Header list of 1zhc.pdb file
Complete list - r 25 2 Bytes
HEADER UNKNOWN FUNCTION 25-APR-05 1ZHC TITLE SOLUTION STRUCTURE OF HP1242 FROM HELICOBACTER PYLORI COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN HP1242; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: CONSERVED HYPOTHETICAL PROTEIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI; SOURCE 3 ORGANISM_TAXID: 85962; SOURCE 4 STRAIN: 26695; SOURCE 5 GENE: HP1242; 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-21A KEYWDS A-HELICAL PROTEIN, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR S.J.KANG,S.J.PARK,S.J.JUNG,B.J.LEE REVDAT 3 13-JUL-11 1ZHC 1 VERSN REVDAT 2 24-FEB-09 1ZHC 1 VERSN REVDAT 1 06-DEC-05 1ZHC 0 JRNL AUTH S.J.KANG,S.J.PARK,S.J.JUNG,B.J.LEE JRNL TITL SOLUTION STRUCTURE OF HP1242 FROM HELICOBACTER PYLORI JRNL REF PROTEINS V. 61 1111 2005 JRNL REFN ISSN 0887-3585 JRNL PMID 16231304 JRNL DOI 10.1002/PROT.20654 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE, REMARK 3 JIANG,KUSZEWSKI,NILGES,PANNU,READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 1040 RESTRAINTS, 911 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 129 REMARK 3 DIHEDRAL ANGLE RESTRAINTS REMARK 4 REMARK 4 1ZHC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-APR-05. REMARK 100 THE RCSB ID CODE IS RCSB032723. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 6.8 REMARK 210 IONIC STRENGTH : 100MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : U-15N, 13C; 50MM PHOSPHATE REMARK 210 BUFFER, 100MM NACL, 1MM EDTA, PH REMARK 210 6.8; 90% H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N- REMARK 210 SEPARATED_NOESY; HNHA; 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2, NMRVIEW 5, CNS 1.1 REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION REMARK 210 ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE REMARK 210 COVALENT GEOMETRY 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: 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 3 SER A 42 125.39 -172.72 REMARK 500 4 PHE A 2 -52.80 -160.09 REMARK 500 5 PHE A 2 143.09 63.27 REMARK 500 5 SER A 42 132.67 -174.81 REMARK 500 6 HIS A 3 -54.90 -145.47 REMARK 500 8 HIS A 3 -55.43 76.49 REMARK 500 8 SER A 42 117.88 -162.94 REMARK 500 9 SER A 42 118.42 -163.59 REMARK 500 11 PHE A 2 42.47 -158.44 REMARK 500 12 SER A 42 117.61 -162.71 REMARK 500 13 HIS A 3 -72.06 -131.82 REMARK 500 14 PHE A 2 -69.31 -153.54 REMARK 500 14 HIS A 3 -39.78 -177.45 REMARK 500 15 HIS A 3 -72.79 -97.25 REMARK 500 15 SER A 42 116.58 -162.00 REMARK 500 17 PHE A 2 -59.35 -133.23 REMARK 500 17 HIS A 3 -59.07 72.16 REMARK 500 17 ASN A 15 24.88 -154.50 REMARK 500 17 SER A 42 116.60 -162.40 REMARK 500 18 HIS A 3 -50.96 -177.02 REMARK 500 18 SER A 42 118.12 -163.08 REMARK 500 REMARK 500 REMARK: NULL DBREF 1ZHC A 1 76 UNP O25839 O25839_HELPY 1 76 SEQRES 1 A 76 MET PHE HIS GLU PHE ARG ASP GLU ILE SER VAL LEU LYS SEQRES 2 A 76 ALA ASN ASN PRO HIS PHE ASP LYS ILE PHE GLU LYS HIS SEQRES 3 A 76 ASN GLN LEU ASP ASP ASP ILE LYS THR ALA GLU GLN GLN SEQRES 4 A 76 ASN ALA SER ASP ALA GLU VAL SER HIS MET LYS LYS GLN SEQRES 5 A 76 LYS LEU LYS LEU LYS ASP GLU ILE HIS SER MET ILE ILE SEQRES 6 A 76 GLU TYR ARG GLU LYS GLN LYS SER GLU ARG ALA HELIX 1 1 PHE A 2 LEU A 12 1 11 HELIX 2 2 HIS A 18 GLN A 38 1 21 HELIX 3 3 SER A 42 ARG A 75 1 34 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