HEADER IMMUNE SYSTEM 28-OCT-19 6T9E TITLE CRYSTAL STRUCTURE OF A BISPECIFIC DUTAFAB IN COMPLEX WITH HUMAN PDGF COMPND MOL_ID: 1; COMPND 2 MOLECULE: DUTAFAB MAT VH CHAIN; COMPND 3 CHAIN: AAA, HHH; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: DUTAFAB MAT VL CHAIN; COMPND 7 CHAIN: BBB, LLL; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: PLATELET-DERIVED GROWTH FACTOR SUBUNIT B; COMPND 11 CHAIN: CCC, DDD; COMPND 12 SYNONYM: PDGF SUBUNIT B,PDGF-2,PLATELET-DERIVED GROWTH FACTOR B COMPND 13 CHAIN,PLATELET-DERIVED GROWTH FACTOR BETA POLYPEPTIDE,PROTO-ONCOGENE COMPND 14 C-SIS; COMPND 15 ENGINEERED: YES; COMPND 16 OTHER_DETAILS: HUMAN PLATELET-DERIVED GROWTH FACTOR SUBUNIT B COMPND 17 PURCHASED FROM PEPROTECH 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: PDGFB, PDGF2, SIS; SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS MONOCLONAL ANTIBODY, BISPECIFIC ANTIBODY, FAB FRAGMENT, PDGF, 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. 2.99 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) : 2.99 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.74 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8 REMARK 3 NUMBER OF REFLECTIONS : 29016 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) : 0.253 REMARK 3 FREE R VALUE : 0.304 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.001 REMARK 3 FREE R VALUE TEST SET COUNT : 1451 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) : 2.99 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.07 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1732 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.35 REMARK 3 BIN R VALUE (WORKING SET) : 0.4600 REMARK 3 BIN FREE R VALUE SET COUNT : 91 REMARK 3 BIN FREE R VALUE : 0.5250 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 7935 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 43.90 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.92 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 6.66900 REMARK 3 B22 (A**2) : -3.40500 REMARK 3 B33 (A**2) : 1.18700 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -6.37200 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): 0.500 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.743 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 49.230 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.920 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.875 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8136 ; 0.006 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11059 ; 1.448 ; 1.641 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1013 ; 8.151 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 385 ;35.015 ;22.312 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1326 ;19.121 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 44 ;16.836 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1066 ; 0.108 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6174 ; 0.006 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3568 ; 0.261 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5423 ; 0.312 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 285 ; 0.183 ; 