HEADER IMMUNE SYSTEM 28-OCT-19 6T9D TITLE CRYSTAL STRUCTURE OF A BISPECIFIC DUTAFAB IN COMPLEX WITH HUMAN TITLE 2 VEGF121 COMPND MOL_ID: 1; COMPND 2 MOLECULE: VP MAT DUTAFAB VH CHAIN; COMPND 3 CHAIN: AAA, HHH; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: VH REGION OF DUTAFAB BISPECIFIC MAB; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: VP MAT DUTAFAB VL CHAIN; COMPND 8 CHAIN: BBB, LLL; COMPND 9 ENGINEERED: YES; COMPND 10 OTHER_DETAILS: VL REGION OF DUTAFAB BISPECIFIC FAB; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: VASCULAR ENDOTHELIAL GROWTH FACTOR A; COMPND 13 CHAIN: CCC, DDD; COMPND 14 SYNONYM: VEGF-A,VASCULAR PERMEABILITY FACTOR,VPF; COMPND 15 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: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 19 ORGANISM_COMMON: HUMAN; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 GENE: VEGFA, VEGF; SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS MONOCLONAL ANTIBODY, BISPECIFIC ANTIBODY, FAB FRAGMENT, VEGF, IMMUNE KEYWDS 2 SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR R.KIMBUNG,D.T.LOGAN,R.BECKMANN,K.JENSEN,J.SPECK,S.FENN,H.KETTENBERGER JRNL AUTH R.BECKMANN,K.JENSEN,S.FENN,J.SPECK,K.KRAUSE,A.MEIER,M.ROTH, JRNL AUTH 2 S.FAUSER,R.KIMBUNG,D.T.LOGAN,M.STEEGMAIER,H.KETTENBERGER JRNL TITL DUTAFABS ARE ENGINEERED THERAPEUTIC FAB FRAGMENTS THAT CAN JRNL TITL 2 BIND TWO TARGETS SIMULTANEOUSLY. JRNL REF NAT COMMUN V. 12 708 2021 JRNL REFN ESSN 2041-1723 JRNL PMID 33514724 JRNL DOI 10.1038/S41467-021-20949-3 REMARK 2 REMARK 2 RESOLUTION. 2.91 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0257 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.91 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.29 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9 REMARK 3 NUMBER OF REFLECTIONS : 28317 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.212 REMARK 3 FREE R VALUE : 0.280 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.001 REMARK 3 FREE R VALUE TEST SET COUNT : 1416 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.91 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1898 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.76 REMARK 3 BIN R VALUE (WORKING SET) : 0.3760 REMARK 3 BIN FREE R VALUE SET COUNT : 100 REMARK 3 BIN FREE R VALUE : 0.3920 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 8047 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 213 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 37.50 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.02 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.39600 REMARK 3 B22 (A**2) : 0.70300 REMARK 3 B33 (A**2) : 0.84300 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.88600 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.461 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.432 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.612 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.901 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.808 