Header list of 1op1.pdb file
Complete list - 8 20 Bytes
HEADER RECEPTOR ASSOCIATED PROTEIN 04-MAR-03 1OP1 TITLE SOLUTION NMR STRUCTURE OF DOMAIN 1 OF RECEPTOR ASSOCIATED PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: ALPHA-2-MACROGLOBULIN RECEPTOR-ASSOCIATED PROTEIN COMPND 3 PRECURSOR; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: DOMAIN 1 OF RECEPTOR ASSOCIATED PROTEIN; COMPND 6 SYNONYM: ALPHA-2-MRAP, LOW DENSITY LIPOPROTEIN RECEPTOR-RELATED COMPND 7 PROTEIN- ASSOCIATED PROTEIN 1, RAP; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: LRPAP1 OR A2MRAP; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: PGEX-2T KEYWDS HELICAL BUNDLE, RECEPTOR ASSOCIATED PROTEIN EXPDTA SOLUTION NMR AUTHOR Y.WU,M.MIGLIORINI,P.YU,D.K.STRICKLAND,Y.-X.WANG REVDAT 3 08-FEB-17 1OP1 1 AUTHOR JRNL VERSN REVDAT 2 24-FEB-09 1OP1 1 VERSN REVDAT 1 26-AUG-03 1OP1 0 JRNL AUTH Y.WU,M.MIGLIORINI,P.YU,D.K.STRICKLAND,Y.X.WANG JRNL TITL 1H, 13C AND 15N RESONANCE ASSIGNMENTS OF DOMAIN 1 OF JRNL TITL 2 RECEPTOR ASSOCIATED PROTEIN. JRNL REF J.BIOMOL.NMR V. 26 187 2003 JRNL REFN ISSN 0925-2738 JRNL PMID 12766414 JRNL DOI 10.1023/A:1023534107920 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NIH-XPLOR 1.0.6 REMARK 3 AUTHORS : ~1.2 MM D1 OF RAP IN A 50 MM~1.2 MM D1 ~1.2 MM D1 REMARK 3 OF RAP INSCHWIETERS, C. D., KUSZEWSKI, J., TJANDRA, REMARK 3 N. AND CLORE, G. M. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1OP1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAR-03. REMARK 100 THE RCSB ID CODE IS RCSB018524. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303.5 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 50 MM NACL, 75 MM NAPI REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : ~1.2 MM 15N/13C ISOTOPE LABELED REMARK 210 D1 OF RAP IN A 50 MM NACL, 75 MM REMARK 210 NAPI, PH 6.5; ~1.2 MM 15N/13C REMARK 210 ISOTPE-LABELED D1 OF RAP IN A 50 REMARK 210 MM NACL, 75 MM NAPI, PH 6.5 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 4D_13C/ REMARK 210 15N-SEPARATED_NOESY; 3D_13C- REMARK 210 SEPARATED_NOESY; HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE, INTERHLX REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS AND REMARK 210 SIMULATED ANNEALING PROTOCOL 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: THE STRUCTURE WAS DETERMINED USING MULTI-DIMENSIONM HETERO REMARK 210 -NUCLEAR NMR SPECTROSCOPY. THE CONSTRAINTS CONSISTS OF NOE, REMARK 210 DIHEDRAL, J-COUPLING, CHEMICAL SHIFT, CONFORMATIONAL DATABASE AS REMARK 210 WELL AS TWO SETS OF DIPOLAR COUPLINGS MEASURED FROM TWO DIFFERENT REMARK 210 ALIGNMENT MEDIA. 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 O LYS A 94 H ALA A 96 1.36 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 20 -154.47 -133.21 REMARK 500 HIS A 36 83.76 50.41 REMARK 500 ASP A 91 -9.45 -44.95 REMARK 500 LYS A 93 -87.52 -140.94 REMARK 500 LYS A 94 -91.89 -87.25 REMARK 500 ASP A 95 -43.35 62.93 REMARK 500 ARG A 97 135.36 62.47 REMARK 500 REMARK 500 REMARK: NULL DBREF 1OP1 A 17 98 UNP P30533 AMRP_HUMAN 51 132 SEQRES 1 A 82 GLY GLU GLU PHE ARG MET GLU LYS LEU ASN GLN LEU TRP SEQRES 2 A 82 GLU LYS ALA GLN ARG LEU HIS LEU PRO PRO VAL ARG LEU SEQRES 3 A 82 ALA GLU LEU HIS ALA ASP LEU LYS ILE GLN GLU ARG ASP SEQRES 4 A 82 GLU LEU ALA TRP LYS LYS LEU LYS LEU ASP GLY LEU ASP SEQRES 5 A 82 GLU ASP GLY GLU LYS GLU ALA ARG LEU ILE ARG ASN LEU SEQRES 6 A 82 ASN VAL ILE LEU ALA LYS TYR GLY LEU ASP GLY LYS LYS SEQRES 7 A 82 ASP ALA ARG GLN HELIX 1 1 MET A 22 HIS A 36 1 15 HELIX 2 2 PRO A 38 GLY A 66 1 29 HELIX 3 3 GLY A 71 GLY A 89 1 19 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 - 8 20 Bytes