HEADER HORMONE/GROWTH FACTOR/RECEPTOR 12-DEC-03 1RV6 TITLE CRYSTAL STRUCTURE OF PLGF IN COMPLEX WITH DOMAIN 2 OF VEGFR1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PLACENTA GROWTH FACTOR (PLGF); COMPND 3 CHAIN: V, W; COMPND 4 FRAGMENT: RECEPTOR BINDING DOMAIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: FLT1 PROTEIN; COMPND 8 CHAIN: X, Y; COMPND 9 FRAGMENT: DOMAIN-2; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_COMMON: HUMAN; SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 10 EXPRESSION_SYSTEM_COMMON: BACTERIA KEYWDS PLGF, VEGF FAMILY, CYSTINE KNOT, GROWTH FACTOR, LIGAND- KEYWDS 2 RECEPTOR COMPLEX, SPECIFICITY EXPDTA X-RAY DIFFRACTION AUTHOR H.W.CHRISTINGER,G.FUH,A.M.DE VOS,C.WIESMANN REVDAT 2 20-APR-04 1RV6 1 JRNL REMARK MASTER REVDAT 1 20-JAN-04 1RV6 0 JRNL AUTH H.W.CHRISTINGER,G.FUH,A.M.DE VOS,C.WIESMANN JRNL TITL THE CRYSTAL STRUCTURE OF PLACENTAL GROWTH FACTOR JRNL TITL 2 IN COMPLEX WITH DOMAIN 2 OF VASCULAR ENDOTHELIAL JRNL TITL 3 GROWTH FACTOR RECEPTOR-1. JRNL REF J.BIOL.CHEM. V. 279 10382 2004 JRNL REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH C.WIESMANN,G.FUH,C.H.CHRISTINGER,C.EIGENBROT, REMARK 1 AUTH 2 J.A.WELLS,A.M.DE VOS REMARK 1 TITL CRYSTAL STRUCTURE AT 1.7 A RESOLUTION OF VEGF IN REMARK 1 TITL 2 COMPLEX WITH DOMAIN 2 OF THE FLT-1 RECEPTOR REMARK 1 REF CELL (CAMBRIDGE,MASS.) V. 91 695 1997 REMARK 1 REFN ASTM CELLB5 US ISSN 0092-8674 REMARK 1 REFERENCE 2 REMARK 1 AUTH S.IYER,D.DEMETRES,G.LEONIDAS,J.SWAMINATHAN, REMARK 1 AUTH 2 D.MAGLIONE,M.BATTISTI,M.TUCCI,G.PERSICO,K.R.ACHARYA REMARK 1 TITL THE CRYSTAL STRUCTURE OF HUMAN PLACENTA GROWTH REMARK 1 TITL 2 FACTOR-1 (PLGF-1), AN ANGIOGENIC PROTEIN, AT 2.0 A REMARK 1 TITL 3 RESOLUTION. REMARK 1 REF J.BIOL.CHEM. V. 276 12153 2001 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 2 REMARK 2 RESOLUTION. 2.45 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.1.07 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 15482 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.198 REMARK 3 R VALUE (WORKING SET) : 0.194 REMARK 3 FREE R VALUE : 0.260 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.900 REMARK 3 FREE R VALUE TEST SET COUNT : 1153 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 25 REMARK 3 BIN RESOLUTION RANGE HIGH : 2.45 REMARK 3 BIN RESOLUTION RANGE LOW : 2.50 REMARK 3 REFLECTION IN BIN (WORKING SET) : 845 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2460 REMARK 3 BIN FREE R VALUE SET COUNT : 59 REMARK 3 BIN FREE R VALUE : 0.2970 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 ALL ATOMS : 3165 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.66 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.78000 REMARK 3 B22 (A**2) : -0.95000 REMARK 3 B33 (A**2) : 1.74000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.514 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.295 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.198 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.654 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.886 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3078 ; 0.013 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4184 ; 1.556 ; 1.971 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 369 ; 6.686 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 133 ;36.168 ;22.632 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 