HEADER IMMUNE SYSTEM 16-NOV-20 7KQK TITLE ANTI-PTAU C21-ABS FAB IN COMPLEX WITH PTAU PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEAVY CHAIN OF FAB FRAGMENT; COMPND 3 CHAIN: A, H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: LIGHT CHAIN OF FAB FRAGMENT; COMPND 7 CHAIN: B, L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: PTAU PEPTIDE; COMPND 11 CHAIN: C, P; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: HEK; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM_CELL_LINE: HEK; SOURCE 13 MOL_ID: 3; SOURCE 14 SYNTHETIC: YES; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_TAXID: 9606 KEYWDS PTAU PEPTIDE, ANTIBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR L.MOSYAK,A.BRINTH REVDAT 1 18-MAY-22 7KQK 0 JRNL AUTH L.MOSYAK,A.BRINTH JRNL TITL ANTI-PTAU C21-ABS FAB IN COMPLEX WITH PTAU PEPTIDE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.11.7 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 64.47 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 3 NUMBER OF REFLECTIONS : 29166 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) : 0.212 REMARK 3 R VALUE (WORKING SET) : 0.211 REMARK 3 FREE R VALUE : 0.231 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.690 REMARK 3 FREE R VALUE TEST SET COUNT : 1368 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 15 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.69 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.61 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2813 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2516 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2673 REMARK 3 BIN R VALUE (WORKING SET) : 0.2502 REMARK 3 BIN FREE R VALUE : 0.2800 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.98 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 140 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6465 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 329 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 55.14 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.88 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 26.31390 REMARK 3 B22 (A**2) : -12.90020 REMARK 3 B33 (A**2) : -13.41370 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -6.93500 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.390 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 1.177 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.287 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 1.023 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.290 REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.875 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.879 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 6630 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 9049 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 2137 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL REMARK 3 GENERAL PLANES : 1111 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 6630 ; 20.