HEADER VIRAL PROTEIN 17-JUN-25 9RM2 TITLE BKPYV VP1 IN COMPLEX WITH 319C07-FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: 319C07 ANTIBODY HEAVY CHAIN, FAB FRAGMENT; COMPND 3 CHAIN: H, A, D, G, M; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 319C07 ANTIBODY LIGHT CHAIN, FAB FRAGMENT; COMPND 7 CHAIN: L, B, E, J, N; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: MAJOR CAPSID PROTEIN VP1; COMPND 11 CHAIN: P, C, F, K, O; COMPND 12 SYNONYM: MAJOR STRUCTURAL PROTEIN VP1; COMPND 13 ENGINEERED: YES; COMPND 14 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: BETAPOLYOMAVIRUS HOMINIS; SOURCE 13 ORGANISM_TAXID: 1891762; SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS FAB ANTIBODY BKPYV VP1 VIRUS CAPSID, VIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR S.SCHMITT,M.HILLENBRAND REVDAT 1 09-JUL-25 9RM2 0 JRNL AUTH M.WEBER,M.HILLENBRAND JRNL TITL A HIGHLY POTENT HUMAN ANTIBODY NEUTRALIZING ALL SEROTYPES OF JRNL TITL 2 BK POLYOMAVIRUS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.96 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0267 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.96 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 91.87 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 92.5 REMARK 3 NUMBER OF REFLECTIONS : 261412 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) : 0.189 REMARK 3 R VALUE (WORKING SET) : 0.187 REMARK 3 FREE R VALUE : 0.218 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 13696 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.96 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.01 REMARK 3 REFLECTION IN BIN (WORKING SET) : 19498 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.12 REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE SET COUNT : 1092 REMARK 3 BIN FREE R VALUE : 0.3090 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 27059 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 391 REMARK 3 SOLVENT ATOMS : 2156 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.49 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.97000 REMARK 3 B22 (A**2) : -0.42000 REMARK 3 B33 (A**2) : 1.54000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.77000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.173 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.149 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.122 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.550 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 27883 ; 0.004 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 25648 ; 0.002 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 37908 ; 1.361 ; 1.648 REMARK 3 BOND ANGLES OTHERS (DEGREES): 59153 ; 1.140 ; 1.569 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3569 ; 7.566 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1238 ;31.971 ;22.528 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 4190 ;12.451 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 132 ;18.329 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3650 ; 0.052 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 31627 ; 0.005 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 6289 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL 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): NULL ; NULL ; NULL 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): 14159 ; 1.822 ; 4.112 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 14158 ; 1.822 ; 4.112 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 17692 ; 2.945 ; 6.153 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 17693 ; 2.944 ; 6.154 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 13724 ; 1.936 ; 4.196 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 13725 ; 1.936 ; 4.197 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 20192 ; 3.101 ; 6.207 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 28760 ; 4.976 ;45.932 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 28454 ; 4.906 ;45.680 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 NCS TYPE: LOCAL REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 30 REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT REMARK 3 1 H 1 220 A 1 220 2235 0.02 0.05 REMARK 3 2 H 1 221 D 1 221 2220 0.01 0.05 REMARK 3 3 H 1 221 G 1 221 2201 0.03 0.05 REMARK 3 4 H 1 221 M 1 221 2249 0.02 0.05 REMARK 3 5 L 1 211 B 1 211 2272 0.03 0.05 REMARK 3 6 L 1 212 E 1 212 2231 0.02 0.05 REMARK 3 7 L 1 211 J 1 211 2278 0.02 0.05 REMARK 3 8 L 1 211 N 1 211 2282 0.02 0.05 REMARK 3 9 P 2 273 C 2 273 2909 0.03 0.05 REMARK 3 10 P 2 273 F 2 273 2904 0.02 0.05 REMARK 3 11 P 3 274 K 3 274 2989 0.03 0.05 REMARK 3 12 P 3 274 O 3 274 2991 0.03 0.05 REMARK 3 13 A 1 223 D 1 223 2304 0.02 0.05 REMARK 3 14 A 1 222 G 1 222 2267 0.03 0.05 REMARK 3 15 A 1 222 M 1 222 2318 0.03 0.05 REMARK 3 16 B 1 211 E 1 211 2214 0.03 0.05 REMARK 3 17 B 1 213 J 1 213 2294 0.02 0.05 REMARK 3 18 B 1 213 N 1 213 2311 0.02 0.05 REMARK 3 19 C 2 273 F 2 273 2935 0.03 0.05 REMARK 3 20 C 3 273 K 3 273 2930 0.03 0.05 REMARK 3 21 C 3 273 O 3 273 2899 0.03 0.05 REMARK 3 22 D 1 221 G 1 221 2273 0.03 0.05 REMARK 3 23 D 1 221 M 1 221 2326 0.03 0.05 REMARK 3 24 E 1 211 J 1 211 2212 0.03 0.05 REMARK 3 25 E 1 211 N 1 211 2234 0.02 0.05 REMARK 3 26 F 3 273 K 3 273 2933 0.02 0.05 REMARK 3 27 F 3 273 O 3 273 2918 0.03 0.05 REMARK 3 28 G 1 222 M 1 222 2324 0.03 0.05 REMARK 3 29 J 1 214 N 1 214 2327 0.02 0.05 REMARK 3 30 K 3 275 O 3 275 3006 0.02 0.05 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK 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 THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 9RM2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-JUN-25. REMARK 100 THE DEPOSITION ID IS D_1292148637. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 07-JUN-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X10SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9999 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 S 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC, XDS (VERSION JAN 31 REMARK 200 DATA SCALING SOFTWARE : AUTOPROC (VERSION 1.1.7), REMARK 200 AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 295460 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.957 REMARK 200 RESOLUTION RANGE LOW (A) : 91.870 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 200 DATA REDUNDANCY : 4.400 REMARK 200 R MERGE (I) : 0.09400 REMARK 200 R SYM (I) : 0.09400 REMARK 200 FOR THE DATA SET : 8.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.99 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7 REMARK 200 DATA REDUNDANCY IN SHELL : 4.10 REMARK 200 R MERGE FOR SHELL (I) : 1.22000 REMARK 200 R SYM FOR SHELL (I) : 1.22000 REMARK 200 FOR SHELL : 1.300 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.70 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MIB BUFFER PH 4.75, 21% (W/V) REMARK 280 PEG 1500, 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 86.03900 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: PENTADECAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTADECAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 69340 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 134080 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -193.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, P, A, B, C, D, E, F, G, REMARK 350 AND CHAINS: J, K, M, N, O 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 H 136 REMARK 465 LYS H 137 REMARK 465 SER H 138 REMARK 465 THR H 139 REMARK 465 SER H 140 REMARK 465 GLY H 141 REMARK 465 LYS H 222 REMARK 465 SER H 223 REMARK 465 GLY L 213 REMARK 465 GLU L 214 REMARK 465 CYS L 215 REMARK 465 MET P -24 REMARK 465 ALA P -23 REMARK 465 PRO P -22 REMARK 465 THR P -21 REMARK 465 LYS P -20 REMARK 465 ARG P -19 REMARK 465 LYS P -18 REMARK 465 GLY P -17 REMARK 465 GLU P -16 REMARK 465 CYS P -15 REMARK 465 PRO P -14 REMARK 465 GLY P -13 REMARK 465 ALA P -12 REMARK 465 ALA P -11 REMARK 465 PRO P -10 REMARK 465 LYS P -9 REMARK 465 LYS P -8 REMARK 465 PRO P -7 REMARK 465 LYS P -6 REMARK 465 GLU P -5 REMARK 465 PRO P -4 REMARK 465 VAL P -3 REMARK 465 GLN P -2 REMARK 465 VAL P -1 REMARK 465 PRO P 0 REMARK 465 LYS P 1 REMARK 465 LYS A 137 REMARK 465 SER A 138 REMARK 465 THR A 139 REMARK 465 SER A 140 REMARK 465 GLY A 141 REMARK 465 MET C -24 REMARK 465 ALA C -23 REMARK 465 PRO C -22 REMARK 465 THR C -21 REMARK 465 LYS C -20 REMARK 465 ARG C -19 REMARK 465 LYS C -18 REMARK 465 GLY C -17 REMARK 465 GLU C -16 REMARK 465 CYS C -15 REMARK 465 PRO C -14 REMARK 465 GLY C -13 REMARK 465 ALA C -12 REMARK 465 ALA C -11 REMARK 465 PRO C -10 REMARK 465 LYS C -9 REMARK 465 LYS C -8 REMARK 465 PRO C -7 REMARK 465 LYS C -6 REMARK 465 GLU C -5 REMARK 465 PRO C -4 REMARK 465 VAL C -3 REMARK 465 GLN C -2 REMARK 465 VAL C -1 REMARK 465 PRO C 0 REMARK 465 LYS C 1 REMARK 465 GLU C 76 REMARK 465 ASP C 77 REMARK 465 LEU C 78 REMARK 465 THR C 79 REMARK 465 PRO C 274 REMARK 465 TYR C 275 REMARK 465 GLY E 213 REMARK 465 GLU E 214 REMARK 465 CYS E 215 REMARK 465 MET F -24 REMARK 465 ALA F -23 REMARK 465 PRO F -22 REMARK 465 THR F -21 REMARK 465 LYS F -20 REMARK 465 ARG F -19 REMARK 465 LYS F -18 REMARK 465 GLY F -17 REMARK 465 GLU F -16 REMARK 465 CYS F -15 REMARK 465 PRO F -14 REMARK 465 GLY F -13 REMARK 465 ALA F -12 REMARK 465 ALA F -11 REMARK 465 PRO F -10 REMARK 465 LYS F -9 REMARK 465 LYS F -8 REMARK 465 PRO F -7 REMARK 465 LYS F -6 REMARK 465 GLU F -5 REMARK 465 PRO F -4 REMARK 465 VAL F -3 REMARK 465 GLN F -2 REMARK 465 VAL F -1 REMARK 465 PRO F 0 REMARK 465 LYS F 1 REMARK 465 GLU F 76 REMARK 465 ASP F 77 REMARK 465 LEU F 78 REMARK 465 THR F 79 REMARK 465 SER F 80 REMARK 465 PRO F 274 REMARK 465 TYR F 275 REMARK 465 SER G 223 REMARK 465 CYS J 215 REMARK 465 MET K -24 REMARK 465 ALA K -23 REMARK 465 PRO K -22 REMARK 465 THR K -21 REMARK 465 LYS K -20 REMARK 465 ARG K -19 REMARK 465 LYS K -18 REMARK 465 GLY K -17 REMARK 465 GLU K -16 REMARK 465 CYS K -15 REMARK 465 PRO K -14 REMARK 465 GLY K -13 REMARK 465 ALA K -12 REMARK 465 ALA K -11 REMARK 465 PRO K -10 REMARK 465 LYS K -9 REMARK 465 LYS K -8 REMARK 465 PRO K -7 REMARK 465 LYS K -6 REMARK 465 GLU K -5 REMARK 465 PRO K -4 REMARK 465 VAL K -3 REMARK 465 GLN K -2 REMARK 465 VAL K -1 REMARK 465 PRO K 0 REMARK 465 LYS K 1 REMARK 465 LEU K 2 REMARK 465 SER M 223 REMARK 465 CYS N 215 REMARK 465 MET O -24 REMARK 465 ALA O -23 REMARK 465 PRO O -22 REMARK 465 THR O -21 REMARK 465 LYS O -20 REMARK 465 ARG O -19 REMARK 465 LYS O -18 REMARK 465 GLY O -17 REMARK 465 GLU O -16 REMARK 465 CYS O -15 REMARK 465 PRO O -14 REMARK 465 GLY O -13 REMARK 465 ALA O -12 REMARK 465 ALA O -11 REMARK 465 PRO O -10 REMARK 465 LYS O -9 REMARK 465 LYS O -8 REMARK 465 PRO O -7 REMARK 465 LYS O -6 REMARK 465 GLU O -5 REMARK 465 PRO O -4 REMARK 465 VAL O -3 REMARK 465 GLN O -2 REMARK 465 VAL O -1 REMARK 465 PRO O 0 REMARK 465 LYS O 1 REMARK 465 LEU O 2 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 GLN H 1 CD OE1 NE2 REMARK 480 GLN H 5 CD OE1 NE2 REMARK 480 LYS H 13 CE