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
(ATOM LINES ARE NOT SHOWN.)
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