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 880 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 7076 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.17 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.97 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.01 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 7KQK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-NOV-20. REMARK 100 THE DEPOSITION ID IS D_1000252961. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-JUL-19 REMARK 200 TEMPERATURE (KELVIN) : 80 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 17-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 300K REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29183 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 REMARK 200 RESOLUTION RANGE LOW (A) : 76.600 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 3.400 REMARK 200 R MERGE (I) : 0.07900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.41000 REMARK 200 R SYM FOR SHELL (I) : NULL 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: PHASER REMARK 200 STARTING MODEL: 4GLR REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.55 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % PEG 3350 (W/V) AND 150 MM DL REMARK 280 -MALIC ACID., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 300K 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 38.29000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4270 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19770 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4300 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19480 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, P 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 141 REMARK 465 SER A 142 REMARK 465 LYS A 143 REMARK 465 SER A 144 REMARK 465 THR A 145 REMARK 465 SER A 146 REMARK 465 GLY A 147 REMARK 465 CYS A 230 REMARK 465 THR B 207 REMARK 465 GLU B 208 REMARK 465 CYS B 209 REMARK 465 SER B 210 REMARK 465 SER H 141 REMARK 465 SER H 142 REMARK 465 LYS H 143 REMARK 465 SER H 144 REMARK 465 THR H 145 REMARK 465 SER H 146 REMARK 465 GLY H 147 REMARK 465 CYS H 230 REMARK 465 GLU L 208 REMARK 465 CYS L 209 REMARK 465 SER L 210 REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 LYS A 224 CD CE NZ REMARK 480 LYS B 154 CG CD CE NZ REMARK 480 ARG B 187 CG CD NE CZ NH1 NH2 REMARK 480 LYS H 224 CD CE NZ REMARK 480 LYS L 154 CG CD CE NZ REMARK 480 ARG L 187 CG CD NE CZ NH1 NH2 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 ALA A 111 7.00 -69.23 REMARK 500 ASN B 46 -47.75 73.57 REMARK 500 ASP B 55 5.77 -66.95 REMARK 500 ASP B 149 -106.50 59.50 REMARK 500 ASN B 168 -0.52 80.40 REMARK 500 VAL H 48 -61.50 -101.69 REMARK 500 ALA H 111 2.82 -68.16 REMARK 500 ASN L 46 -52.76 69.12 REMARK 500 ASP L 55 7.55 -67.08 REMARK 500 ALA L 79 -179.62 -171.33 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 403 DISTANCE = 6.07 ANGSTROMS REMARK 525 HOH A 404 DISTANCE = 7.08 ANGSTROMS REMARK 525 HOH A 405 DISTANCE = 9.46 ANGSTROMS REMARK 525 