Header list of 1yg0.pdb file
Complete list - 25 201 Bytes
HEADER METAL TRANSPORT 04-JAN-05 1YG0 TITLE SOLUTION STRUCTURE OF APO-COPP FROM HELICOBACTER PYLORI COMPND MOL_ID: 1; COMPND 2 MOLECULE: COP ASSOCIATED PROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: HPCOPP, COPPER ION BINDING 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: COPP; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DH5A; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-1 KEYWDS OPEN-FACED BETA-SANDWICH, MISSING C-TERMINAL BETA-SHEET, METAL KEYWDS 2 TRANSPORT EXPDTA SOLUTION NMR MDLTYP MINIMIZED AVERAGE AUTHOR B.J.LEE,S.J.PARK REVDAT 3 13-JUL-11 1YG0 1 VERSN REVDAT 2 24-FEB-09 1YG0 1 VERSN REVDAT 1 24-JAN-06 1YG0 0 JRNL AUTH B.J.LEE,S.J.PARK JRNL TITL SOLUTION STRUCTURE OF APO-COPP FROM HELICOBACTER PYLORI JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1, X-PLOR 3.8 REMARK 3 AUTHORS : BRUCKER (CNS), BRUCKER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1250 RESTRAINTS, 1115 ARE REMARK 3 NOE-DERIVED REMARK 3 DISTANCE CONSTRAINTS, 95 DIHEDRAL ANGLE RESTRAINTS, 40 DISTANCE REMARK 3 RESTRAINTS REMARK 3 FROM HYDROGEN BONDS. REMARK 4 REMARK 4 1YG0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-JAN-05. REMARK 100 THE RCSB ID CODE IS RCSB031470. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 7 REMARK 210 IONIC STRENGTH : 500MM NACL, 10MM DTT REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2MM HPCOPP U-15N, 13C; 50MM REMARK 210 PHOSPHATE BUFFER, 10MM DTT, 500MM REMARK 210 NACL NA; 90% H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_13C-SEPARATED_ REMARK 210 NOESY; 3D_15N-SEPARATED_NOESY; REMARK 210 HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CNS 1.1, NMRPIPE 5.4, XWINNMR 3.5 REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION REMARK 210 ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D AND 3D REMARK 210 TECHNIQUES. 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 H SER A 30 O GLU A 44 1.56 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 PHE A 5 -169.79 -128.45 REMARK 500 SER A 9 38.22 -95.99 REMARK 500 ILE A 10 -156.33 -85.37 REMARK 500 THR A 11 53.32 81.05 REMARK 500 PHE A 31 123.23 -170.09 REMARK 500 ASP A 46 -169.97 -78.37 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1CPZ RELATED DB: PDB REMARK 900 HOMOLOGOUS COOPER CHAPERONE REMARK 900 RELATED ID: 1K0V RELATED DB: PDB REMARK 900 HOMOLOGOUS COOPER CHAPERONE DBREF 1YG0 A 1 66 UNP Q48271 COPP_HELPY 1 66 SEQRES 1 A 66 MET LYS ALA THR PHE GLN VAL PRO SER ILE THR CYS ASN SEQRES 2 A 66 HIS CYS VAL ASP LYS ILE GLU LYS PHE VAL GLY GLU ILE SEQRES 3 A 66 GLU GLY VAL SER PHE ILE ASP VAL SER VAL GLU LYS LYS SEQRES 4 A 66 SER VAL VAL VAL GLU PHE ASP ALA PRO ALA THR GLN ASP SEQRES 5 A 66 LEU ILE LYS GLU ALA LEU LEU ASP ALA GLY GLN GLU VAL SEQRES 6 A 66 VAL HELIX 1 1 ASN A 13 GLY A 24 1 12 HELIX 2 2 THR A 50 GLY A 62 1 13 SHEET 1 A 3 LYS A 2 PHE A 5 0 SHEET 2 A 3 SER A 40 PHE A 45 -1 O VAL A 41 N PHE A 5 SHEET 3 A 3 VAL A 29 SER A 35 -1 N SER A 30 O GLU A 44 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 - 25 201 Bytes