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): 4085 ; 5.489 ; 6.290 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5087 ; 8.908 ; 9.425 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4051 ; 5.338 ; 6.231 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5972 ; 8.836 ; 9.288 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL 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 : 1 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : Chains A H Chains B L Chains REMARK 3 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 6T9E 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_1292104964. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 03-MAY-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I03 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9760 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29016 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.989 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 (%) : 97.7 REMARK 200 DATA REDUNDANCY : 3.000 REMARK 200 R MERGE (I) : 0.16200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.99 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.20 REMARK 200 COMPLETENESS FOR SHELL (%) : 92.8 REMARK 200 DATA REDUNDANCY IN SHELL : 3.00 REMARK 200 R MERGE FOR SHELL (I) : 0.77300 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.800 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: 4QCI REMARK 200 REMARK 200 REMARK: PLATES REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 43.50 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: DUTAFAB AND PDGF-BB (PEPROTECH, REMARK 280 CATALOGUE NUMBER 100-13A) WERE MIXED AT A 1:1 MOLAR RATIO IN REMARK 280 RELATION TO PDGF MONOMER. THE COMPLEX WAS CONCENTRATED TO 12 MG/ REMARK 280 ML AND CRYSTALLIZATION WAS PERFORMED BY HANGING DROP VAPOUR REMARK 280 DIFFUSION AGAINST 0.1 M TRIS PH 7.5, 42 % 2-METHYL-2,4- REMARK 280 PENTANEDIOL (MPD) AT 20 C. PLATE-SHAPED CRYSTALS GREW WITHIN A REMARK 280 FEW WEEKS AND WERE FROZEN IN LIQUID NITROGEN WITH 20% GLYCEROL REMARK 280 AS CRYO-PROTECTANT., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 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 37.73700 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: 12190 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 46940 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -79.0 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 SER A 190 REMARK 465 SER A 191 REMARK 465 LEU A 192 REMARK 465 GLY A 193 REMARK 465 THR A 194 REMARK 465 LYS A 195 REMARK 465 THR A 196 REMARK 465 LYS A 217 REMARK 465 SER A 218 REMARK 465 CYS A 219 REMARK 465 THR A 220 REMARK 465 LYS B 190 REMARK 465 VAL B 191 REMARK 465 TYR B 192 REMARK 465 ARG B 211 REMARK 465 GLY B 212 REMARK 465 GLU B 213 REMARK 465 CYS B 214 REMARK 465 SER C 1 REMARK 465 LEU C 2 REMARK 465 GLY C 3 REMARK 465 SER C 4 REMARK 465 LEU C 5 REMARK 465 THR C 6 REMARK 465 VAL C 102 REMARK 465 ALA C 103 REMARK 465 ALA C 104 REMARK 465 ALA C 105 REMARK 465 ARG C 106 REMARK 465 PRO C 107 REMARK 465 VAL C 108 REMARK 465 THR C 109 REMARK 465 SER D 1 REMARK 465 LEU D 2 REMARK 465 GLY D 3 REMARK 465 SER D 4 REMARK 