HOH C 309 DISTANCE = 7.46 ANGSTROMS REMARK 525 HOH P 308 DISTANCE = 7.55 ANGSTROMS DBREF 7KQK A 1 230 PDB 7KQK 7KQK 1 230 DBREF 7KQK B 1 210 PDB 7KQK 7KQK 1 210 DBREF 7KQK C 224 233 PDB 7KQK 7KQK 224 233 DBREF 7KQK H 1 230 PDB 7KQK 7KQK 1 230 DBREF 7KQK L 1 210 PDB 7KQK 7KQK 1 210 DBREF 7KQK P 224 233 PDB 7KQK 7KQK 224 233 SEQRES 1 A 230 GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 230 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 A 230 PHE THR LEU SER SER TYR GLN MET MET TRP VAL ARG GLN SEQRES 4 A 230 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA GLY ILE THR SEQRES 5 A 230 GLY ARG GLY GLY VAL THR GLY TYR ALA ASP SER VAL LYS SEQRES 6 A 230 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 A 230 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 A 230 ALA VAL TYR TYR CYS ALA LYS PRO ALA LEU ASP SER ASP SEQRES 9 A 230 GLN CYS GLY PHE PRO GLU ALA GLY CYS ILE ASP ALA TRP SEQRES 10 A 230 GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR SEQRES 11 A 230 LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SEQRES 12 A 230 SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL SEQRES 13 A 230 LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SEQRES 14 A 230 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 15 A 230 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 16 A 230 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 17 A 230 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 18 A 230 ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 1 B 210 SER GLU LEU THR GLN ASP PRO ALA VAL SER VAL ALA LEU SEQRES 2 B 210 GLY GLN THR VAL ARG ILE THR CYS GLN GLY ASP ASP SER SEQRES 3 B 210 TYR TYR GLY TRP TYR GLN GLN LYS PRO GLY GLN ALA PRO SEQRES 4 B 210 VAL THR VAL ILE TYR GLY ASN ASP ASN ARG PRO SER GLY SEQRES 5 B 210 ILE PRO ASP ARG PHE SER GLY SER SER SER GLY ASN THR SEQRES 6 B 210 ALA SER LEU THR ILE THR GLY ALA GLN ALA GLU ASP GLU SEQRES 7 B 210 ALA ASP TYR TYR CYS GLY ALA TYR ASP SER SER GLY GLY SEQRES 8 B 210 GLY GLY ILE PHE GLY GLY GLY THR LYS LEU THR VAL LEU SEQRES 9 B 210 GLY GLN PRO LYS ALA ALA PRO SER VAL THR LEU PHE PRO SEQRES 10 B 210 PRO SER SER GLU GLU LEU GLN ALA ASN LYS ALA THR LEU SEQRES 11 B 210 VAL CYS LEU ILE SER ASP PHE TYR PRO GLY ALA VAL THR SEQRES 12 B 210 VAL ALA TRP LYS ALA ASP SER SER PRO VAL LYS ALA GLY SEQRES 13 B 210 VAL GLU THR THR THR PRO SER LYS GLN SER ASN ASN LYS SEQRES 14 B 210 TYR ALA ALA SER SER TYR LEU SER LEU THR PRO GLU GLN SEQRES 15 B 210 TRP LYS SER HIS ARG SER TYR SER CYS GLN VAL THR HIS SEQRES 16 B 210 GLU GLY SER THR VAL GLU LYS THR VAL ALA PRO THR GLU SEQRES 17 B 210 CYS SER SEQRES 1 C 10 LYS LYS VAL ALA VAL VAL ARG TPO PRO PRO SEQRES 1 H 230 GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 230 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 230 PHE THR LEU SER SER TYR GLN MET MET TRP VAL ARG GLN SEQRES 4 H 230 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA GLY ILE THR SEQRES 5 H 230 GLY ARG GLY GLY VAL THR GLY TYR ALA ASP SER VAL LYS