NZ REMARK 480 ARG H 26 CD NE CZ NH1 NH2 REMARK 480 LYS H 43 NZ REMARK 480 ARG H 64 CD NE CZ NH1 NH2 REMARK 480 LYS H 76 NZ REMARK 480 LYS H 81 NZ REMARK 480 ARG H 83 NE CZ NH1 NH2 REMARK 480 THR H 143 OG1 CG2 REMARK 480 SER H 169 OG REMARK 480 SER H 180 OG REMARK 480 SER H 195 OG REMARK 480 SER H 196 OG REMARK 480 LEU H 197 CD1 CD2 REMARK 480 THR H 199 OG1 CG2 REMARK 480 GLN H 200 CD OE1 NE2 REMARK 480 ILE H 203 CD1 REMARK 480 LYS H 209 CD CE NZ REMARK 480 LYS H 214 CE NZ REMARK 480 LYS H 217 NZ REMARK 480 LYS H 218 CG CD CE NZ REMARK 480 VAL H 219 CG1 CG2 REMARK 480 GLU H 220 CD OE1 OE2 REMARK 480 ARG L 24 CZ NH1 NH2 REMARK 480 LYS L 108 NZ REMARK 480 ILE L 118 CD1 REMARK 480 SER L 122 OG REMARK 480 ASP L 123 CG OD1 OD2 REMARK 480 LYS L 127 CE NZ REMARK 480 LYS L 146 CD CE NZ REMARK 480 GLN L 148 CD OE1 NE2 REMARK 480 LYS L 150 NZ REMARK 480 ASN L 153 CG OD1 ND2 REMARK 480 LEU L 155 CG CD1 CD2 REMARK 480 SER L 157 OG REMARK 480 LYS L 170 CG CD CE NZ REMARK 480 LYS L 189 NZ REMARK 480 LYS L 191 CE NZ REMARK 480 GLU L 196 CD OE1 OE2 REMARK 480 SER L 204 OG REMARK 480 VAL L 206 CG1 CG2 REMARK 480 LYS L 208 CE NZ REMARK 480 PHE L 210 CG CD1 CD2 CE1 CE2 CZ REMARK 480 ASN L 211 CG OD1 ND2 REMARK 480 LEU P 2 CD1 CD2 REMARK 480 ILE P 4 CD1 REMARK 480 GLU P 12 CD OE1 OE2 REMARK 480 LYS P 14 CE NZ REMARK 480 THR P 15 OG1 CG2 REMARK 480 VAL P 17 CG1 CG2 REMARK 480 ASP P 18 CG OD1 OD2 REMARK 480 GLU P 223 CD OE1 OE2 REMARK 480 ARG P 265 CZ NH1 NH2 REMARK 480 GLN A 1 CD OE1 NE2 REMARK 480 GLN A 5 CD OE1 NE2 REMARK 480 ARG A 26 NE CZ NH1 NH2 REMARK 480 LYS A 43 CD CE NZ REMARK 480 ARG A 64 CD NE CZ NH1 NH2 REMARK 480 LYS A 75 NZ REMARK 480 LYS A 209 CG CD CE NZ REMARK 480 LYS A 214 CD CE NZ REMARK 480 LYS A 218 NZ REMARK 480 LYS A 222 CG CD CE NZ REMARK 480 ARG B 24 CZ NH1 NH2 REMARK 480 ARG B 78 NE CZ NH1 NH2 REMARK 480 LYS B 108 NZ REMARK 480 LYS B 127 NZ REMARK 480 SER B 128 OG REMARK 480 GLU B 144 CD OE1 OE2 REMARK 480 LYS B 146 CD CE NZ REMARK 480 ASN B 159 CG OD1 ND2 REMARK 480 GLU B 166 CD OE1 OE2 REMARK 480 LYS B 170 CD CE NZ REMARK 480 LYS B 189 NZ REMARK 480 GLU B 214 CD OE1 OE2 REMARK 480 CYS B 215 SG REMARK 480 LEU C 2 CG CD1 CD2 REMARK 480 LEU C 3 CD1 CD2 REMARK 480 ILE C 4 CD1 REMARK 480 LYS C 5 CE NZ REMARK 480 LYS C 14 NZ REMARK 480 LYS C 156 CD CE NZ REMARK 480 LYS C 272 NZ REMARK 480 ASN C 273 CG OD1 ND2 REMARK 480 GLN D 1 CG CD OE1 NE2 REMARK 480 GLN D 5 CD OE1 NE2 REMARK 480 LYS D 13 CE NZ REMARK 480 ARG D 26 NE CZ NH1 NH2 REMARK 480 LYS D 43 CE NZ REMARK 480 ARG D 64 CG CD NE CZ NH1 NH2 REMARK 480 LYS D 76 CE NZ REMARK 480 LYS D 81 CE NZ REMARK 480 GLN D 113 CD OE1 NE2 REMARK 480 SER D 123 OG REMARK 480 LYS D 151 CE NZ REMARK 480 SER D 180 OG REMARK 480 LYS D 209 CE NZ REMARK 480 LYS D 214 CD CE NZ REMARK 480 LYS D 218 CD CE NZ REMARK 480 GLU D 220 CD OE1 OE2 REMARK 480 LYS D 222 CE NZ REMARK 480 SER D 223 OG REMARK 480 ARG E 78 CZ NH1 NH2 REMARK 480 ILE E 107 CD1 REMARK 480 LYS E 108 CE NZ REMARK 480 GLU E 124 CD OE1 OE2 REMARK 480 LYS E 127 CD CE NZ REMARK 480 GLU E 144 CD OE1 OE2 REMARK 480 LYS E 146 CG CD CE NZ REMARK 480 VAL E 147 CG1 CG2 REMARK 480 GLN E 148 CD OE1 NE2 REMARK 480 LYS E 150 CG CD CE NZ REMARK 480 ASN E 153 CG OD1 ND2 REMARK 480 LEU E 155 CG CD1 CD2 REMARK 480 SER E 157 OG REMARK 480 GLN E 161 CD OE1 NE2 REMARK 480 SER E 169 OG REMARK 480 LYS E 170 CD CE NZ REMARK 480 LEU E 182 CG CD1 CD2 REMARK 480 LYS E 184 CD CE NZ REMARK 480 GLU E 188 CD OE1 OE2 REMARK 480 LYS E 189 NZ REMARK 480 LYS E 191 CD CE NZ REMARK 480 GLU E 196 CD OE1 OE2 REMARK 480 SER E 204 OG REMARK 480 ARG E 212 CD NE CZ NH1 NH2 REMARK 480 LEU F 2 CD1 CD2 REMARK 480 ILE F 4 CD1 REMARK 480 LYS F 5 CD CE NZ REMARK 480 GLU F 12 CD OE1 OE2 REMARK 480 LYS F 14 NZ REMARK 480 VAL F 17 CG1 CG2 REMARK 480 ASP F 18 CG OD1 OD2 REMARK 480 ASN F 73 CG OD1 ND2 REMARK 480 LYS F 156 CE NZ REMARK 480 LYS F 231 NZ REMARK 480 GLN G 1 CD OE1 NE2 REMARK 480 LYS G 13 NZ REMARK 480 LYS G 43 NZ REMARK 480 ARG G 64 NE CZ NH1 NH2 REMARK 480 SER G 136 OG REMARK 480 LYS G 137 NZ REMARK 480 THR G 139 OG1 CG2 REMARK 480 SER G 140 OG REMARK 480 LYS G 209 NZ REMARK 480 LYS G 214 NZ REMARK 480 LYS G 217 NZ REMARK 480 LYS G 218 NZ REMARK 480 GLU G 220 CG CD OE1 OE2 REMARK 480 LYS G 222 CG CD CE NZ REMARK 480 ARG J 24 CZ NH1 NH2 REMARK 480 ARG J 78 CZ NH1 NH2 REMARK 480 LYS J 146 CD CE NZ REMARK 480 LYS J 150 CE NZ REMARK 480 LEU J 155 CD1 CD2 REMARK 480 LYS J 170 CE NZ REMARK 480 LYS J 189 NZ REMARK 480 LYS J 191 CE NZ REMARK 480 GLU J 214 CG CD OE1 OE2 REMARK 480 ILE K 4 CD1 REMARK 480 LYS K 5 CD CE NZ REMARK 480 LYS K 14 NZ REMARK 480 THR K 15 OG1 CG2 REMARK 480 VAL K 17 CG1 CG2 REMARK 480 ASP K 18 CG OD1 OD2 REMARK 480 GLN M 1 CD OE1 NE2 REMARK 480 GLN M 5 CD OE1 NE2 REMARK 480 LYS M 43 NZ REMARK 480 GLN M 113 CD OE1 NE2 REMARK 480 SER M 136 OG REMARK 480 LYS M 137 CE NZ REMARK 480 LYS M 209 CE NZ REMARK 480 LYS M 218 NZ REMARK 480 LYS M 222 NZ REMARK 480 ARG N 24 CZ NH1 NH2 REMARK 480 ARG N 78 CZ NH1 NH2 REMARK 480 LYS N 146 CE NZ REMARK 480 LYS N 170 CD CE NZ REMARK 480 LYS N 184 NZ REMARK 480 LYS N 208 NZ REMARK 480 GLU N 214 CD OE1 OE2 REMARK 480 ILE O 4 CD1 REMARK 480 GLU O 12 CD OE1 OE2 REMARK 480 LYS O 14 CE NZ REMARK 480 VAL O 17 CG1 CG2 REMARK 480 ASP O 18 CG OD1 OD2 REMARK 480 ILE O 20 CD1 REMARK 480 LYS O 156 CE NZ REMARK 480 GLU O 192 CD OE1 OE2 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 SER H 15 -16.20 88.97 REMARK 500 ASP H 109 57.73 -143.26 REMARK 500 ALA L 52 -40.86 73.87 REMARK 500 VAL L 85 -156.86 -137.20 REMARK 500 SER L 157 -55.77 -144.38 REMARK 500 LEU P 11 -154.57 -109.98 REMARK 500 THR P 15 79.67 -109.46 REMARK 500 ASP P 18 39.40 -98.02 REMARK 500 LEU P 38 52.83 -108.94 REMARK 500 HIS P 114 -2.15 75.63 REMARK 500 VAL P 164 -123.90 -116.85 REMARK 500 ALA P 178 -43.70 -137.74 REMARK 500 ARG P 190 -144.37 -129.56 REMARK 500 ARG P 190 -144.27 -129.66 REMARK 500 SER A 15 -16.63 89.15 REMARK 500 ASP A 109 59.67 -147.92 REMARK 500 ALA B 52 -40.54 73.90 REMARK 500 VAL B 85 -155.91 -136.60 REMARK 500 GLU B 214 95.69 -167.95 REMARK 500 LEU C 11 -156.22 -109.29 REMARK 500 LEU C 38 55.51 -112.51 REMARK 500 LEU C 38 55.39 -112.51 REMARK 500 GLU C 48 33.00 70.29 REMARK 500 HIS C 114 -3.13 75.67 REMARK 500 VAL C 164 -123.00 -116.47 REMARK 500 ALA C 178 -41.31 -133.48 REMARK 500 ARG C 190 -143.68 -131.24 REMARK 500 ARG C 190 -144.23 -130.98 REMARK 500 SER D 15 -17.08 89.76 REMARK 500 ASP D 109 57.37 -146.46 REMARK 500 ALA E 52 -41.16 73.64 REMARK 500 VAL E 85 -157.40 -136.28 REMARK 500 SER E 157 -49.99 -132.85 REMARK 500 LEU F 11 -154.61 -109.09 REMARK 500 THR F 15 64.17 -110.30 REMARK 500 ASP F 18 42.47 -100.09 REMARK 500 LEU F 38 51.14 -115.55 REMARK 500 HIS F 114 -2.88 75.76 REMARK 500 VAL F 164 -121.17 -115.72 REMARK 500 ALA F 178 -40.90 -134.74 REMARK 500 ARG F 190 -143.59 -129.62 REMARK 500 SER G 15 -17.12 87.87 REMARK 500 ASP G 109 54.95 -142.63 REMARK 500 ASP G 152 60.82 68.88 REMARK 500 ALA J 52 -40.14 73.72 REMARK 500 VAL J 85 -157.34 -137.26 REMARK 500 LEU K 11 -153.25 -108.85 REMARK 500 HIS K 114 -2.46 75.38 REMARK 500 VAL K 164 -121.97 -115.78 REMARK 500 ALA K 178 -42.51 -137.10 REMARK 500 REMARK 500 THIS ENTRY HAS 64 RAMACHANDRAN OUTLIERS. 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 508 DISTANCE = 6.40 ANGSTROMS REMARK 525 HOH K 622 DISTANCE = 6.20 ANGSTROMS DBREF 9RM2 H 1 223 PDB 9RM2 9RM2 1 223 DBREF 9RM2 L 1 215 PDB 9RM2 9RM2 1 215 DBREF 9RM2 P -24 275 UNP P03088 VP1_POVBK 1 300 DBREF 9RM2 A 1 223 PDB 9RM2 9RM2 1 223 DBREF 9RM2 B 1 215 PDB 9RM2 9RM2 1 215 DBREF 9RM2 C -24 275 UNP P03088 VP1_POVBK 1 300 DBREF 9RM2 D 1 223 PDB 9RM2 9RM2 1 223 DBREF 9RM2 E 1 215 PDB 9RM2 9RM2 1 215 DBREF 9RM2 F -24 275 UNP P03088 VP1_POVBK 1 300 DBREF 9RM2 G 1 223 PDB 9RM2 9RM2 1 223 DBREF 9RM2 J 1 215 PDB 9RM2 9RM2 1 215 DBREF 9RM2 K -24 275 UNP P03088 VP1_POVBK 1 300 DBREF 9RM2 M 1 223 PDB 9RM2 9RM2 1 223 DBREF 9RM2 N 1 215 PDB 9RM2 9RM2 1 215 DBREF 9RM2 O -24 275 UNP P03088 VP1_POVBK 1 300 SEQADV 9RM2 SER P 80 UNP P03088 CYS 105 ENGINEERED MUTATION SEQADV 9RM2 ASP P 133 UNP P03088 GLU 158 VARIANT SEQADV 9RM2 THR P 146 UNP P03088 SER 171 VARIANT SEQADV 9RM2 THR P 194 UNP P03088 ALA 219 VARIANT SEQADV 9RM2 SER C 80 UNP P03088 CYS 105 ENGINEERED MUTATION SEQADV 9RM2 ASP C 133 UNP P03088 GLU 158 VARIANT SEQADV 9RM2 THR C 146 UNP P03088 SER 171 VARIANT SEQADV 9RM2 THR C 194 UNP P03088 ALA 219 VARIANT SEQADV 9RM2 SER F 80 UNP P03088 CYS 105 ENGINEERED MUTATION SEQADV 9RM2 ASP F 133 UNP P03088 GLU 158 VARIANT SEQADV 9RM2 THR F 146 UNP P03088 SER 171 VARIANT SEQADV 9RM2 THR F 194 UNP P03088 ALA 219 VARIANT SEQADV 9RM2 SER K 80 UNP P03088 CYS 105 ENGINEERED MUTATION SEQADV 9RM2 ASP K 133 UNP P03088 GLU 158 VARIANT SEQADV 9RM2 THR K 146 UNP P03088 SER 171 VARIANT SEQADV 9RM2 THR K 194 UNP P03088 ALA 219 VARIANT SEQADV 9RM2 SER O 80 UNP P03088 CYS 105 ENGINEERED MUTATION SEQADV 9RM2 ASP O 133 UNP P03088 GLU 158 VARIANT SEQADV 9RM2 THR O 146 UNP P03088 SER 171 VARIANT SEQADV 9RM2 THR O 194 UNP P03088 ALA 219 VARIANT SEQRES 1 H 223 GLN VAL GLN LEU GLN GLN TRP GLY ALA GLY LEU LEU LYS SEQRES 2 H 223 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL TYR ARG SEQRES 3 H 223 GLY SER PHE SER ALA TYR TYR TRP THR TRP PHE ARG GLN SEQRES 4 H 223 PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY GLU ILE ASN SEQRES 5 H 223 HIS ARG GLY TYR THR ASN TYR ASN PRO SER LEU ARG GLY SEQRES 6 H 223 ARG VAL SER ILE SER VAL ASP THR SER LYS LYS GLN PHE SEQRES 7 H 223 SER LEU LYS LEU ARG SER VAL ASN ALA ALA ASP THR ALA SEQRES 8 H 223 VAL TYR TYR CYS ALA THR LEU ARG SER THR SER GLY TRP SEQRES 9 H 223 HIS ASP TYR PHE ASP TYR TRP GLY GLN GLY THR LEU VAL SEQRES 10 H 223 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 H 223 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 H 223 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 H 223 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 H 223 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 H 223 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 H 223 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 H 223 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 18 H 223 LYS SER SEQRES 1 L 215 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 L 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 215 GLN SER VAL SER SER SER TYR LEU ALA TRP TYR GLN GLN SEQRES 4 L 215 THR PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SEQRES 5 L 215 SER SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 L 215 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG SEQRES 7 L 215 LEU GLU PRO GLU ASP PHE VAL VAL TYR PHE CYS LEU GLN SEQRES 8 L 215 TYR GLY SER SER PRO LEU THR PHE GLY PRO GLY THR LYS SEQRES 9 L 215 VAL ASP ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 L 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 L 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 P 300 MET ALA PRO THR LYS ARG LYS GLY GLU CYS PRO GLY ALA SEQRES 2 P 300 ALA PRO LYS LYS PRO LYS GLU PRO VAL GLN VAL PRO LYS SEQRES 3 P 300 LEU LEU ILE LYS GLY GLY VAL GLU