465 LEU D 5 REMARK 465 THR D 6 REMARK 465 ALA D 103 REMARK 465 ALA D 104 REMARK 465 ALA D 105 REMARK 465 ARG D 106 REMARK 465 PRO D 107 REMARK 465 VAL D 108 REMARK 465 THR D 109 REMARK 465 SER H 190 REMARK 465 SER H 191 REMARK 465 LEU H 192 REMARK 465 GLY H 193 REMARK 465 THR H 194 REMARK 465 LYS H 195 REMARK 465 THR H 196 REMARK 465 LYS H 217 REMARK 465 SER H 218 REMARK 465 CYS H 219 REMARK 465 THR H 220 REMARK 465 LYS L 190 REMARK 465 ASN L 210 REMARK 465 ARG L 211 REMARK 465 GLY L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 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 ILE C 7 CG1 CG2 CD1 REMARK 470 ILE D 7 CG1 CG2 CD1 REMARK 470 VAL L 191 CG1 CG2 REMARK 470 TYR L 192 CG CD1 CD2 CE1 CE2 CZ OH 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 CD2 TYRHH 197 O VALHH 214 2.00 REMARK 500 CE2 TYRHH 197 O VALHH 214 2.11 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 GLNAA 39 114.12 -167.86 REMARK 500 THRAA 91 108.04 -54.63 REMARK 500 PHEAA 103 75.18 52.47 REMARK 500 SERAA 115 143.23 -171.32 REMARK 500 SERAA 116 70.67 -104.29 REMARK 500 SERAA 130 133.37 169.83 REMARK 500 SERAA 131 -77.47 49.43 REMARK 500 SERAA 135 -109.51 21.35 REMARK 500 LEUBB 47 -60.03 -108.65 REMARK 500 LYSBB 52 -12.54 -146.81 REMARK 500 PROBB 59 151.87 -45.77 REMARK 500 HISBB 68 -101.90 55.25 REMARK 500 ALABB 84 -173.41 -175.24 REMARK 500 TYRBB 91 36.72 -150.14 REMARK 500 SERBB 127 -172.00 -69.17 REMARK 500 ASNBB 138 81.47 51.24 REMARK 500 LYSBB 149 107.61 172.50 REMARK 500 ASPCC 31 112.14 -165.87 REMARK 500 ALACC 35 43.75 -97.75 REMARK 500 ARGCC 79 -117.24 48.19 REMARK 500 ASPDD 31 115.18 -169.77 REMARK 500 THRDD 33 91.86 -50.54 REMARK 500 ALADD 35 79.58 -15.73 REMARK 500 ARGDD 79 49.30 19.37 REMARK 500 LYSDD 80 -58.84 157.37 REMARK 500 GLNHH 39 114.44 -168.06 REMARK 500 THRHH 91 107.94 -56.24 REMARK 500 PHEHH 103 74.93 52.54 REMARK 500 SERHH 115 142.67 -170.40 REMARK 500 SERHH 116 71.50 -103.72 REMARK 500 SERHH 130 -158.20 -157.48 REMARK 500 LYSHH 132 94.52 -63.40 REMARK 500 SERHH 133 -43.60 127.82 REMARK 500 SERHH 135 115.27 -21.07 REMARK 500 LEULL 47 -60.56 -108.83 REMARK 500 LYSLL 52 -13.35 -146.40 REMARK 500 PROLL 59 151.86 -46.40 REMARK 500 HISLL 68 -101.55 54.75 REMARK 500 ALALL 84 -173.08 -175.64 REMARK 500 TYRLL 91 36.50 -149.99 REMARK 500 ASNLL 138 81.51 50.92 REMARK 500 ASPLL 151 -135.36 54.98 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 ILEDD 7 ALADD 8 -144.26 REMARK 500 REMARK 500 REMARK: NULL DBREF 6T9EAA 1 220 PDB 6T9E 6T9E 1 220 DBREF 6T9EBB 1 214 PDB 6T9E 6T9E 1 214 DBREF 6T9ECC 1 109 UNP P01127 PDGFB_HUMAN 82 190 DBREF 6T9EDD 1 109 UNP P01127 PDGFB_HUMAN 82 190 DBREF 6T9EHH 1 220 PDB 6T9E 6T9E 1 220 DBREF 6T9ELL 1 214 PDB 6T9E 6T9E 1 214 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 214 ALA ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2BB 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS HIS GLY SER SEQRES 3BB 214 TYR TRP LEU SER ASN TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4BB 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ASP GLY LYS SEQRES 5BB 214 GLU ARG GLU HIS GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6BB 214 