SEQRES 6 H 230 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 H 230 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 230 ALA VAL TYR TYR CYS ALA LYS PRO ALA LEU ASP SER ASP SEQRES 9 H 230 GLN CYS GLY PHE PRO GLU ALA GLY CYS ILE ASP ALA TRP SEQRES 10 H 230 GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR SEQRES 11 H 230 LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SEQRES 12 H 230 SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL SEQRES 13 H 230 LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SEQRES 14 H 230 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 15 H 230 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 16 H 230 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 17 H 230 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 18 H 230 ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 1 L 210 SER GLU LEU THR GLN ASP PRO ALA VAL SER VAL ALA LEU SEQRES 2 L 210 GLY GLN THR VAL ARG ILE THR CYS GLN GLY ASP ASP SER SEQRES 3 L 210 TYR TYR GLY TRP TYR GLN GLN LYS PRO GLY GLN ALA PRO SEQRES 4 L 210 VAL THR VAL ILE TYR GLY ASN ASP ASN ARG PRO SER GLY SEQRES 5 L 210 ILE PRO ASP ARG PHE SER GLY SER SER SER GLY ASN THR SEQRES 6 L 210 ALA SER LEU THR ILE THR GLY ALA GLN ALA GLU ASP GLU SEQRES 7 L 210 ALA ASP TYR TYR CYS GLY ALA TYR ASP SER SER GLY GLY SEQRES 8 L 210 GLY GLY ILE PHE GLY GLY GLY THR LYS LEU THR VAL LEU SEQRES 9 L 210 GLY GLN PRO LYS ALA ALA PRO SER VAL THR LEU PHE PRO SEQRES 10 L 210 PRO SER SER GLU GLU LEU GLN ALA ASN LYS ALA THR LEU SEQRES 11 L 210 VAL CYS LEU ILE SER ASP PHE TYR PRO GLY ALA VAL THR SEQRES 12 L 210 VAL ALA TRP LYS ALA ASP SER SER PRO VAL LYS ALA GLY SEQRES 13 L 210 VAL GLU THR THR THR PRO SER LYS GLN SER ASN ASN LYS SEQRES 14 L 210 TYR ALA ALA SER SER TYR LEU SER LEU THR PRO GLU GLN SEQRES 15 L 210 TRP LYS SER HIS ARG SER TYR SER CYS GLN VAL THR HIS SEQRES 16 L 210 GLU GLY SER THR VAL GLU LYS THR VAL ALA PRO THR GLU SEQRES 17 L 210 CYS SER SEQRES 1 P 10 LYS LYS VAL ALA VAL VAL ARG TPO PRO PRO HET TPO C 231 11 HET TPO P 231 11 HETNAM TPO PHOSPHOTHREONINE HETSYN TPO PHOSPHONOTHREONINE FORMUL 3 TPO 2(C4 H10 N O6 P) FORMUL 7 HOH *329(H2 O) HELIX 1 AA1 THR A 28 TYR A 32 5 5 HELIX 2 AA2 ASN A 74 LYS A 76 5 3 HELIX 3 AA3 ARG A 87 THR A 91 5 5 HELIX 4 AA4 SER A 201 LEU A 203 5 3 HELIX 5 AA5 LYS A 215 ASN A 218 5 4 HELIX 6 AA6 GLN B 74 GLU B 78 5 5 HELIX 7 AA7 SER B 119 ALA B 125 1 7 HELIX 8 AA8 THR B 179 SER B 185 1 7 HELIX 9 AA9 THR H 28 TYR H 32 5 5 HELIX 10 AB1 ASN H 74 LYS H 76 5 3 HELIX 11 AB2 ARG H 87 THR H 91 5 5 HELIX 12 AB3 SER H 201 LEU H 203 5 3 HELIX 13 AB4 LYS H 215 ASN H 218 5 4 HELIX 14 AB5 GLN L 74 GLU L 78 5 5 HELIX 15 AB6 SER L 119 ALA L 125 1 7 HELIX 16 AB7 THR L 179 SER L 185 1 7 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O ALA A 23 N LEU A 5 SHEET 3 AA1 4 THR A 78 MET A 83 -1 O LEU A 81 N LEU A 20 SHEET 4 AA1 4 PHE A 68 ASP A 73 -1 N SER A 71 O TYR A 80 SHEET 1 AA2 6 GLY A 10 VAL A 12 0 SHEET 2 AA2 6 THR A 121 VAL A 125 1 O THR A 124 N GLY A 10 SHEET 