VAL LEU GLU VAL LYS SEQRES 4 P 300 THR GLY VAL ASP ALA ILE THR GLU VAL GLU CYS PHE LEU SEQRES 5 P 300 ASN PRO GLU MET GLY ASP PRO ASP GLU ASN LEU ARG GLY SEQRES 6 P 300 PHE SER LEU LYS LEU SER ALA GLU ASN ASP PHE SER SER SEQRES 7 P 300 ASP SER PRO GLU ARG LYS MET LEU PRO CYS TYR SER THR SEQRES 8 P 300 ALA ARG ILE PRO LEU PRO ASN LEU ASN GLU ASP LEU THR SEQRES 9 P 300 SER GLY ASN LEU LEU MET TRP GLU ALA VAL THR VAL GLN SEQRES 10 P 300 THR GLU VAL ILE GLY ILE THR SER MET LEU ASN LEU HIS SEQRES 11 P 300 ALA GLY SER GLN LYS VAL HIS GLU HIS GLY GLY GLY LYS SEQRES 12 P 300 PRO ILE GLN GLY SER ASN PHE HIS PHE PHE ALA VAL GLY SEQRES 13 P 300 GLY ASP PRO LEU GLU MET GLN GLY VAL LEU MET ASN TYR SEQRES 14 P 300 ARG THR LYS TYR PRO ASP GLY THR ILE THR PRO LYS ASN SEQRES 15 P 300 PRO THR ALA GLN SER GLN VAL MET ASN THR ASP HIS LYS SEQRES 16 P 300 ALA TYR LEU ASP LYS ASN ASN ALA TYR PRO VAL GLU CYS SEQRES 17 P 300 TRP VAL PRO ASP PRO SER ARG ASN GLU ASN THR ARG TYR SEQRES 18 P 300 PHE GLY THR PHE THR GLY GLY GLU ASN VAL PRO PRO VAL SEQRES 19 P 300 LEU HIS VAL THR ASN THR ALA THR THR VAL LEU LEU ASP SEQRES 20 P 300 GLU GLN GLY VAL GLY PRO LEU CYS LYS ALA ASP SER LEU SEQRES 21 P 300 TYR VAL SER ALA ALA ASP ILE CYS GLY LEU PHE THR ASN SEQRES 22 P 300 SER SER GLY THR GLN GLN TRP ARG GLY LEU ALA ARG TYR SEQRES 23 P 300 PHE LYS ILE ARG LEU ARG LYS ARG SER VAL LYS ASN PRO SEQRES 24 P 300 TYR SEQRES 1 A 223 GLN VAL GLN LEU GLN GLN TRP GLY ALA GLY LEU LEU LYS SEQRES 2 A 223 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL TYR ARG SEQRES 3 A 223 GLY SER PHE SER ALA TYR TYR TRP THR TRP PHE ARG GLN SEQRES 4 A 223 PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY GLU ILE ASN SEQRES 5 A 223 HIS ARG GLY TYR THR ASN TYR ASN PRO SER LEU ARG GLY SEQRES 6 A 223 ARG VAL SER ILE SER VAL ASP THR SER LYS LYS GLN PHE SEQRES 7 A 223 SER LEU LYS LEU ARG SER VAL ASN ALA ALA ASP THR ALA SEQRES 8 A 223 VAL TYR TYR CYS ALA THR LEU ARG SER THR SER GLY TRP SEQRES 9 A 223 HIS ASP TYR PHE ASP TYR TRP GLY GLN GLY THR LEU VAL SEQRES 10 A 223 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 A 223 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 A 223 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 A 223 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 A 223 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 A 223 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 A 223 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 A 223 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 18 A 223 LYS SER SEQRES 1 B 215 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 B 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 B 215 GLN SER VAL SER SER SER TYR LEU ALA TRP TYR GLN GLN SEQRES 4 B 215 THR PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SEQRES 5 B 215 SER SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 B 215 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG SEQRES 7 B 215 LEU GLU PRO GLU ASP PHE VAL VAL TYR PHE CYS LEU GLN SEQRES 8 B 215 TYR GLY SER SER PRO LEU THR PHE GLY PRO GLY THR LYS SEQRES 9 B 215 VAL ASP ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 B 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 B 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 B 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 B 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 B 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 B 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 B 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 B 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 C 300 MET ALA PRO THR LYS ARG LYS GLY GLU CYS PRO GLY ALA SEQRES 2 C 300 ALA PRO LYS LYS PRO LYS GLU PRO VAL GLN VAL PRO LYS SEQRES 3 C 300 LEU LEU ILE LYS GLY GLY VAL GLU VAL LEU GLU VAL LYS SEQRES 4 C 300 THR GLY VAL ASP ALA ILE THR GLU VAL GLU CYS PHE LEU SEQRES 5 C 300 ASN PRO GLU MET GLY ASP PRO ASP GLU ASN LEU ARG GLY SEQRES 6 C 300 PHE SER LEU LYS LEU SER ALA GLU ASN ASP PHE SER SER SEQRES 7 C 300 ASP SER PRO GLU ARG LYS MET LEU PRO CYS TYR SER THR SEQRES 8 C 300 ALA ARG ILE PRO LEU PRO ASN LEU ASN GLU ASP LEU THR SEQRES 9 C 300 SER GLY ASN LEU LEU MET TRP GLU ALA VAL THR VAL GLN SEQRES 10 C 300 THR GLU VAL ILE GLY ILE THR SER MET LEU ASN LEU HIS SEQRES 11 C 300 ALA GLY SER GLN LYS VAL HIS GLU HIS GLY GLY GLY LYS SEQRES 12 C 300 PRO ILE GLN GLY SER ASN PHE HIS PHE PHE ALA VAL GLY SEQRES 13 C 300 GLY ASP PRO LEU GLU MET GLN GLY VAL LEU MET ASN TYR SEQRES 14 C 300 ARG THR LYS TYR PRO ASP GLY THR ILE THR PRO LYS ASN SEQRES 15 C 300 PRO THR ALA GLN SER GLN VAL MET ASN THR ASP HIS LYS SEQRES 16 C 300 ALA TYR LEU ASP LYS ASN ASN ALA TYR PRO VAL GLU CYS SEQRES 17 C 300 TRP VAL PRO ASP PRO SER ARG ASN GLU ASN THR ARG TYR SEQRES 18 C 300 PHE GLY THR PHE THR GLY GLY GLU ASN VAL PRO PRO VAL SEQRES 19 C 300 LEU HIS VAL THR ASN THR ALA THR THR VAL LEU LEU ASP SEQRES 20 C 300 GLU GLN GLY VAL GLY PRO LEU CYS LYS ALA ASP SER LEU SEQRES 21 C 300 TYR VAL SER ALA ALA ASP ILE CYS GLY LEU PHE THR ASN SEQRES 22 C 300 SER SER GLY THR GLN GLN TRP ARG GLY LEU ALA ARG TYR SEQRES 23 C 300 PHE LYS ILE ARG LEU ARG LYS ARG SER VAL LYS ASN PRO SEQRES 24 C 300 TYR SEQRES 1 D 223 GLN VAL GLN LEU GLN GLN TRP GLY ALA GLY LEU LEU LYS SEQRES 2 D 223 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL TYR ARG SEQRES 3 D 223 GLY SER PHE SER ALA TYR TYR TRP THR TRP PHE ARG GLN SEQRES 4 D 223 PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY GLU ILE ASN SEQRES 5 D 223 HIS ARG GLY TYR THR ASN TYR ASN PRO