GLY SER HIS GLU ASP TYR THR LEU THR ILE SER SER LEU SEQRES 7BB 214 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8BB 214 ARG TYR HIS PRO TYR THR PHE GLY GLN GLY THR LYS LEU SEQRES 9BB 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10BB 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11BB 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12BB 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13BB 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14BB 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15BB 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16BB 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17BB 214 PHE ASN ARG GLY GLU CYS SEQRES 1CC 109 SER LEU GLY SER LEU THR ILE ALA GLU PRO ALA MET ILE SEQRES 2CC 109 ALA GLU CYS LYS THR ARG THR GLU VAL PHE GLU ILE SER SEQRES 3CC 109 ARG ARG LEU ILE ASP ARG THR ASN ALA ASN PHE LEU VAL SEQRES 4CC 109 TRP PRO PRO CYS VAL GLU VAL GLN ARG CYS SER GLY CYS SEQRES 5CC 109 CYS ASN ASN ARG ASN VAL GLN CYS ARG PRO THR GLN VAL SEQRES 6CC 109 GLN LEU ARG PRO VAL GLN VAL ARG LYS ILE GLU ILE VAL SEQRES 7CC 109 ARG LYS LYS PRO ILE PHE LYS LYS ALA THR VAL THR LEU SEQRES 8CC 109 GLU ASP HIS LEU ALA CYS LYS CYS GLU THR VAL ALA ALA SEQRES 9CC 109 ALA ARG PRO VAL THR SEQRES 1DD 109 SER LEU GLY SER LEU THR ILE ALA GLU PRO ALA MET ILE SEQRES 2DD 109 ALA GLU CYS LYS THR ARG THR GLU VAL PHE GLU ILE SER SEQRES 3DD 109 ARG ARG LEU ILE ASP ARG THR ASN ALA ASN PHE LEU VAL SEQRES 4DD 109 TRP PRO PRO CYS VAL GLU VAL GLN ARG CYS SER GLY CYS SEQRES 5DD 109 CYS ASN ASN ARG ASN VAL GLN CYS ARG PRO THR GLN VAL SEQRES 6DD 109 GLN LEU ARG PRO VAL GLN VAL ARG LYS ILE GLU ILE VAL SEQRES 7DD 109 ARG LYS LYS PRO ILE PHE LYS LYS ALA THR VAL THR LEU SEQRES 8DD 109 GLU ASP HIS LEU ALA CYS LYS CYS GLU THR VAL ALA ALA SEQRES 9DD 109 ALA ARG PRO VAL THR 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 214 ALA ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2LL 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS HIS GLY SER SEQRES 3LL 214 TYR TRP LEU SER ASN TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4LL 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ASP GLY LYS SEQRES 5LL 214 GLU ARG GLU HIS GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6LL 214 GLY SER HIS GLU ASP TYR THR LEU THR ILE SER SER LEU SEQRES 7LL 214 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8LL 214 ARG TYR HIS PRO TYR THR PHE GLY GLN GLY THR LYS LEU SEQRES 9LL 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10LL 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11LL 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12LL 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13LL 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14LL 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15LL 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16LL 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17LL 214 PHE ASN ARG GLY GLU CYS HELIX 1 AA1 GLYAA 26 THRAA 32 5 7 HELIX 2 AA2 THRAA 62 ILEAA 65 5 4 HELIX 3 AA3 ARGAA 87 THRAA 91 5 5 HELIX 4 AA4 SERAA 159 ALAAA 161 5 3 HELIX 5 AA5 LYSAA 204 ASNAA 207 5 4 HELIX 6 AA6 GLNBB 79 PHEBB 