533 ;18.714 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;17.083 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 479 ; 0.103 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2272 ; 0.005 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1185 ; 0.216 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 180 ; 0.152 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 56 ; 0.173 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.147 ; 0.200 REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1867 ; 3.008 ; 2.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3070 ; 4.649 ; 5.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1211 ; 3.749 ; 2.500 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1114 ; 5.405 ; 5.000 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 4 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : V 22 V 115 REMARK 3 ORIGIN FOR THE GROUP (A): 7.6291 32.8255 17.8849 REMARK 3 T TENSOR REMARK 3 T11: 0.0783 T22: 0.0634 REMARK 3 T33: 0.0164 T12: 0.0192 REMARK 3 T13: -0.0214 T23: 0.0069 REMARK 3 L TENSOR REMARK 3 L11: 9.0822 L22: 1.4092 REMARK 3 L33: 0.9021 L12: 0.9677 REMARK 3 L13: -0.8503 L23: 0.2559 REMARK 3 S TENSOR REMARK 3 S11: 0.1207 S12: -0.3853 S13: 0.3049 REMARK 3 S21: 0.1251 S22: -0.1515 S23: 0.0790 REMARK 3 S31: -0.0687 S32: -0.0004 S33: 0.0307 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : W 21 W 115 REMARK 3 ORIGIN FOR THE GROUP (A): 22.2917 23.7364 19.5114 REMARK 3 T TENSOR REMARK 3 T11: 0.1014 T22: 0.0954 REMARK 3 T33: 0.0718 T12: 0.0112 REMARK 3 T13: -0.0073 T23: 0.0320 REMARK 3 L TENSOR REMARK 3 L11: 8.7291 L22: 1.1355 REMARK 3 L33: 0.0643 L12: 2.8452 REMARK 3 L13: 0.4275 L23: 0.4534 REMARK 3 S TENSOR REMARK 3 S11: 0.1476 S12: -0.3190 S13: -0.1455 REMARK 3 S21: 0.1205 S22: -0.1544 S23: -0.0760 REMARK 3 S31: 0.0932 S32: 0.0069 S33: 0.0068 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : X 133 X 224 REMARK 3 ORIGIN FOR THE GROUP (A): -4.9886 3.5484 12.7052 REMARK 3 T TENSOR REMARK 3 T11: 0.2635 T22: 0.0749 REMARK 3 T33: 0.1206 T12: -0.0617 REMARK 3 T13: -0.0470 T23: 0.0424 REMARK 3 L TENSOR REMARK 3 L11: 3.6224 L22: 2.5549 REMARK 3 L33: 9.7249 L12: 0.6880 REMARK 3 L13: -0.1172 L23: 0.8763 REMARK 3 S TENSOR REMARK 3 S11: 0.0370 S12: -0.0812 S13: -0.2924 REMARK 3 S21: 0.0736 S22: 0.0897 S23: 0.1166 REMARK 3 S31: 0.7811 S32: -0.4831 S33: -0.1267 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : Y 133 Y 224 REMARK 3 ORIGIN FOR THE GROUP (A): 35.5832 49.7000 5.8560 REMARK 3 T TENSOR REMARK 3 T11: 0.3252 T22: 0.1622 REMARK 3 T33: 0.4911 T12: -0.0351 REMARK 3 T13: 0.1198 T23: 0.1021 REMARK 3 L TENSOR REMARK 3 L11: 11.0444 L22: 6.2688 REMARK 3 L33: 10.5123 L12: 0.0652 REMARK 3 L13: -3.9352 L23: -2.2192 REMARK 3 S TENSOR REMARK 3 S11: 0.5986 S12: 0.4017 S13: 1.3665 REMARK 3 S21: -0.3208 S22: -0.0489 S23: -0.6714 REMARK 3 S31: -0.7068 S32: 0.2567 S33: -0.5497 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 1RV6 COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.101 (2007-05-29) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB021062. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-APR-1998 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 6.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL7-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.08 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15482 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.450 REMARK 200 RESOLUTION RANGE LOW (A) : 25.