SER LEU ARG GLY SEQRES 6 D 223 ARG VAL SER ILE SER VAL ASP THR SER LYS LYS GLN PHE SEQRES 7 D 223 SER LEU LYS LEU ARG SER VAL ASN ALA ALA ASP THR ALA SEQRES 8 D 223 VAL TYR TYR CYS ALA THR LEU ARG SER THR SER GLY TRP SEQRES 9 D 223 HIS ASP TYR PHE ASP TYR TRP GLY GLN GLY THR LEU VAL SEQRES 10 D 223 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 D 223 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 D 223 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 D 223 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 D 223 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 D 223 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 D 223 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 D 223 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 18 D 223 LYS SER SEQRES 1 E 215 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 E 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 E 215 GLN SER VAL SER SER SER TYR LEU ALA TRP TYR GLN GLN SEQRES 4 E 215 THR PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SEQRES 5 E 215 SER SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 E 215 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG SEQRES 7 E 215 LEU GLU PRO GLU ASP PHE VAL VAL TYR PHE CYS LEU GLN SEQRES 8 E 215 TYR GLY SER SER PRO LEU THR PHE GLY PRO GLY THR LYS SEQRES 9 E 215 VAL ASP ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 E 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 E 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 E 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 E 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 E 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 E 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 E 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 E 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 F 300 MET ALA PRO THR LYS ARG LYS GLY GLU CYS PRO GLY ALA SEQRES 2 F 300 ALA PRO LYS LYS PRO LYS GLU PRO VAL GLN VAL PRO LYS SEQRES 3 F 300 LEU LEU ILE LYS GLY GLY VAL GLU VAL LEU GLU VAL LYS SEQRES 4 F 300 THR GLY VAL ASP ALA ILE THR GLU VAL GLU CYS PHE LEU SEQRES 5 F 300 ASN PRO GLU MET GLY ASP PRO ASP GLU ASN LEU ARG GLY SEQRES 6 F 300 PHE SER LEU LYS LEU SER ALA GLU ASN ASP PHE SER SER SEQRES 7 F 300 ASP SER PRO GLU ARG LYS MET LEU PRO CYS TYR SER THR SEQRES 8 F 300 ALA ARG ILE PRO LEU PRO ASN LEU ASN GLU ASP LEU THR SEQRES 9 F 300 SER GLY ASN LEU LEU MET TRP GLU ALA VAL THR VAL GLN SEQRES 10 F 300 THR GLU VAL ILE GLY ILE THR SER MET LEU ASN LEU HIS SEQRES 11 F 300 ALA GLY SER GLN LYS VAL HIS GLU HIS GLY GLY GLY LYS SEQRES 12 F 300 PRO ILE GLN GLY SER ASN PHE HIS PHE PHE ALA VAL GLY SEQRES 13 F 300 GLY ASP PRO LEU GLU MET GLN GLY VAL LEU MET ASN TYR SEQRES 14 F 300 ARG THR LYS TYR PRO ASP GLY THR ILE THR PRO LYS ASN SEQRES 15 F 300 PRO THR ALA GLN SER GLN VAL MET ASN THR ASP HIS LYS SEQRES 16 F 300 ALA TYR LEU ASP LYS ASN ASN ALA TYR PRO VAL GLU CYS SEQRES 17 F 300 TRP VAL PRO ASP PRO SER ARG ASN GLU ASN THR ARG TYR SEQRES 18 F 300 PHE GLY THR PHE THR GLY GLY GLU ASN VAL PRO PRO VAL SEQRES 19 F 300 LEU HIS VAL THR ASN THR ALA THR THR VAL LEU LEU ASP SEQRES 20 F 300 GLU GLN GLY VAL GLY PRO LEU CYS LYS ALA ASP SER LEU SEQRES 21 F 300 TYR VAL SER ALA ALA ASP ILE CYS GLY LEU PHE THR ASN SEQRES 22 F 300 SER SER GLY THR GLN GLN TRP ARG GLY LEU ALA ARG TYR SEQRES 23 F 300 PHE LYS ILE ARG LEU ARG LYS ARG SER VAL LYS ASN PRO SEQRES 24 F 300 TYR SEQRES 1 G 223 GLN VAL GLN LEU GLN GLN TRP GLY ALA GLY LEU LEU LYS SEQRES 2 G 223 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL TYR ARG SEQRES 3 G 223 GLY SER PHE SER ALA TYR TYR TRP THR TRP PHE ARG GLN SEQRES 4 G 223 PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY GLU ILE ASN SEQRES 5 G 223 HIS ARG GLY TYR THR ASN TYR ASN PRO SER LEU ARG GLY SEQRES 6 G 223 ARG VAL SER ILE SER VAL ASP THR SER LYS LYS GLN PHE SEQRES 7 G 223 SER LEU LYS LEU ARG SER VAL ASN ALA ALA ASP THR ALA SEQRES 8 G 223 VAL TYR TYR CYS ALA THR LEU ARG SER THR SER GLY TRP SEQRES 9 G 223 HIS ASP TYR PHE ASP TYR TRP GLY GLN GLY THR LEU VAL SEQRES 10 G 223 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 G 223 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 G 223 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 G 223 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 G 223 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 G 223 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 G 223 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 G 223 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 18 G 223 LYS SER SEQRES 1 J 215 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 J 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 J 215 GLN SER VAL SER SER SER TYR LEU ALA TRP TYR GLN GLN SEQRES 4 J 215 THR PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SEQRES 5 J 215 SER SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 J 215 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG SEQRES 7 J 215 LEU GLU PRO GLU ASP PHE VAL VAL TYR PHE CYS LEU GLN SEQRES 8 J 215 TYR GLY SER SER PRO LEU THR PHE GLY PRO GLY THR LYS SEQRES 9 J 215 VAL ASP ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 J 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 J 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 J 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 J 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 J 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 J 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 J 