83 5 5 HELIX 7 AA7 SERBB 121 LYSBB 126 1 6 HELIX 8 AA8 LYSBB 183 HISBB 189 1 7 HELIX 9 AA9 GLYHH 26 THRHH 32 5 7 HELIX 10 AB1 THRHH 62 ILEHH 65 5 4 HELIX 11 AB2 ARGHH 87 THRHH 91 5 5 HELIX 12 AB3 SERHH 130 SERHH 135 1 6 HELIX 13 AB4 SERHH 159 ALAHH 161 5 3 HELIX 14 AB5 LYSHH 204 ASNHH 207 5 4 HELIX 15 AB6 GLNLL 79 PHELL 83 5 5 HELIX 16 AB7 SERLL 121 LYSLL 126 1 6 HELIX 17 AB8 LYSLL 183 HISLL 189 1 7 SHEET 1 AA1 4 VALAA 5 SERAA 7 0 SHEET 2 AA1 4 SERAA 17 ALAAA 23 -1 O SERAA 21 N SERAA 7 SHEET 3 AA1 4 THRAA 78 ASNAA 84 -1 O METAA 83 N LEUAA 18 SHEET 4 AA1 4 PHEAA 68 ASPAA 73 -1 N THRAA 69 O GLNAA 82 SHEET 1 AA2 6 LEUAA 11 VALAA 12 0 SHEET 2 AA2 6 THRAA 110 VALAA 114 1 O THRAA 113 N VALAA 12 SHEET 3 AA2 6 ALAAA 92 ASPAA 99 -1 N ALAAA 92 O VALAA 112 SHEET 4 AA2 6 ASPAA 33 GLNAA 39 -1 N VALAA 37 O TYRAA 95 SHEET 5 AA2 6 GLUAA 46 ILEAA 51 -1 O GLUAA 46 N ARGAA 38 SHEET 6 AA2 6 THRAA 58 TYRAA 60 -1 O TYRAA 59 N SERAA 50 SHEET 1 AA3 4 SERAA 123 LEUAA 127 0 SHEET 2 AA3 4 ALAAA 139 TYRAA 148 -1 O LEUAA 144 N PHEAA 125 SHEET 3 AA3 4 TYRAA 179 VALAA 187 -1 O VALAA 187 N ALAAA 139 SHEET 4 AA3 4 VALAA 166 THRAA 168 -1 N HISAA 167 O VALAA 184 SHEET 1 AA4 4 SERAA 123 LEUAA 127 0 SHEET 2 AA4 4 ALAAA 139 TYRAA 148 -1 O LEUAA 144 N PHEAA 125 SHEET 3 AA4 4 TYRAA 179 VALAA 187 -1 O VALAA 187 N ALAAA 139 SHEET 4 AA4 4 VALAA 172 LEUAA 173 -1 N VALAA 172 O SERAA 180 SHEET 1 AA5 3 THRAA 154 TRPAA 157 0 SHEET 2 AA5 3 ILEAA 198 HISAA 203 -1 O ASNAA 200 N SERAA 156 SHEET 3 AA5 3 THRAA 208 LYSAA 213 -1 O THRAA 208 N HISAA 203 SHEET 1 AA6 4 THRBB 5 SERBB 7 0 SHEET 2 AA6 4 VALBB 19 HISBB 24 -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 65 O THRBB 72 SHEET 1 AA7 6 SERBB 10 SERBB 14 0 SHEET 2 AA7 6 THRBB 102 LYSBB 107 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 PROBB 44 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 SERBB 14 0 SHEET 2 AA8 4 THRBB 102 LYSBB 107 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 GLNBB 160 O THRBB 178 SHEET 1 AB1 3 LYSBB 145 TRPBB 148 0 SHEET 2 AB1 3 CYSBB 194 THRBB 197 -1 O GLUBB 195 N GLNBB 147 SHEET 3 AB1 3 VALBB 205 LYSBB 207 -1 O VALBB 205 N VALBB 196 SHEET 1 AB2 3 GLUCC 9 PROCC 10 0 SHEET 2 AB2 3 VALDD 58 VALDD 78 1 O GLNDD 71 N GLUCC 9 SHEET 3 AB2 3 PHEDD 37 TRPDD 40 -1 N LEUDD 38 O ILEDD 75 SHEET 1 AB3 3 GLUCC 9 PROCC 10 0 SHEET 2 AB3 3 VALDD 58 VALDD 78 1 O GLNDD 71 N GLUCC 9 SHEET 3 AB3 3 LYSDD 81 THRDD 101 -1 O VALDD 89 N VALDD 70 SHEET 1 AB4 2 LYSCC 17 GLUCC 24 0 SHEET 2 AB4 2 CYSCC 43 SERCC 50 -1 O VALCC 44 N PHECC 23 SHEET 1 AB5 3 PHECC 37 TRPCC 40 0 SHEET 2 AB5 3 GLNCC 59 VALCC 78 -1 O ILECC 75 N LEUCC 38 SHEET 3 AB5 3 LYSCC 81 GLUCC 100 -1 O VALCC 89 N VALCC 70 SHEET 1 AB6 2 LYSDD 17 GLUDD 24 0 SHEET 2 AB6 2 CYSDD 43 SERDD 50 -1 O VALDD 44 N PHEDD 23 SHEET 1 AB7 4 VALHH 5 SERHH 7 0 SHEET 2 AB7 4 SERHH 17 ALAHH 23 -1 O SERHH 21 N SERHH 7 SHEET 3 AB7 4 THRHH 78 ASNHH 84 -1 O METHH 83 N LEUHH 18 SHEET 4 AB7 4 PHEHH 68 ASPHH 73 -1 N THRHH 69 O GLNHH 82 SHEET 1 AB8 6 LEUHH 11 VALHH 12 0 SHEET 2 AB8 6 THRHH 110 VALHH 114 1 O THRHH 113 N VALHH 12 SHEET 3 AB8 6 ALAHH 92 ASPHH 99 -1 N ALAHH 92 O VALHH 112 SHEET 4 AB8 6 ASPHH 33 GLNHH 39 -1 N VALHH 37 O