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8295 ; 0.007 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 7323 ; 0.001 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11276 ; 1.525 ; 1.647 REMARK 3 BOND ANGLES OTHERS (DEGREES): 17124 ; 1.169 ; 1.573 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1077 ;21.628 ; 5.460 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 384 ;36.368 ;23.047 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1313 ;18.883 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 33 ;17.518 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1069 ; 0.055 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10461 ; 0.005 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1713 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1408 ; 0.185 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 55 ; 0.248 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3685 ; 0.168 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 265 ; 0.184 ; 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): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL 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): 4137 ; 2.372 ; 3.752 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4136 ; 2.372 ; 3.752 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5160 ; 3.925 ; 5.618 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5161 ; 3.925 ; 5.618 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4158 ; 2.192 ; 3.892 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4159 ; 2.192 ; 3.893 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6114 ; 3.615 ; 5.748 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6115 ; 3.615 ; 5.749 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL 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 : 3 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : Chains A H REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : Chains B L REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 3 REMARK 3 CHAIN NAMES : Chains C D REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 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 THEIR REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 6T9D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292104471. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-NOV-14 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : MAX II REMARK 200 BEAMLINE : I911-3 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL REMARK 200 OPTICS : KB MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28318 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9 REMARK 200 DATA REDUNDANCY : 3.000 REMARK 200 R MERGE (I) : 0.21200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.10 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2 REMARK 200 DATA REDUNDANCY IN SHELL : 3.00 REMARK 200 R MERGE FOR SHELL (I) : 0.84200 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.500 