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 J 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 K 300 MET ALA PRO THR LYS ARG LYS GLY GLU CYS PRO GLY ALA SEQRES 2 K 300 ALA PRO LYS LYS PRO LYS GLU PRO VAL GLN VAL PRO LYS SEQRES 3 K 300 LEU LEU ILE LYS GLY GLY VAL GLU VAL LEU GLU VAL LYS SEQRES 4 K 300 THR GLY VAL ASP ALA ILE THR GLU VAL GLU CYS PHE LEU SEQRES 5 K 300 ASN PRO GLU MET GLY ASP PRO ASP GLU ASN LEU ARG GLY SEQRES 6 K 300 PHE SER LEU LYS LEU SER ALA GLU ASN ASP PHE SER SER SEQRES 7 K 300 ASP SER PRO GLU ARG LYS MET LEU PRO CYS TYR SER THR SEQRES 8 K 300 ALA ARG ILE PRO LEU PRO ASN LEU ASN GLU ASP LEU THR SEQRES 9 K 300 SER GLY ASN LEU LEU MET TRP GLU ALA VAL THR VAL GLN SEQRES 10 K 300 THR GLU VAL ILE GLY ILE THR SER MET LEU ASN LEU HIS SEQRES 11 K 300 ALA GLY SER GLN LYS VAL HIS GLU HIS GLY GLY GLY LYS SEQRES 12 K 300 PRO ILE GLN GLY SER ASN PHE HIS PHE PHE ALA VAL GLY SEQRES 13 K 300 GLY ASP PRO LEU GLU MET GLN GLY VAL LEU MET ASN TYR SEQRES 14 K 300 ARG THR LYS TYR PRO ASP GLY THR ILE THR PRO LYS ASN SEQRES 15 K 300 PRO THR ALA GLN SER GLN VAL MET ASN THR ASP HIS LYS SEQRES 16 K 300 ALA TYR LEU ASP LYS ASN ASN ALA TYR PRO VAL GLU CYS SEQRES 17 K 300 TRP VAL PRO ASP PRO SER ARG ASN GLU ASN THR ARG TYR SEQRES 18 K 300 PHE GLY THR PHE THR GLY GLY GLU ASN VAL PRO PRO VAL SEQRES 19 K 300 LEU HIS VAL THR ASN THR ALA THR THR VAL LEU LEU ASP SEQRES 20 K 300 GLU GLN GLY VAL GLY PRO LEU CYS LYS ALA ASP SER LEU SEQRES 21 K 300 TYR VAL SER ALA ALA ASP ILE CYS GLY LEU PHE THR ASN SEQRES 22 K 300 SER SER GLY THR GLN GLN TRP ARG GLY LEU ALA ARG TYR SEQRES 23 K 300 PHE LYS ILE ARG LEU ARG LYS ARG SER VAL LYS ASN PRO SEQRES 24 K 300 TYR SEQRES 1 M 223 GLN VAL GLN LEU GLN GLN TRP GLY ALA GLY LEU LEU LYS SEQRES 2 M 223 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL TYR ARG SEQRES 3 M 223 GLY SER PHE SER ALA TYR TYR TRP THR TRP PHE ARG GLN SEQRES 4 M 223 PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY GLU ILE ASN SEQRES 5 M 223 HIS ARG GLY TYR THR ASN TYR ASN PRO SER LEU ARG GLY SEQRES 6 M 223 ARG VAL SER ILE SER VAL ASP THR SER LYS LYS GLN PHE SEQRES 7 M 223 SER LEU LYS LEU ARG SER VAL ASN ALA ALA ASP THR ALA SEQRES 8 M 223 VAL TYR TYR CYS ALA THR LEU ARG SER THR SER GLY TRP SEQRES 9 M 223 HIS ASP TYR PHE ASP TYR TRP GLY GLN GLY THR LEU VAL SEQRES 10 M 223 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 M 223 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 M 223 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 M 223 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 M 223 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 M 223 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 M 223 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 M 223 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 18 M 223 LYS SER SEQRES 1 N 215 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 N 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 N 215 GLN SER VAL SER SER SER TYR LEU ALA TRP TYR GLN GLN SEQRES 4 N 215 THR PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SEQRES 5 N 215 SER SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 N 215 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG SEQRES 7 N 215 LEU GLU PRO GLU ASP PHE VAL VAL TYR PHE CYS LEU GLN SEQRES 8 N 215 TYR GLY SER SER PRO LEU THR PHE GLY PRO GLY THR LYS SEQRES 9 N 215 VAL ASP ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 N 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 N 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 N 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 N 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 N 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 N 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 N 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 N 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 O 300 MET ALA PRO THR LYS ARG LYS GLY GLU CYS PRO GLY ALA SEQRES 2 O 300 ALA PRO LYS LYS PRO LYS GLU PRO VAL GLN VAL PRO LYS SEQRES 3 O 300 LEU LEU ILE LYS GLY GLY VAL GLU VAL LEU GLU VAL LYS SEQRES 4 O 300 THR GLY VAL ASP ALA ILE THR GLU VAL GLU CYS PHE LEU SEQRES 5 O 300 ASN PRO GLU MET GLY ASP PRO ASP GLU ASN LEU ARG GLY SEQRES 6 O 300 PHE SER LEU LYS LEU SER ALA GLU ASN ASP PHE SER SER SEQRES 7 O 300 ASP SER PRO GLU ARG LYS MET LEU PRO CYS TYR SER THR SEQRES 8 O 300 ALA ARG ILE PRO LEU PRO ASN LEU ASN GLU ASP LEU THR SEQRES 9 O 300 SER GLY ASN LEU LEU MET TRP GLU ALA VAL THR VAL GLN SEQRES 10 O 300 THR GLU VAL ILE GLY ILE THR SER MET LEU ASN LEU HIS SEQRES 11 O 300 ALA GLY SER GLN LYS VAL HIS GLU HIS GLY GLY GLY LYS SEQRES 12 O 300 PRO ILE GLN GLY SER ASN PHE HIS PHE PHE ALA VAL GLY SEQRES 13 O 300 GLY ASP PRO LEU GLU MET GLN GLY VAL LEU MET ASN TYR SEQRES 14 O 300 ARG THR LYS TYR PRO ASP GLY THR ILE THR PRO LYS ASN SEQRES 15 O 300 PRO THR ALA GLN SER GLN VAL MET ASN THR ASP HIS LYS SEQRES 16 O 300 ALA TYR LEU ASP LYS ASN ASN ALA TYR PRO VAL GLU CYS SEQRES 17 O 300 TRP VAL PRO ASP PRO SER ARG ASN GLU ASN THR ARG TYR SEQRES 18 O 300 PHE GLY THR PHE THR GLY GLY GLU ASN VAL PRO PRO VAL SEQRES 19 O 300 LEU HIS VAL THR ASN THR ALA THR THR VAL LEU LEU ASP SEQRES 20 O 300 GLU GLN GLY VAL GLY PRO LEU CYS LYS ALA ASP SER LEU SEQRES 21 O 300 TYR VAL SER ALA ALA ASP ILE CYS GLY LEU PHE THR ASN SEQRES 22 O 300 SER SER GLY THR GLN GLN TRP ARG GLY LEU ALA ARG TYR SEQRES 23 O 300 PHE LYS ILE ARG LEU ARG LYS ARG SER VAL LYS ASN PRO SEQRES 24 O 300 TYR HET CL H 301 1 HET PGE H 302 10 HET PGE H 303 10 HET EDO H 304 4 HET EDO H 