TYRHH 95 SHEET 5 AB8 6 GLUHH 46 ILEHH 51 -1 O GLUHH 46 N ARGHH 38 SHEET 6 AB8 6 THRHH 58 TYRHH 60 -1 O TYRHH 59 N SERHH 50 SHEET 1 AB9 4 SERHH 123 LEUHH 127 0 SHEET 2 AB9 4 THRHH 138 TYRHH 148 -1 O LEUHH 144 N PHEHH 125 SHEET 3 AB9 4 TYRHH 179 PROHH 188 -1 O VALHH 187 N ALAHH 139 SHEET 4 AB9 4 VALHH 166 THRHH 168 -1 N HISHH 167 O VALHH 184 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 VALHH 187 N ALAHH 139 SHEET 4 AC1 4 VALHH 172 LEUHH 173 -1 N VALHH 172 O SERHH 180 SHEET 1 AC2 3 THRHH 154 TRPHH 157 0 SHEET 2 AC2 3 ILEHH 198 HISHH 203 -1 O ASNHH 200 N SERHH 156 SHEET 3 AC2 3 THRHH 208 LYSHH 213 -1 O THRHH 208 N HISHH 203 SHEET 1 AC3 4 THRLL 5 SERLL 7 0 SHEET 2 AC3 4 VALLL 19 HISLL 24 -1 O THRLL 22 N SERLL 7 SHEET 3 AC3 4 ASPLL 70 ILELL 75 -1 O TYRLL 71 N CYSLL 23 SHEET 4 AC3 4 PHELL 62 SERLL 67 -1 N SERLL 65 O THRLL 72 SHEET 1 AC4 6 SERLL 10 SERLL 14 0 SHEET 2 AC4 6 THRLL 102 LYSLL 107 1 O GLULL 105 N LEULL 11 SHEET 3 AC4 6 ALALL 84 GLNLL 90 -1 N TYRLL 86 O THRLL 102 SHEET 4 AC4 6 LEULL 33 GLNLL 38 -1 N TYRLL 36 O TYRLL 87 SHEET 5 AC4 6 PROLL 44 TYRLL 49 -1 O LYSLL 45 N GLNLL 37 SHEET 6 AC4 6 GLULL 53 ARGLL 54 -1 O GLULL 53 N TYRLL 49 SHEET 1 AC5 4 SERLL 10 SERLL 14 0 SHEET 2 AC5 4 THRLL 102 LYSLL 107 1 O GLULL 105 N LEULL 11 SHEET 3 AC5 4 ALALL 84 GLNLL 90 -1 N TYRLL 86 O THRLL 102 SHEET 4 AC5 4 THRLL 97 PHELL 98 -1 O THRLL 97 N GLNLL 90 SHEET 1 AC6 4 SERLL 114 PHELL 118 0 SHEET 2 AC6 4 THRLL 129 PHELL 139 -1 O LEULL 135 N PHELL 116 SHEET 3 AC6 4 TYRLL 173 SERLL 182 -1 O TYRLL 173 N PHELL 139 SHEET 4 AC6 4 SERLL 159 VALLL 163 -1 N GLNLL 160 O THRLL 178 SHEET 1 AC7 4 ALALL 153 GLNLL 155 0 SHEET 2 AC7 4 LYSLL 145 VALLL 150 -1 N TRPLL 148 O GLNLL 155 SHEET 3 AC7 4 TYRLL 192 THRLL 197 -1 O GLULL 195 N GLNLL 147 SHEET 4 AC7 4 VALLL 205 PHELL 209 -1 O VALLL 205 N VALLL 196 SSBOND 1 CYSAA 22 CYSAA 96 1555 1555 2.02 SSBOND 2 CYSAA 143 CYSAA 199 1555 1555 2.06 SSBOND 3 CYSBB 23 CYSBB 88 1555 1555 2.06 SSBOND 4 CYSBB 134 CYSBB 194 1555 1555 2.05 SSBOND 5 CYSCC 16 CYSCC 60 1555 1555 2.02 SSBOND 6 CYSCC 43 CYSDD 52 1555 1555 2.06 SSBOND 7 CYSCC 49 CYSCC 97 1555 1555 2.06 SSBOND 8 CYSCC 52 CYSDD 43 1555 1555 2.05 SSBOND 9 CYSCC 53 CYSCC 99 1555 1555 2.05 SSBOND 10 CYSDD 16 CYSDD 60 1555 1555 2.03 SSBOND 11 CYSDD 49 CYSDD 97 1555 1555 2.07 SSBOND 12 CYSDD 53 CYSDD 99 1555 1555 2.05 SSBOND 13 CYSHH 22 CYSHH 96 1555 1555 2.03 SSBOND 14 CYSHH 143 CYSHH 199 1555 1555 2.06 SSBOND 15 CYSLL 23 CYSLL 88 1555 1555 2.07 SSBOND 16 CYSLL 134 CYSLL 194 1555 1555 2.04 CISPEP 1 PHEAA 149 PROAA 150 0 -14.68 CISPEP 2 GLUAA 151 PROAA 152 0 -5.23 CISPEP 3 SERBB 7 PROBB 8 0 -3.39 CISPEP 4 HISBB 94 PROBB 95 0 5.00 CISPEP 5 TYRBB 140 PROBB 141 0 4.77 CISPEP 6 TRPCC 40 PROCC 41 0 -8.58 CISPEP 7 TRPDD 40 PRODD 41 0 -8.52 CISPEP 8 PHEHH 149 PROHH 150 0 -14.30 CISPEP 9 GLUHH 151 PROHH 152 0 -5.03 CISPEP 10 SERLL 7 PROLL 8 0 -3.52 CISPEP 11 HISLL 94 PROLL 95 0 5.01 CISPEP 12 TYRLL 140 PROLL 141 0 5.00 CRYST1 89.301 75.474 116.505 90.00 110.58 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 0.011198 0.000000 0.004206 0.00000 SCALE2 0.000000 0.013250 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009169 0.00000