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 1BJ1, 1JPS REMARK 200 REMARK 200 REMARK: NEEDLES REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.06 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: VEGFA-121 FROM PEPROTECH, CATALOGUE REMARK 280 NUMBER 100-20A, WAS MIXED AT A 1:1 MOLAR RATIO TO VEGF MONOMER. REMARK 280 THE COMPLEX WAS CONCENTRATED TO 11 MG/ML. CRYSTALLIZATION REMARK 280 INVOLVED HANGING DROP VAPOUR DIFFUSION AGAINST 0.1 M MES PH 6.5 REMARK 280 AND 1.6 M MAGNESIUM SULPHATE. CRYSTALS GREW IN ABOUT 120 DAYS REMARK 280 AND WERE FROZEN IN LIQUID NITROGEN WITH 20 % GLYCEROL AS REMARK 280 CRYOPROTECTANT., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 53.93750 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL 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: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 14340 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 44690 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -92.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: AAA, BBB, CCC, DDD, HHH, LLL 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 ASP A 0 REMARK 465 LEU A 1 REMARK 465 SER A 132 REMARK 465 THR A 133 REMARK 465 SER A 134 REMARK 465 GLY A 135 REMARK 465 CYS A 218 REMARK 465 THR A 219 REMARK 465 ALA C 1 REMARK 465 PRO C 2 REMARK 465 MET C 3 REMARK 465 ALA C 4 REMARK 465 GLU C 5 REMARK 465 GLY C 6 REMARK 465 GLY C 7 REMARK 465 GLY C 8 REMARK 465 GLN C 9 REMARK 465 ASN C 10 REMARK 465 HIS C 11 REMARK 465 LYS C 84 REMARK 465 PRO C 85 REMARK 465 HIS C 86 REMARK 465 GLN C 87 REMARK 465 GLY C 88 REMARK 465 LYS C 108 REMARK 465 ASP C 109 REMARK 465 ARG C 110 REMARK 465 ALA C 111 REMARK 465 ARG C 112 REMARK 465 GLN C 113 REMARK 465 GLU C 114 REMARK 465 ASN C 115 REMARK 465 CYS C 116 REMARK 465 ASP C 117 REMARK 465 LYS C 118 REMARK 465 PRO C 119 REMARK 465 ARG C 120 REMARK 465 ARG C 121 REMARK 465 ALA D 1 REMARK 465 PRO D 2 REMARK 465 MET D 3 REMARK 465 ALA D 4 REMARK 465 GLU D 5 REMARK 465 GLY D 6 REMARK 465 GLY D 7 REMARK 465 GLY D 8 REMARK 465 GLN D 9 REMARK 465 ASN D 10 REMARK 465 HIS D 11 REMARK 465 LYS D 108 REMARK 465 ASP D 109 REMARK 465 ARG D 110 REMARK 465 ALA D 111 REMARK 465 ARG D 112 REMARK 465 GLN D 113 REMARK 465 GLU D 114 REMARK 465 ASN D 115 REMARK 465 CYS D 116 REMARK 465 ASP D 117 REMARK 465 LYS D 118 REMARK 465 PRO D 119 REMARK 465 ARG D 120 REMARK 465 ARG D 121 REMARK 465 ASP H 1 REMARK 465 LEU H 2 REMARK 465 SER H 131 REMARK 465 LYS H 132 REMARK 465 SER H 133 REMARK 465 THR H 134 REMARK 465 SER H 135 REMARK 465 GLY H 136 REMARK 465 CYS H 219 REMARK 465 THR H 220 REMARK 465 GLY L 212 REMARK 465 GLU L 213 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 131 CG CD CE NZ 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 DISTANCE REMARK 500 O HOHAA 322 O HOHDD 218 2.07 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 TRPAA 26 -35.52 -25.89 REMARK 500 GLNAA 38 115.30 -164.88 REMARK 500 GLUAA 45 112.55 -160.26 REMARK 500 ARGAA 66 -17.96 -146.17 