 HELIX 8 8 LYS A 557 ARG A 574 1 18 HELIX 9 9 ALA A 580 SER A 595 1 16 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 - t 20 2 Bytes