Header list of 1qsz.pdb file
Complete list - 2 20 Bytes
HEADER HORMONE/GROWTH FACTOR RECEPTOR 24-JUN-99 1QSZ TITLE THE VEGF-BINDING DOMAIN OF FLT-1 (MINIMIZED MEAN) COMPND MOL_ID: 1; COMPND 2 MOLECULE: VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: SECOND EXTRACELLULAR IMMUNOGLOBULIN-LIKE DOMAIN; COMPND 5 SYNONYM: FLT-1; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 OTHER_DETAILS: MODIFIED QIAGEN PQE30 CONTAINING HIS-TAG AND GENENASE SOURCE 8 CLEAVAGE SITE KEYWDS IMMUNOGLOBULIN-LIKE DOMAIN, I-SET, VEGF RECEPTOR, HORMONE-GROWTH KEYWDS 2 FACTOR RECEPTOR COMPLEX EXPDTA SOLUTION NMR MDLTYP MINIMIZED AVERAGE AUTHOR M.A.STAROVASNIK,H.W.CHRISTINGER,C.WIESMANN,M.A.CHAMPE,A.M.DE VOS, AUTHOR 2 N.J.SKELTON REVDAT 3 02-MAR-22 1QSZ 1 REMARK REVDAT 2 24-FEB-09 1QSZ 1 VERSN REVDAT 1 10-NOV-99 1QSZ 0 JRNL AUTH M.A.STAROVASNIK,H.W.CHRISTINGER,C.WIESMANN,M.A.CHAMPE, JRNL AUTH 2 A.M.DE VOS,N.J.SKELTON JRNL TITL SOLUTION STRUCTURE OF THE VEGF-BINDING DOMAIN OF FLT-1: JRNL TITL 2 COMPARISON OF ITS FREE AND BOUND STATES. JRNL REF J.MOL.BIOL. V. 293 531 1999 JRNL REFN ISSN 0022-2836 JRNL PMID 10543948 JRNL DOI 10.1006/JMBI.1999.3134 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : UXNMR 910901, DISCOVER 95.0 REMARK 3 AUTHORS : BRUKER (UXNMR), MOLECULAR SIMULATIONS, INC. REMARK 3 (DISCOVER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE IS BASED ON A TOTAL OF REMARK 3 2054 NOE-DERIVED DISTANCE RESTRAINTS, 122 DIHEDRAL RESTRAINTS, REMARK 3 AND 44 DISTANCE RESTRAINTS FROM HYDROGEN BONDS. REMARK 4 REMARK 4 1QSZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUN-99. REMARK 100 THE DEPOSITION ID IS D_1000009229. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 5.7 REMARK 210 IONIC STRENGTH : 150MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM FLT-1(DOMAIN2) U-15N,13C; REMARK 210 PHOSPHATE BUFFERED SALINE, PH REMARK 210 5.7; 50UM EDTA; 100UM NAN3; 50UM REMARK 210 DSS; 1MM FLT-1(DOMAIN2) U-15N; REMARK 210 PHOSPHATE BUFFERED SALINE, PH REMARK 210 5.7; 50UM EDTA; 100UM NAN3; 50UM REMARK 210 DSS; 1MM FLT-1(DOMAIN2) 15% 13C; REMARK 210 PHOSPHATE BUFFERED SALINE, PH REMARK 210 5.7; 50UM EDTA; 100UM NAN3; 50UM REMARK 210 DSS REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; HNHA; HNHB; 3D_ REMARK 210 15N_SEPARATED_TOCSY (32 AND 96 REMARK 210 MS); 3D_15N_SEPARATED_ROESY REMARK 210 (40MS) REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : AMX; INOVA REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX 97.0, DGII 95.0, DISCOVER REMARK 210 95.0 REMARK 210 METHOD USED : DISTANCE GEOMETRY/SIMULATED REMARK 210 ANNEALING; MOLECULAR 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: AN ADDITIONAL SAMPLE THAT WAS 15% 13C LABELED WAS USED TO REMARK 210 OBTAIN STEREOSPECIFIC ASSIGNMENTS OF PROCHIRAL METHYL GROUPS. 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 TYR A 139 -168.78 -68.72 REMARK 500 SER A 140 -65.18 -122.92 REMARK 500 GLU A 141 -53.27 -136.57 REMARK 500 THR A 166 94.14 66.46 REMARK 500 LEU A 174 39.66 -140.85 REMARK 500 LYS A 182 -62.45 -139.63 REMARK 500 LYS A 190 -55.13 -147.58 REMARK 500 VAL A 211 -93.90 -84.52 REMARK 500 LEU A 215 99.30 -69.59 REMARK 500 THR A 226 -88.27 -0.47 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1QSV RELATED DB: PDB REMARK 900 ENSEMBLE OF 20 STRUCTURES FROM WHICH THIS MINIMIZED MEAN STRUCTURE REMARK 900 WAS DERIVED. REMARK 900 RELATED ID: 1FLT RELATED DB: PDB REMARK 900 1.7 A RESOLUTION CRYSTAL STRUCTURE OF THE SECOND IMMUNOGLOBULIN- REMARK 900 LIKE DOMAIN OF FLT-1 IN COMPLEX WITH VEGF DBREF 1QSZ A 129 229 UNP P17948 VGFR1_HUMAN 129 229 SEQRES 1 A 101 SER ASP THR GLY ARG PRO PHE VAL GLU MET TYR SER GLU SEQRES 2 A 101 ILE PRO GLU ILE ILE HIS MET THR GLU GLY ARG GLU LEU SEQRES 3 A 101 VAL ILE PRO CYS ARG VAL THR SER PRO ASN ILE THR VAL SEQRES 4 A 101 THR LEU LYS LYS PHE PRO LEU ASP THR LEU ILE PRO ASP SEQRES 5 A 101 GLY LYS ARG ILE ILE TRP ASP SER ARG LYS GLY PHE ILE SEQRES 6 A 101 ILE SER ASN ALA THR TYR LYS GLU ILE GLY LEU LEU THR SEQRES 7 A 101 CYS GLU ALA THR VAL ASN GLY HIS LEU TYR LYS THR ASN SEQRES 8 A 101 TYR LEU THR HIS ARG GLN THR ASN THR ILE HELIX 1 1 SER A 162 THR A 166 5 5 HELIX 2 2 THR A 198 ILE A 202 5 5 SHEET 1 A 5 GLU A 144 MET A 148 0 SHEET 2 A 5 LEU A 215 ARG A 224 1 O ASN A 219 N GLU A 144 SHEET 3 A 5 GLY A 203 THR A 210 -1 O GLY A 203 N THR A 222 SHEET 4 A 5 THR A 168 LYS A 171 -1 N THR A 168 O GLU A 208 SHEET 5 A 5 ASP A 175 THR A 176 -1 N ASP A 175 O LYS A 171 SHEET 1 B 3 LEU A 154 ILE A 156 0 SHEET 2 B 3 GLY A 191 ILE A 194 -1 N PHE A 192 O ILE A 156 SHEET 3 B 3 ILE A 184 ASP A 187 -1 O ILE A 185 N ILE A 193 SSBOND 1 CYS A 158 CYS A 207 1555 1555 2.05 CISPEP 1 PHE A 172 PRO A 173 0 0.50 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 - 2 20 Bytes