REMARK 500 ASPAA 73 0.82 -69.49 REMARK 500 ASPAA 74 -60.19 -92.45 REMARK 500 GLUAA 88 -33.22 -31.05 REMARK 500 SERAA 129 -133.52 -86.36 REMARK 500 THRAA 162 -50.97 -129.70 REMARK 500 LYSAA 216 127.48 77.05 REMARK 500 LEUBB 47 -68.11 -109.57 REMARK 500 LYSBB 52 -2.51 -147.19 REMARK 500 HISBB 68 -104.86 47.05 REMARK 500 ALABB 84 -168.37 -171.24 REMARK 500 TYRBB 91 28.49 -141.66 REMARK 500 ASNBB 138 81.20 47.77 REMARK 500 ASNBB 152 -5.58 71.16 REMARK 500 LYSBB 169 -61.15 -98.94 REMARK 500 CYSCC 26 111.51 -30.26 REMARK 500 ASNCC 62 -45.40 95.73 REMARK 500 CYSDD 26 111.15 -31.12 REMARK 500 ASPDD 41 21.08 -58.53 REMARK 500 GLUDD 44 -62.65 -108.64 REMARK 500 ASNDD 62 -49.24 94.11 REMARK 500 GLNDD 87 -122.61 -95.24 REMARK 500 GLNDD 89 120.53 172.79 REMARK 500 TRPHH 27 -34.52 -25.54 REMARK 500 GLUHH 46 112.08 -161.32 REMARK 500 ARGHH 67 -19.48 -143.94 REMARK 500 GLUHH 89 -28.37 -35.15 REMARK 500 ASPHH 100 44.32 -140.02 REMARK 500 THRHH 163 -48.77 -130.38 REMARK 500 LYSHH 217 -99.04 81.63 REMARK 500 HISLL 68 -105.73 47.46 REMARK 500 ALALL 84 -171.98 -170.41 REMARK 500 TYRLL 91 27.48 -141.61 REMARK 500 ASNLL 138 80.98 47.13 REMARK 500 LYSLL 169 -62.56 -97.27 REMARK 500 HISLL 198 139.43 -171.72 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 GLYAA 65 ARGAA 66 -148.94 REMARK 500 GLYHH 66 ARGHH 67 -147.24 REMARK 500 REMARK 500 REMARK: NULL DBREF 6T9DAA 0 219 PDB 6T9D 6T9D 0 219 DBREF 6T9DBB 1 213 PDB 6T9D 6T9D 1 213 DBREF 6T9DCC 1 121 UNP P15692 VEGFA_HUMAN 27 147 DBREF 6T9DDD 1 121 UNP P15692 VEGFA_HUMAN 27 147 DBREF 6T9DHH 1 220 PDB 6T9D 6T9D 1 220 DBREF 6T9DLL 1 213 PDB 6T9D 6T9D 1 213 SEQADV 6T9D ASNCC 115 UNP P15692 LYS 141 CONFLICT SEQADV 6T9D ASNDD 115 UNP P15692 LYS 141 CONFLICT SEQRES 1AA 220 ASP LEU GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2AA 220 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA ASP GLY SEQRES 3AA 220 TRP TRP PHE GLY TYR THR ASP MET SER TRP VAL ARG GLN SEQRES 4AA 220 ALA PRO GLY LYS GLY LEU GLU TRP VAL GLY SER ILE SER SEQRES 5AA 220 TYR LYS GLY GLY SER THR TYR TYR ASN THR LYS PHE ILE SEQRES 6AA 220 GLY ARG PHE THR ILE SER ARG ASP ASP ASP THR ASN THR SEQRES 7AA 220 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8AA 220 ALA VAL TYR TYR CYS ALA ARG ASP ASP GLY TYR PHE ASP SEQRES 9AA 220 THR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SEQRES 10AA 220 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 11AA 220 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 12AA 220 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 13AA 220 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 14AA 220 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 15AA 220 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR LYS SEQRES 16AA 220 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR SEQRES 17AA 220 LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS THR SEQRES 1BB 213 ALA ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2BB 213 SER VAL GLY ASP ARG VAL THR ILE THR CYS HIS