3 AA2 6 ALA A 92 PRO A 99 -1 N TYR A 94 O THR A 121 SHEET 4 AA2 6 MET A 34 GLN A 39 -1 N VAL A 37 O TYR A 95 SHEET 5 AA2 6 LEU A 45 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 6 AA2 6 THR A 58 TYR A 60 -1 O GLY A 59 N GLY A 50 SHEET 1 AA3 4 GLY A 10 VAL A 12 0 SHEET 2 AA3 4 THR A 121 VAL A 125 1 O THR A 124 N GLY A 10 SHEET 3 AA3 4 ALA A 92 PRO A 99 -1 N TYR A 94 O THR A 121 SHEET 4 AA3 4 ILE A 114 TRP A 117 -1 O ALA A 116 N LYS A 98 SHEET 1 AA4 4 SER A 134 LEU A 138 0 SHEET 2 AA4 4 THR A 149 TYR A 159 -1 O GLY A 153 N LEU A 138 SHEET 3 AA4 4 TYR A 190 PRO A 199 -1 O TYR A 190 N TYR A 159 SHEET 4 AA4 4 VAL A 177 THR A 179 -1 N HIS A 178 O VAL A 195 SHEET 1 AA5 4 SER A 134 LEU A 138 0 SHEET 2 AA5 4 THR A 149 TYR A 159 -1 O GLY A 153 N LEU A 138 SHEET 3 AA5 4 TYR A 190 PRO A 199 -1 O TYR A 190 N TYR A 159 SHEET 4 AA5 4 VAL A 183 LEU A 184 -1 N VAL A 183 O SER A 191 SHEET 1 AA6 3 THR A 165 TRP A 168 0 SHEET 2 AA6 3 TYR A 208 HIS A 214 -1 O ASN A 211 N SER A 167 SHEET 3 AA6 3 THR A 219 VAL A 225 -1 O VAL A 221 N VAL A 212 SHEET 1 AA7 5 ALA B 8 ALA B 12 0 SHEET 2 AA7 5 THR B 99 LEU B 104 1 O LEU B 104 N VAL B 11 SHEET 3 AA7 5 ASP B 80 ASP B 87 -1 N TYR B 81 O THR B 99 SHEET 4 AA7 5 GLY B 29 GLN B 33 -1 N GLN B 33 O ASP B 80 SHEET 5 AA7 5 VAL B 40 ILE B 43 -1 O ILE B 43 N TRP B 30 SHEET 1 AA8 4 ALA B 8 ALA B 12 0 SHEET 2 AA8 4 THR B 99 LEU B 104 1 O LEU B 104 N VAL B 11 SHEET 3 AA8 4 ASP B 80 ASP B 87 -1 N TYR B 81 O THR B 99 SHEET 4 AA8 4 GLY B 92 PHE B 95 -1 O GLY B 92 N ASP B 87 SHEET 1 AA9 3 VAL B 17 GLN B 22 0 SHEET 2 AA9 3 THR B 65 ILE B 70 -1 O LEU B 68 N ILE B 19 SHEET 3 AA9 3 PHE B 57 SER B 62 -1 N SER B 58 O THR B 69 SHEET 1 AB1 4 SER B 112 PHE B 116 0 SHEET 2 AB1 4 ALA B 128 PHE B 137 -1 O SER B 135 N SER B 112 SHEET 3 AB1 4 TYR B 170 LEU B 178 -1 O LEU B 178 N ALA B 128 SHEET 4 AB1 4 VAL B 157 THR B 159 -1 N GLU B 158 O TYR B 175 SHEET 1 AB2 4 SER B 112 PHE B 116 0 SHEET 2 AB2 4 ALA B 128 PHE B 137 -1 O SER B 135 N SER B 112 SHEET 3 AB2 4 TYR B 170 LEU B 178 -1 O LEU B 178 N ALA B 128 SHEET 4 AB2 4 SER B 163 LYS B 164 -1 N SER B 163 O ALA B 171 SHEET 1 AB3 4 SER B 151 PRO B 152 0 SHEET 2 AB3 4 THR B 143 ALA B 148 -1 N ALA B 148 O SER B 151 SHEET 3 AB3 4 TYR B 189 HIS B 195 -1 O GLN B 192 N ALA B 145 SHEET 4 AB3 4 SER B 198 VAL B 204 -1 O VAL B 200 N VAL B 193 SHEET 1 AB4 4 GLN H 3 SER H 7 0 SHEET 2 AB4 4 LEU H 18 SER H 25 -1 O ALA H 23 N LEU H 5 SHEET 3 AB4 4 THR H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 AB4 4 PHE H 68 ASP H 73 -1 N SER H 71 O TYR H 80 SHEET 1 AB5 6 GLY H 10 VAL H 12 0 SHEET 2 AB5 6 THR H 121 VAL H 125 1 O THR H 124 N GLY H 10 SHEET 3 AB5 6 ALA H 92 PRO H 99 -1 N TYR H 94 O THR H 121 SHEET 4 AB5 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AB5 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AB5 6 THR H 58 TYR H 60 -1 O GLY H 59 N GLY H 50 SHEET 1 AB6 4 GLY H 10 VAL H 12 0 SHEET 2 AB6 4 THR H 121 VAL H 125 1 O THR H 124 N GLY H 10 SHEET 3 AB6 4 ALA H 92 PRO H 99 -1 N TYR H 94 O THR H 121 SHEET 