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 200 DATA REDUNDANCY : 4.200 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.04600 REMARK 200 FOR THE DATA SET : 16.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.16100 REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: 1FLT REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.73 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 1/2-X,-Y,1/2+Z REMARK 290 3555 -X,1/2+Y,1/2-Z REMARK 290 4555 1/2+X,1/2-Y,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 27.14050 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 57.67300 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.98950 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 57.67300 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.14050 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.98950 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 APPLY THE FOLLOWING TO CHAINS: V, W, X, Y 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLU V 19 REMARK 465 VAL V 20 REMARK 465 GLU V 21 REMARK 465 ARG V 116 REMARK 465 GLU V 117 REMARK 465 LYS V 118 REMARK 465 MET V 119 REMARK 465 GLU W 19 REMARK 465 VAL W 20 REMARK 465 ARG W 116 REMARK 465 GLU W 117 REMARK 465 LYS W 118 REMARK 465 MET W 119 REMARK 465 ASP X 130 REMARK 465 THR X 131 REMARK 465 GLY X 132 REMARK 465 GLN X 225 REMARK 465 THR X 226 REMARK 465 ASN X 227 REMARK 465 THR X 228 REMARK 465 ILE X 229 REMARK 465 ASP Y 130 REMARK 465 THR Y 131 REMARK 465 GLY Y 132 REMARK 465 GLN Y 225 REMARK 465 THR Y 226 REMARK 465 ASN Y 227 REMARK 465 THR Y 228 REMARK 465 ILE Y 229 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI REMARK 500 OE2 GLU W 27 NH1 ARG W 31 2.15 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 MET W 86 SD MET W 86 CE 0.089 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 LEU V 88 CA - CB - CG ANGL. DEV. = 15.7 DEGREES REMARK 500 LEU W 88 CA - CB - CG ANGL. DEV. = 13.5 DEGREES DBREF 1RV6 V 19 119 UNP P49763 PLGF_HUMAN 37 131 DBREF 1RV6 W 19 119 UNP P49763 PLGF_HUMAN 37 131 DBREF 1RV6 X 130 229 UNP P17948 VGFR1_HUMAN 130 229 DBREF 1RV6 Y 130 229 UNP P17948 VGFR1_HUMAN 130 229 SEQRES 1 V 101 GLU VAL GLU VAL VAL PRO PHE GLN GLU VAL TRP GLY ARG SEQRES 2 V 101 SER TYR CYS ARG ALA LEU GLU ARG LEU VAL ASP VAL VAL SEQRES 3 V 101 SER GLU TYR PRO SER GLU VAL GLU HIS MET PHE SER PRO SEQRES 4 V 101 SER CYS VAL SER LEU LEU ARG CYS THR GLY CYS CYS GLY SEQRES 5 V 101 ASP GLU ASN LEU HIS CYS VAL PRO VAL GLU THR ALA ASN SEQRES 6 V 101 VAL THR MET GLN LEU LEU LYS ILE ARG SER GLY ASP ARG SEQRES 7 V 101 PRO SER TYR VAL GLU LEU THR PHE SER GLN HIS VAL ARG SEQRES 8 V 101 CYS GLU CYS ARG PRO LEU ARG GLU LYS MET SEQRES 1 W 101 GLU VAL GLU VAL VAL PRO PHE GLN GLU VAL TRP GLY ARG SEQRES 2 W 101 SER TYR CYS ARG ALA LEU GLU ARG LEU VAL ASP VAL VAL SEQRES 3 W 101 SER GLU TYR PRO SER GLU VAL GLU HIS MET PHE SER PRO SEQRES 4 W 101 SER CYS VAL SER LEU LEU ARG CYS THR GLY CYS CYS GLY SEQRES 5 W 101 ASP GLU ASN LEU HIS CYS VAL PRO VAL GLU THR ALA ASN SEQRES 6 W 101 VAL THR MET GLN LEU LEU LYS ILE ARG SER GLY ASP ARG SEQRES 7 W 101 PRO SER TYR VAL GLU LEU THR PHE SER GLN HIS VAL ARG SEQRES 8 W 101 CYS GLU CYS ARG PRO LEU ARG GLU LYS MET SEQRES 1 X 100 ASP THR GLY ARG PRO PHE VAL GLU MET TYR SER GLU ILE SEQRES 2 