GLY SER SEQRES 3BB 213 TYR TRP LEU SER ASN TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4BB 213 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ASP GLY LYS SEQRES 5BB 213 GLU ARG GLU HIS GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6BB 213 GLY SER HIS GLU ASP TYR THR LEU THR ILE SER SER LEU SEQRES 7BB 213 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8BB 213 ARG TYR HIS PRO TYR THR PHE GLY GLN GLY THR LYS LEU SEQRES 9BB 213 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10BB 213 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11BB 213 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12BB 213 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13BB 213 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14BB 213 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15BB 213 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16BB 213 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17BB 213 PHE ASN ARG GLY GLU SEQRES 1CC 121 ALA PRO MET ALA GLU GLY GLY GLY GLN ASN HIS HIS GLU SEQRES 2CC 121 VAL VAL LYS PHE MET ASP VAL TYR GLN ARG SER TYR CYS SEQRES 3CC 121 HIS PRO ILE GLU THR LEU VAL ASP ILE PHE GLN GLU TYR SEQRES 4CC 121 PRO ASP GLU ILE GLU TYR ILE PHE LYS PRO SER CYS VAL SEQRES 5CC 121 PRO LEU MET ARG CYS GLY GLY CYS CYS ASN ASP GLU GLY SEQRES 6CC 121 LEU GLU CYS VAL PRO THR GLU GLU SER ASN ILE THR MET SEQRES 7CC 121 GLN ILE MET ARG ILE LYS PRO HIS GLN GLY GLN HIS ILE SEQRES 8CC 121 GLY GLU MET SER PHE LEU GLN HIS ASN LYS CYS GLU CYS SEQRES 9CC 121 ARG PRO LYS LYS ASP ARG ALA ARG GLN GLU ASN CYS ASP SEQRES 10CC 121 LYS PRO ARG ARG SEQRES 1DD 121 ALA PRO MET ALA GLU GLY GLY GLY GLN ASN HIS HIS GLU SEQRES 2DD 121 VAL VAL LYS PHE MET ASP VAL TYR GLN ARG SER TYR CYS SEQRES 3DD 121 HIS PRO ILE GLU THR LEU VAL ASP ILE PHE GLN GLU TYR SEQRES 4DD 121 PRO ASP GLU ILE GLU TYR ILE PHE LYS PRO SER CYS VAL SEQRES 5DD 121 PRO LEU MET ARG CYS GLY GLY CYS CYS ASN ASP GLU GLY SEQRES 6DD 121 LEU GLU CYS VAL PRO THR GLU GLU SER ASN ILE THR MET SEQRES 7DD 121 GLN ILE MET ARG ILE LYS PRO HIS GLN GLY GLN HIS ILE SEQRES 8DD 121 GLY GLU MET SER PHE LEU GLN HIS ASN LYS CYS GLU CYS SEQRES 9DD 121 ARG PRO LYS LYS ASP ARG ALA ARG GLN GLU ASN CYS ASP SEQRES 10DD 121 LYS PRO ARG ARG SEQRES 1HH 220 ASP LEU GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2HH 220 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA ASP GLY SEQRES 3HH 220 TRP TRP PHE GLY TYR THR ASP MET SER TRP VAL ARG GLN SEQRES 4HH 220 ALA PRO GLY LYS GLY LEU GLU TRP VAL GLY SER ILE SER SEQRES 5HH 220 TYR LYS GLY GLY SER THR TYR TYR ASN THR LYS PHE ILE SEQRES 6HH 220 GLY ARG PHE THR ILE SER ARG ASP ASP ASP THR ASN THR SEQRES 7HH 220 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8HH 220 ALA VAL TYR TYR CYS ALA ARG ASP ASP GLY TYR PHE ASP SEQRES 9HH 220 THR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SEQRES 10HH 220 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 11HH 220 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 