Header list of 1vhp.pdb file
Complete list - r 2 2 Bytes
HEADER IMMUNOGLOBULIN 16-APR-96 1VHP TITLE VH-P8, NMR COMPND MOL_ID: 1; COMPND 2 MOLECULE: VH-P8; COMPND 3 CHAIN: A; COMPND 4 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: CAMELISED HUMAN VH; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: T7; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11A DERIVATIVE; SOURCE 10 EXPRESSION_SYSTEM_GENE: CAMELISED HUMAN VH KEYWDS VH DOMAIN, ANTIBODY, HUMAN, IMMUNOGLOBULIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR L.RIECHMANN REVDAT 3 02-MAR-22 1VHP 1 REMARK SEQADV REVDAT 2 24-FEB-09 1VHP 1 VERSN REVDAT 1 08-NOV-96 1VHP 0 JRNL AUTH L.RIECHMANN JRNL TITL REARRANGEMENT OF THE FORMER VL INTERFACE IN THE SOLUTION JRNL TITL 2 STRUCTURE OF A CAMELISED, SINGLE ANTIBODY VH DOMAIN. JRNL REF J.MOL.BIOL. V. 259 957 1996 JRNL REFN ISSN 0022-2836 JRNL PMID 8683598 JRNL DOI 10.1006/JMBI.1996.0373 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH L.RIECHMANN,J.DAVIES REMARK 1 TITL BACKBONE ASSIGNMENT, SECONDARY STRUCTURE AND PROTEIN A REMARK 1 TITL 2 BINDING OF AN ISOLATED, HUMAN ANTIBODY VH DOMAIN REMARK 1 REF J.BIOMOL.NMR V. 6 141 1995 REMARK 1 REFN ISSN 0925-2738 REMARK 1 REFERENCE 2 REMARK 1 AUTH J.DAVIES,L.RIECHMANN REMARK 1 TITL 'CAMELISING' HUMAN ANTIBODY FRAGMENTS: NMR STUDIES ON VH REMARK 1 TITL 2 DOMAINS REMARK 1 REF FEBS LETT. V. 339 285 1994 REMARK 1 REFN ISSN 0014-5793 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1VHP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000177037. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : NULL REMARK 210 PH : NULL REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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 DBREF 1VHP A 1 117 GB 8489277 AAF75628 1 119 SEQADV 1VHP VAL A 5 GB 8489277 LEU 5 CONFLICT SEQADV 1VHP GLU A 44 GB 8489277 GLY 44 CONFLICT SEQADV 1VHP ARG A 45 GB 8489277 LEU 45 CONFLICT SEQADV 1VHP ILE A 47 GB 8489277 TRP 47 CONFLICT SEQADV 1VHP VAL A 51 GB 8489277 ILE 51 CONFLICT SEQADV 1VHP ARG A 98 GB 8489277 GLU 98 CONFLICT SEQADV 1VHP LEU A 99 GB 8489277 ASP 99 CONFLICT SEQADV 1VHP LYS A 100 GB 8489277 PRO 100 CONFLICT SEQADV 1VHP TYR A 102 GB 8489277 ILE 102 CONFLICT SEQADV 1VHP ALA A 103 GB 8489277 ARG 103 CONFLICT SEQADV 1VHP A GB 8489277 GLY 104 DELETION SEQADV 1VHP A GB 8489277 TYR 105 DELETION SEQRES 1 A 117 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 117 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 A 117 PHE THR PHE SER SER TYR ALA MET SER TRP VAL ARG GLN SEQRES 4 A 117 ALA PRO GLY LYS GLU ARG GLU ILE VAL SER ALA VAL SER SEQRES 5 A 117 GLY SER GLY GLY SER THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 A 117 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 A 117 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 A 117 ALA VAL TYR TYR CYS ALA ARG LEU LYS LYS TYR ALA PHE SEQRES 9 A 117 ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER HELIX 1 1 ASN A 74 LYS A 76 5 3 SHEET 1 A 4 LEU A 4 SER A 7 0 SHEET 2 A 4 LEU A 18 ALA A 24 -1 N ALA A 23 O VAL A 5 SHEET 3 A 4 THR A 78 MET A 83 -1 N MET A 83 O LEU A 18 SHEET 4 A 4 PHE A 68 ILE A 70 -1 N THR A 69 O GLN A 82 SHEET 1 B 2 MET A 34 VAL A 37 0 SHEET 2 B 2 ILE A 47 VAL A 51 -1 N VAL A 51 O MET A 34 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.02 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 2 2 Bytes