X 100 PRO GLU ILE ILE HIS MET THR GLU GLY ARG GLU LEU VAL SEQRES 3 X 100 ILE PRO CYS ARG VAL THR SER PRO ASN ILE THR VAL THR SEQRES 4 X 100 LEU LYS LYS PHE PRO LEU ASP THR LEU ILE PRO ASP GLY SEQRES 5 X 100 LYS ARG ILE ILE TRP ASP SER ARG LYS GLY PHE ILE ILE SEQRES 6 X 100 SER ASN ALA THR TYR LYS GLU ILE GLY LEU LEU THR CYS SEQRES 7 X 100 GLU ALA THR VAL ASN GLY HIS LEU TYR LYS THR ASN TYR SEQRES 8 X 100 LEU THR HIS ARG GLN THR ASN THR ILE SEQRES 1 Y 100 ASP THR GLY ARG PRO PHE VAL GLU MET TYR SER GLU ILE SEQRES 2 Y 100 PRO GLU ILE ILE HIS MET THR GLU GLY ARG GLU LEU VAL SEQRES 3 Y 100 ILE PRO CYS ARG VAL THR SER PRO ASN ILE THR VAL THR SEQRES 4 Y 100 LEU LYS LYS PHE PRO LEU ASP THR LEU ILE PRO ASP GLY SEQRES 5 Y 100 LYS ARG ILE ILE TRP ASP SER ARG LYS GLY PHE ILE ILE SEQRES 6 Y 100 SER ASN ALA THR TYR LYS GLU ILE GLY LEU LEU THR CYS SEQRES 7 Y 100 GLU ALA THR VAL ASN GLY HIS LEU TYR LYS THR ASN TYR SEQRES 8 Y 100 LEU THR HIS ARG GLN THR ASN THR ILE HET B3P 301 19 HETNAM B3P 2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)- HETNAM 2 B3P PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL FORMUL 5 B3P C11 H26 N2 O6 FORMUL 6 HOH *161(H2 O) HELIX 1 1 PRO V 24 TYR V 33 1 10 HELIX 2 2 VAL V 43 TYR V 47 1 5 HELIX 3 3 PRO W 24 TYR W 33 1 10 HELIX 4 4 VAL W 43 TYR W 47 1 5 HELIX 5 5 PRO W 48 VAL W 51 5 4 HELIX 6 6 THR X 198 ILE X 202 5 5 HELIX 7 7 THR Y 198 ILE Y 202 5 5 SHEET 1 A 2 ARG V 35 ASP V 42 0 SHEET 2 A 2 CYS V 59 THR V 66 -1 O ARG V 64 N LEU V 37 SHEET 1 B 3 MET V 54 SER V 56 0 SHEET 2 B 3 LEU V 74 ILE V 91 -1 O LEU V 89 N SER V 56 SHEET 3 B 3 SER V 98 PRO V 114 -1 O GLN V 106 N ALA V 82 SHEET 1 C 2 ARG W 35 ASP W 42 0 SHEET 2 C 2 CYS W 59 THR W 66 -1 O VAL W 60 N VAL W 41 SHEET 1 D 3 MET W 54 SER W 56 0 SHEET 2 D 3 LEU W 74 ILE W 91 -1 O ILE W 91 N MET W 54 SHEET 3 D 3 SER W 98 PRO W 114 -1 O GLN W 106 N ALA W 82 SHEET 1 E 5 GLU X 144 HIS X 147 0 SHEET 2 E 5 HIS X 214 HIS X 223 1 O LEU X 221 N GLU X 144 SHEET 3 E 5 GLY X 203 VAL X 211 -1 N LEU X 205 O TYR X 220 SHEET 4 E 5 THR X 168 LYS X 171 -1 N LYS X 170 O THR X 206 SHEET 5 E 5 ASP X 175 LEU X 177 -1 O LEU X 177 N LEU X 169 SHEET 1 F 3 LEU X 154 ILE X 156 0 SHEET 2 F 3 GLY X 191 ILE X 194 -1 O ILE X 194 N LEU X 154 SHEET 3 F 3 ILE X 184 ASP X 187 -1 N ILE X 185 O ILE X 193 SHEET 1 G 5 GLU Y 144 HIS Y 147 0 SHEET 2 G 5 LEU Y 215 HIS Y 223 1 O LEU Y 221 N ILE Y 146 SHEET 3 G 5 LEU Y 204 THR Y 210 -1 N ALA Y 209 O TYR Y 216 SHEET 4 G 5 THR Y 168 LYS Y 171 -1 N LYS Y 170 O THR Y 206 SHEET 5 G 5 ASP Y 175 LEU Y 177 -1 O ASP Y 175 N LYS Y 171 SHEET 1 H 3 LEU Y 154 ILE Y 156 0 SHEET 2 H 3 GLY Y 191 ILE Y 194 -1 O ILE Y 194 N LEU Y 154 SHEET 3 H 3 ILE Y 184 ASP Y 187 -1 N ASP Y 187 O GLY Y 191 SSBOND 1 CYS V 59 CYS W 68 SSBOND 2 CYS V 68 CYS W 59 SSBOND 3 CYS V 34 CYS V 76 SSBOND 4 CYS V 65 CYS V 110 SSBOND 5 CYS V 69 CYS V 112 SSBOND 6 CYS W 34 CYS W 76 SSBOND 7 CYS W 65 CYS W 110 SSBOND 8 CYS W 69 CYS W 112 SSBOND 9 CYS X 158 CYS X 207 SSBOND 10 CYS Y 158 CYS Y 207 CISPEP 1 SER V 56 PRO V 57 0 1.41 CISPEP 2 SER W 56 PRO W 57 0 3.73 CISPEP 3 PHE X 172 PRO X 173 0 2.47 CISPEP 4 PHE Y 172 PRO Y 173 0 -1.01 CRYST1 54.281 71.979 115.346 90.00 90.00 90.00 P 21 21 21 8 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 0.018423 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013893 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008670 0.00000