12HH 220 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 13HH 220 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 14HH 220 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 15HH 220 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR LYS SEQRES 16HH 220 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR SEQRES 17HH 220 LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS THR SEQRES 1LL 213 ALA ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2LL 213 SER VAL GLY ASP ARG VAL THR ILE THR CYS HIS GLY SER SEQRES 3LL 213 TYR TRP LEU SER ASN TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4LL 213 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ASP GLY LYS SEQRES 5LL 213 GLU ARG GLU HIS GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6LL 213 GLY SER HIS GLU ASP TYR THR LEU THR ILE SER SER LEU SEQRES 7LL 213 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8LL 213 ARG TYR HIS PRO TYR THR PHE GLY GLN GLY THR LYS LEU SEQRES 9LL 213 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10LL 213 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11LL 213 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12LL 213 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13LL 213 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14LL 213 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15LL 213 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16LL 213 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17LL 213 PHE ASN ARG GLY GLU FORMUL 7 HOH *213(H2 O) HELIX 1 AA1 GLYAA 25 THRAA 31 5 7 HELIX 2 AA2 THRAA 61 ILEAA 64 5 4 HELIX 3 AA3 ARGAA 86 THRAA 90 5 5 HELIX 4 AA4 SERAA 158 ALAAA 160 5 3 HELIX 5 AA5 LYSAA 203 ASNAA 206 5 4 HELIX 6 AA6 GLNBB 79 PHEBB 83 5 5 HELIX 7 AA7 SERBB 121 GLYBB 128 1 8 HELIX 8 AA8 LYSBB 183 HISBB 189 1 7 HELIX 9 AA9 LYSCC 16 TYRCC 25 1 10 HELIX 10 AB1 ILECC 35 TYRCC 39 1 5 HELIX 11 AB2 LYSDD 16 TYRDD 25 1 10 HELIX 12 AB3 ILEDD 35 TYRDD 39 1 5 HELIX 13 AB4 GLYHH 26 THRHH 32 5 7 HELIX 14 AB5 THRHH 62 ILEHH 65 5 4 HELIX 15 AB6 ARGHH 87 THRHH 91 5 5 HELIX 16 AB7 SERHH 159 ALAHH 161 5 3 HELIX 17 AB8 LYSHH 204 ASNHH 207 5 4 HELIX 18 AB9 GLNLL 79 PHELL 83 5 5 HELIX 19 AC1 SERLL 121 GLYLL 128 1 8 HELIX 20 AC2 LYSLL 183 HISLL 189 1 7 SHEET 1 AA1 4 LEUAA 3 SERAA 6 0 SHEET 2 AA1 4 LEUAA 17 ALAAA 23 -1 O SERAA 20 N SERAA 6 SHEET 3 AA1 4 THRAA 77 METAA 82 -1 O LEUAA 78 N CYSAA 21 SHEET 4 AA1 4 PHEAA 67 ASPAA 72 -1 N SERAA 70 O TYRAA 79 SHEET 1 AA2 6 GLYAA 9 VALAA 11 0 SHEET 2 AA2 6 THRAA 109 VALAA 113 1 O THRAA 112 N GLYAA 9 SHEET 3 AA2 6 ALAAA 91 ASPAA 98 -1 N TYRAA 93 O THRAA 109 SHEET 4 AA2 6 ASPAA 32 GLNAA 38 -1 N VALAA 36 O TYRAA 94 SHEET 5 AA2 6 LEUAA 44 ILEAA 50 -1 O VALAA 47 N TRPAA 35 SHEET 6 AA2 6 THRAA 57 TYRAA 59 -1 O TYRAA 58 N SERAA 49 SHEET 1 AA3 4 SERAA 122 LEUAA 126 0 SHEET 2 AA3 4 THRAA 137 TYRAA 147 -1 O LEUAA 143 N PHEAA 124 SHEET 3 AA3 4 TYRAA 178 PROAA 187 -1 O TYRAA 178 N TYRAA 147 SHEET 4 AA3 4 VALAA 165 THRAA 167 -1 N HISAA 166 O VALAA 183 