4 AB6 4 ILE H 114 TRP H 117 -1 O ASP H 115 N LYS H 98 SHEET 1 AB7 4 SER H 134 LEU H 138 0 SHEET 2 AB7 4 THR H 149 TYR H 159 -1 O LEU H 155 N PHE H 136 SHEET 3 AB7 4 TYR H 190 PRO H 199 -1 O TYR H 190 N TYR H 159 SHEET 4 AB7 4 VAL H 177 THR H 179 -1 N HIS H 178 O VAL H 195 SHEET 1 AB8 4 SER H 134 LEU H 138 0 SHEET 2 AB8 4 THR H 149 TYR H 159 -1 O LEU H 155 N PHE H 136 SHEET 3 AB8 4 TYR H 190 PRO H 199 -1 O TYR H 190 N TYR H 159 SHEET 4 AB8 4 VAL H 183 LEU H 184 -1 N VAL H 183 O SER H 191 SHEET 1 AB9 3 THR H 165 TRP H 168 0 SHEET 2 AB9 3 ILE H 209 HIS H 214 -1 O ASN H 211 N SER H 167 SHEET 3 AB9 3 THR H 219 LYS H 224 -1 O VAL H 221 N VAL H 212 SHEET 1 AC1 5 ALA L 8 VAL L 11 0 SHEET 2 AC1 5 THR L 99 VAL L 103 1 O THR L 102 N VAL L 11 SHEET 3 AC1 5 ALA L 79 ASP L 87 -1 N TYR L 81 O THR L 99 SHEET 4 AC1 5 GLY L 29 GLN L 33 -1 N GLN L 33 O ASP L 80 SHEET 5 AC1 5 VAL L 40 ILE L 43 -1 O ILE L 43 N TRP L 30 SHEET 1 AC2 4 ALA L 8 VAL L 11 0 SHEET 2 AC2 4 THR L 99 VAL L 103 1 O THR L 102 N VAL L 11 SHEET 3 AC2 4 ALA L 79 ASP L 87 -1 N TYR L 81 O THR L 99 SHEET 4 AC2 4 GLY L 92 PHE L 95 -1 O GLY L 92 N ASP L 87 SHEET 1 AC3 3 VAL L 17 GLN L 22 0 SHEET 2 AC3 3 THR L 65 ILE L 70 -1 O LEU L 68 N ILE L 19 SHEET 3 AC3 3 PHE L 57 SER L 62 -1 N SER L 58 O THR L 69 SHEET 1 AC4 4 SER L 112 PHE L 116 0 SHEET 2 AC4 4 ALA L 128 PHE L 137 -1 O LEU L 133 N THR L 114 SHEET 3 AC4 4 TYR L 170 LEU L 178 -1 O LEU L 178 N ALA L 128 SHEET 4 AC4 4 VAL L 157 THR L 159 -1 N GLU L 158 O TYR L 175 SHEET 1 AC5 4 SER L 112 PHE L 116 0 SHEET 2 AC5 4 ALA L 128 PHE L 137 -1 O LEU L 133 N THR L 114 SHEET 3 AC5 4 TYR L 170 LEU L 178 -1 O LEU L 178 N ALA L 128 SHEET 4 AC5 4 SER L 163 LYS L 164 -1 N SER L 163 O ALA L 171 SHEET 1 AC6 4 SER L 151 PRO L 152 0 SHEET 2 AC6 4 THR L 143 ALA L 148 -1 N ALA L 148 O SER L 151 SHEET 3 AC6 4 TYR L 189 HIS L 195 -1 O GLN L 192 N ALA L 145 SHEET 4 AC6 4 SER L 198 VAL L 204 -1 O VAL L 200 N VAL L 193 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.04 SSBOND 2 CYS A 106 CYS A 113 1555 1555 2.05 SSBOND 3 CYS A 154 CYS A 210 1555 1555 2.04 SSBOND 4 CYS B 21 CYS B 83 1555 1555 2.04 SSBOND 5 CYS B 132 CYS B 191 1555 1555 2.04 SSBOND 6 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 7 CYS H 106 CYS H 113 1555 1555 2.04 SSBOND 8 CYS H 154 CYS H 210 1555 1555 2.03 SSBOND 9 CYS L 21 CYS L 83 1555 1555 2.04 SSBOND 10 CYS L 132 CYS L 191 1555 1555 2.04 LINK C ARG C 230 N TPO C 231 1555 1555 1.34 LINK C TPO C 231 N PRO C 232 1555 1555 1.36 LINK C ARG P 230 N TPO P 231 1555 1555 1.33 LINK C TPO P 231 N PRO P 232 1555 1555 1.37 CISPEP 1 PHE A 160 PRO A 161 0 -6.12 CISPEP 2 GLU A 162 PRO A 163 0 8.55 CISPEP 3 TYR B 138 PRO B 139 0 -0.88 CISPEP 4 PHE H 160 PRO H 161 0 -4.06 CISPEP 5 GLU H 162 PRO H 163 0 5.46 CISPEP 6 TYR L 138 PRO L 139 0 0.62 CRYST1 52.370 76.580 119.470 90.00 90.36 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 0.019095 0.000000 0.000120 0.00000 SCALE2 0.000000 0.013058 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008370 0.00000