SHEET 1 AA4 4 SERAA 122 LEUAA 126 0 SHEET 2 AA4 4 THRAA 137 TYRAA 147 -1 O LEUAA 143 N PHEAA 124 SHEET 3 AA4 4 TYRAA 178 PROAA 187 -1 O TYRAA 178 N TYRAA 147 SHEET 4 AA4 4 VALAA 171 LEUAA 172 -1 N VALAA 171 O SERAA 179 SHEET 1 AA5 3 THRAA 153 TRPAA 156 0 SHEET 2 AA5 3 ILEAA 197 HISAA 202 -1 O ASNAA 199 N SERAA 155 SHEET 3 AA5 3 THRAA 207 LYSAA 212 -1 O THRAA 207 N HISAA 202 SHEET 1 AA6 4 METBB 4 SERBB 7 0 SHEET 2 AA6 4 VALBB 19 GLYBB 25 -1 O THRBB 22 N SERBB 7 SHEET 3 AA6 4 ASPBB 70 ILEBB 75 -1 O TYRBB 71 N CYSBB 23 SHEET 4 AA6 4 PHEBB 62 SERBB 67 -1 N SERBB 63 O THRBB 74 SHEET 1 AA7 6 SERBB 10 ALABB 13 0 SHEET 2 AA7 6 THRBB 102 ILEBB 106 1 O GLUBB 105 N LEUBB 11 SHEET 3 AA7 6 ALABB 84 GLNBB 90 -1 N TYRBB 86 O THRBB 102 SHEET 4 AA7 6 LEUBB 33 GLNBB 38 -1 N TYRBB 36 O TYRBB 87 SHEET 5 AA7 6 LYSBB 45 TYRBB 49 -1 O LYSBB 45 N GLNBB 37 SHEET 6 AA7 6 GLUBB 53 ARGBB 54 -1 O GLUBB 53 N TYRBB 49 SHEET 1 AA8 4 SERBB 10 ALABB 13 0 SHEET 2 AA8 4 THRBB 102 ILEBB 106 1 O GLUBB 105 N LEUBB 11 SHEET 3 AA8 4 ALABB 84 GLNBB 90 -1 N TYRBB 86 O THRBB 102 SHEET 4 AA8 4 THRBB 97 PHEBB 98 -1 O THRBB 97 N GLNBB 90 SHEET 1 AA9 4 SERBB 114 PHEBB 118 0 SHEET 2 AA9 4 THRBB 129 PHEBB 139 -1 O LEUBB 135 N PHEBB 116 SHEET 3 AA9 4 TYRBB 173 SERBB 182 -1 O TYRBB 173 N PHEBB 139 SHEET 4 AA9 4 SERBB 159 VALBB 163 -1 N SERBB 162 O SERBB 176 SHEET 1 AB1 4 ALABB 153 LEUBB 154 0 SHEET 2 AB1 4 LYSBB 145 VALBB 150 -1 N VALBB 150 O ALABB 153 SHEET 3 AB1 4 VALBB 191 THRBB 197 -1 O THRBB 197 N LYSBB 145 SHEET 4 AB1 4 VALBB 205 ASNBB 210 -1 O VALBB 205 N VALBB 196 SHEET 1 AB2 3 VALCC 14 VALCC 15 0 SHEET 2 AB2 3 LEUDD 66 ILEDD 83 1 O GLNDD 79 N VALCC 15 SHEET 3 AB2 3 ILEDD 46 LYSDD 48 -1 N ILEDD 46 O ILEDD 83 SHEET 1 AB3 3 VALCC 14 VALCC 15 0 SHEET 2 AB3 3 LEUDD 66 ILEDD 83 1 O GLNDD 79 N VALCC 15 SHEET 3 AB3 3 GLNDD 89 PRODD 106 -1 O GLNDD 98 N SERDD 74 SHEET 1 AB4 2 HISCC 27 ASPCC 34 0 SHEET 2 AB4 2 CYSCC 51 GLYCC 58 -1 O LEUCC 54 N THRCC 31 SHEET 1 AB5 3 ILECC 46 LYSCC 48 0 SHEET 2 AB5 3 LEUCC 66 ILECC 83 -1 O ILECC 83 N ILECC 46 SHEET 3 AB5 3 HISCC 90 PROCC 106 -1 O GLNCC 98 N SERCC 74 SHEET 1 AB6 3 ILECC 46 LYSCC 48 0 SHEET 2 AB6 3 LEUCC 66 ILECC 83 -1 O ILECC 83 N ILECC 46 SHEET 3 AB6 3 VALDD 14 VALDD 15 1 O VALDD 15 N GLNCC 79 SHEET 1 AB7 2 HISDD 27 ASPDD 34 0 SHEET 2 AB7 2 CYSDD 51 GLYDD 58 -1 O LEUDD 54 N THRDD 31 SHEET 1 AB8 4 LEUHH 4 SERHH 7 0 SHEET 2 AB8 4 LEUHH 18 ALAHH 24 -1 O SERHH 21 N SERHH 7 SHEET 3 AB8 4 THRHH 78 METHH 83 -1 O LEUHH 79 N CYSHH 22 SHEET 4 AB8 4 PHEHH 68 ASPHH 73 -1 N SERHH 71 O TYRHH 80 SHEET 1 AB9 6 LEUHH 11 VALHH 12 0 SHEET 2 AB9 6 THRHH 110 VALHH 114 1 O THRHH 113 N VALHH 12 SHEET 3 AB9 6 ALAHH 92 ASPHH 99 -1 N TYRHH 94 O THRHH 110 SHEET 4 AB9 6 ASPHH 33 GLNHH 39 -1 N VALHH 37 O TYRHH 95 SHEET 5 AB9 6 LEUHH 45 ILEHH 51 -1 O VALHH 48 N TRPHH 36 SHEET 6 AB9 6 THRHH 58 TYRHH 60 -1 O TYRHH 59 N SERHH 50 SHEET 1 AC1 4 SERHH 123 LEUHH 127 0 SHEET 2 AC1 4 THRHH 138 TYRHH 148 -1 O LEUHH 144 N PHEHH 125 SHEET 3 AC1 4 TYRHH 179 PROHH 188 -1 O TYRHH 179 N TYRHH 148 SHEET 4 AC1 4 VALHH 166 THRHH 168 -1 N HISHH 167 O VALHH 184 SHEET 1 AC2 4 SERHH 123 LEUHH 127 0 SHEET 2 AC2 4 THRHH 138 TYRHH 148 -1 O LEUHH 144 N PHEHH 125 SHEET 3 AC2 4 TYRHH 179 PROHH 188 -1 O TYRHH 179 N TYRHH 148 SHEET 4 AC2 4 VALHH 172 LEUHH 173 -1 N VALHH 172 O SERHH 180 SHEET 1 AC3 3 THRHH 154 TRPHH 157 0 SHEET 2 AC3 3 TYRHH 197 HISHH 203 -1 O ASNHH 200 N SERHH 156 SHEET 3 AC3 3 THRHH 208 VALHH 214 -1 O THRHH 208 N HISHH 203 SHEET 1 AC4 4 METLL 4 SERLL 7 0 SHEET 2 AC4 4 VALLL 19 GLYLL 25 -1 O THRLL 22 N SERLL 7 SHEET 3 AC4 4 ASPLL 70 ILELL 75 -1 O TYRLL 71 N CYSLL 23 SHEET 4 AC4 4 PHELL 62 SERLL 67 -1 N SERLL 63 O THRLL 74 SHEET 1 AC5 6 SERLL 10 ALALL 13 0 SHEET 2 AC5 6 THRLL 102 ILELL 106 1 O GLULL 105 N LEULL 11 SHEET 3 AC5 6 ALALL 84 GLNLL 90 -1 N TYRLL 86 O THRLL 102 SHEET 4 AC5 6 LEULL 33 GLNLL 38 -1 N TYRLL 36 O TYRLL 87 SHEET 5 AC5 6 LYSLL 45 TYRLL 49 -1 O LYSLL 45 N GLNLL 37 SHEET 6 AC5 6 GLULL 53 ARGLL 54 -1 O GLULL 53 N TYRLL 49 SHEET 1 AC6 4 SERLL 10 ALALL 13 0 SHEET 2 AC6 4 THRLL 102 ILELL 106 1 O GLULL 105 N LEULL 11 SHEET 3 AC6 4 ALALL 84 GLNLL 90 -1 N TYRLL 86 O THRLL 102 SHEET 4 AC6 4 THRLL 97 PHELL 98 -1 O THRLL 97 N GLNLL 90 SHEET 1 AC7 4 SERLL 114 PHELL 118 0 SHEET 2 AC7 4 THRLL 129 PHELL 139 -1 O LEULL 135 N PHELL 116 SHEET 3 AC7 4 TYRLL 173 SERLL 182 -1 O TYRLL 173 N PHELL 139 SHEET 4 AC7 4 SERLL 159 VALLL 163 -1 N SERLL 162 O SERLL 176 SHEET 1 AC8 4 ALALL 153 GLNLL 155 0 SHEET 2 AC8 4 LYSLL 145 VALLL 150 -1 N VALLL 150 O ALALL 153 SHEET 3 AC8 4 VALLL 191 THRLL 197 -1 O THRLL 197 N LYSLL 145 SHEET 4 AC8 4 VALLL 205 ASNLL 210 -1 O VALLL 205 N VALLL 196 SSBOND 1 CYSAA 21 CYSAA 95 1555 1555 2.04 SSBOND 2 CYSAA 142 CYSAA 198 1555 1555 2.03 SSBOND 3 CYSBB 23 CYSBB 88 1555 1555 2.07 SSBOND 4 CYSBB 134 CYSBB 194 1555 1555 2.08 SSBOND 5 CYSCC 26 CYSCC 68 1555 1555 2.07 SSBOND 6 CYSCC 51 CYSDD 60 1555 1555 2.08 SSBOND 7 CYSCC 57 CYSCC 102 1555 1555 2.09 SSBOND 8 CYSCC 60 CYSDD 51 1555 1555 2.06 SSBOND 9 CYSCC 61 CYSCC 104 1555 1555 2.11 SSBOND 10 CYSDD 26 CYSDD 68 1555 1555 2.09 SSBOND 11 CYSDD 57 CYSDD 102 1555 1555 2.11 SSBOND 12 CYSDD 61 CYSDD 104 1555 1555 2.11 SSBOND 13 CYSHH 22 CYSHH 96 1555 1555 2.01 SSBOND 14 CYSHH 143 CYSHH 199 1555 1555 2.03 SSBOND 15 CYSLL 23 CYSLL 88 1555 1555 2.11 SSBOND 16 CYSLL 134 CYSLL 194 1555 1555 2.04 CISPEP 1 PHEAA 148 PROAA 149 0 -15.68 CISPEP 2 GLUAA 150 PROAA 151 0 0.11 CISPEP 3 SERBB 7 PROBB 8 0 -10.27 CISPEP 4 HISBB 94 PROBB 95 0 -4.62 CISPEP 5 TYRBB 140 PROBB 141 0 -0.47 CISPEP 6 LYSCC 48 PROCC 49 0 -0.71 CISPEP 7 LYSDD 48 PRODD 49 0 0.35 CISPEP 8 PHEHH 149 PROHH 150 0 -17.26 CISPEP 9 GLUHH 151 PROHH 152 0 3.09 CISPEP 10 SERLL 7 PROLL 8 0 -11.36 CISPEP 11 HISLL 94 PROLL 95 0 -1.17 CISPEP 12 TYRLL 140 PROLL 141 0 -1.21 CRYST1 70.080 107.875 87.369 90.00 95.34 90.00 P 1 21 1 4 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 0.014269 0.000000 0.001334 0.00000 SCALE2 0.000000 0.009270 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011496 0.00000