305 4 HET PG4 L 301 13 HET PG5 L 302 12 HET CL P 301 1 HET PG4 P 302 13 HET PGE P 303 10 HET EDO P 304 4 HET CL A 301 1 HET PG4 B 301 13 HET PGE B 302 10 HET PGE B 303 10 HET PGE B 304 10 HET PEG B 305 7 HET EDO B 306 4 HET EDO B 307 4 HET CL C 301 1 HET PGE C 302 10 HET EDO C 303 4 HET EDO C 304 4 HET EDO D 301 4 HET PEG D 302 7 HET EDO D 303 4 HET EDO D 304 4 HET CL E 301 1 HET PGE E 302 10 HET PEG E 303 7 HET CL F 301 1 HET EDO F 302 4 HET PEG F 303 7 HET 1PE G 301 16 HET EDO G 302 4 HET PG5 J 301 12 HET EDO J 302 4 HET EDO J 303 4 HET P6G J 304 19 HET CL K 301 1 HET PEG K 302 7 HET PEG K 303 7 HET EDO K 304 4 HET EDO K 305 4 HET EDO K 306 4 HET EDO K 307 4 HET EDO K 308 4 HET CL M 301 1 HET PG4 M 302 13 HET PGE M 303 10 HET EDO M 304 4 HET EDO M 305 4 HET EDO M 306 4 HET EDO M 307 4 HET PG4 N 301 13 HET PG4 N 302 13 HET PEG N 303 7 HET CL O 301 1 HET PEG O 302 7 HET PEG O 303 7 HETNAM CL CHLORIDE ION HETNAM PGE TRIETHYLENE GLYCOL HETNAM EDO 1,2-ETHANEDIOL HETNAM PG4 TETRAETHYLENE GLYCOL HETNAM PG5 1-METHOXY-2-[2-(2-METHOXY-ETHOXY]-ETHANE HETNAM PEG DI(HYDROXYETHYL)ETHER HETNAM 1PE PENTAETHYLENE GLYCOL HETNAM P6G HEXAETHYLENE GLYCOL HETSYN EDO ETHYLENE GLYCOL HETSYN 1PE PEG400 HETSYN P6G POLYETHYLENE GLYCOL PEG400 FORMUL 16 CL 9(CL 1-) FORMUL 17 PGE 9(C6 H14 O4) FORMUL 19 EDO 23(C2 H6 O2) FORMUL 21 PG4 6(C8 H18 O5) FORMUL 22 PG5 2(C8 H18 O4) FORMUL 32 PEG 9(C4 H10 O3) FORMUL 49 1PE C10 H22 O6 FORMUL 54 P6G C12 H26 O7 FORMUL 76 HOH *2156(H2 O) HELIX 1 AA1 SER H 28 TYR H 32 5 5 HELIX 2 AA2 PRO H 61 ARG H 64 5 4 HELIX 3 AA3 ASN H 86 THR H 90 5 5 HELIX 4 AA4 SER H 164 ALA H 166 5 3 HELIX 5 AA5 SER H 195 GLY H 198 5 4 HELIX 6 AA6 LYS H 209 ASN H 212 5 4 HELIX 7 AA7 VAL L 29 SER L 32 5 4 HELIX 8 AA8 GLU L 80 PHE L 84 5 5 HELIX 9 AA9 SER L 122 SER L 128 1 7 HELIX 10 AB1 LYS L 184 LYS L 189 1 6 HELIX 11 AB2 GLU P 57 LEU P 61 5 5 HELIX 12 AB3 GLY P 97 ASN P 103 5 7 HELIX 13 AB4 THR P 159 VAL P 164 5 6 HELIX 14 AB5 PRO P 180 GLU P 182 5 3 HELIX 15 AB6 CYS P 230 ALA P 232 5 3 HELIX 16 AB7 SER A 28 TYR A 32 5 5 HELIX 17 AB8 PRO A 61 ARG A 64 5 4 HELIX 18 AB9 ASN A 86 THR A 90 5 5 HELIX 19 AC1 SER A 164 ALA A 166 5 3 HELIX 20 AC2 SER A 195 GLN A 200 1 6 HELIX 21 AC3 LYS A 209 ASN A 212 5 4 HELIX 22 AC4 VAL B 29 SER B 32 5 4 HELIX 23 AC5 GLU B 80 PHE B 84 5 5 HELIX 24 AC6 SER B 122 GLY B 129 1 8 HELIX 25 AC7 LYS B 184 LYS B 189 1 6 HELIX 26 AC8 GLU C 57 LEU C 61 5 5 HELIX 27 AC9 GLY C 97 ASN C 103 5 7 HELIX 28 AD1 THR C 159 VAL C 164 5 6 HELIX 29 AD2 PRO C 180 GLU C 182 5 3 HELIX 30 AD3 CYS C 230 ALA C 232 5 3 HELIX 31 AD4 SER D 28 TYR D 32 5 5 HELIX 32 AD5 PRO D 61 ARG D 64 5 4 HELIX 33 AD6 ASN D 86 THR D 90 5 5 HELIX 34 AD7 SER D 135 LYS D 137 5 3 HELIX 35 AD8 SER D 164 ALA D 166 5 3 HELIX 36 AD9 SER D 195 LEU D 197 5 3 HELIX 37 AE1 LYS D 209 ASN D 212 5 4 HELIX 38 AE2 VAL E 29 SER E 32 5 4 HELIX 39 AE3 GLU E 80 PHE E 84 5 5 HELIX 40 AE4 SER E 122 GLY E 129 1 8 HELIX 41 AE5 LYS E 184 LYS E 189 1 6 HELIX 42 AE6 GLU F 57 LEU F 61 5 5 HELIX 43 AE7 GLY F 97 ASN F 103 5 7 HELIX 44 AE8 THR F 159 VAL F 164 5 6 HELIX 45 AE9 PRO F 180 GLU F 182 5 3 HELIX 46 AF1 CYS F 230 ALA F 232 5 3 HELIX 47 AF2 SER G 28 TYR G 32 5 5 HELIX 48 AF3 PRO G 61 ARG G 64 5 4 HELIX 49 AF4 ASN G 86 THR G 90 5 5 HELIX 50 AF5 SER G 135 LYS G 137 5 3 HELIX 51 AF6 SER G 164 ALA G 166 5 3 HELIX 52 AF7 SER G 195 GLN G 200 1 6 HELIX 53 AF8 LYS G 209 ASN G 212 5 4 HELIX 54 AF9 VAL J 29 SER J 32 5 4 HELIX 55 AG1 GLU J 80 PHE J 84 5 5 HELIX 56 AG2 SER J 122 GLY J 129 1 8 HELIX 57 AG3 LYS J 184 LYS J 189 1 6 HELIX 58 AG4 GLU K 57 LEU K 61 5 5 HELIX 59 AG5 GLY K 97 ASN K 103 5 7 HELIX 60 AG6 THR K 159 VAL K 164 5 6 HELIX 61 AG7 PRO K 180 GLU K 182 5 3 HELIX 62 AG8 CYS K 230 ALA K 232 5 3 HELIX 63 AG9 SER M 28 TYR M 32 5 5 HELIX 64 AH1 PRO M 61 ARG M 64 5 4 HELIX 65 AH2 ASN M 86 THR M 90 5 5 HELIX 66 AH3 SER M 135 LYS M 137 5 3 HELIX 67 AH4 SER M 164 ALA M 166 5 3 HELIX 68 AH5 SER M 195 GLN M 200 1 6 HELIX 69 AH6 LYS M 209 ASN M 212 5 4 HELIX 70 AH7 VAL N 29 SER N 32 5 4 HELIX 71 AH8 GLU N 80 PHE N 84 5 5 HELIX 72 AH9 SER N 122 GLY N 129 1 8 HELIX 73 AI1 LYS N 184 LYS N 189 1 6 HELIX 74 AI2 GLU O 57 LEU O 61 5 5 HELIX 75 AI3 GLY O 97 ASN O 103 5 7 HELIX 76 AI4 THR O 159 VAL O 164 5 6 HELIX 77 AI5 PRO O 180 GLU O 182 5 3 HELIX 78 AI6 CYS O 230 ALA O 232 5 3 SHEET 1 AA1 4 GLN H 3 TRP H 7 0 SHEET 2 AA1 4 LEU H 18 ARG H 26 -1 O ALA H 23 N GLN H 5 SHEET 3 AA1 4 GLN H 77 LEU H 82 -1 O PHE H 78 N CYS H 22 SHEET 4 AA1 4 VAL H 67 ASP H 72 -1 N ASP H 72 O GLN H 77 SHEET 1 AA2 6 LEU H 11 LEU H 12 0 SHEET 2 AA2 6 THR H 115 VAL H 119 1 O THR H 118 N LEU H 12 SHEET 3 AA2 6 ALA H 91 SER H 100 -1 N ALA H 91 O VAL H 117 SHEET 4 AA2 6 TRP H 34 GLN H 39 -1 N THR H 35 O ALA H 96 SHEET 5 AA2 6 GLU H 46 ILE H 51 -1 O ILE H 51 N TRP H 34 SHEET 6 AA2 6 THR H 57 TYR H 59 -1 O ASN H 58 N GLU H 50 SHEET 1 AA3 4 LEU H 11 LEU H 12 0 SHEET 2 AA3 4 THR H 115 VAL H 119 1 O THR H 118 N LEU H 12 SHEET 3 AA3 4 ALA H 91 SER H 100 -1 N ALA H 91 O VAL H 117 SHEET 4 AA3 4 GLY H 103 TRP H 111 -1 O PHE H 108 N LEU H 98 SHEET 1 AA4 4 SER H 128 LEU H 132 0 SHEET 2 AA4 4 THR H 143 TYR H 153 -1 O LEU H 149 N PHE H 130 SHEET 3 AA4 4 TYR H 184 PRO H 193 -1 O TYR H 184 N TYR H 153 SHEET 4 AA4 4 VAL H 171 THR H 173 -1 N HIS H 172 O VAL H 189 SHEET 1 AA5 4 SER H 128 LEU H 132 0 SHEET 2 AA5 4 THR H 143 TYR H 153 -1 O LEU H 149 N PHE H 130 SHEET 3 AA5 4 TYR H 184 PRO H 193 -1 O TYR H 184 N TYR H 153 SHEET 4 AA5 4 VAL H 177 LEU H 178 -1 N VAL H 177 O SER H 185 SHEET 1 AA6 3 THR H 159 TRP H 162 0 SHEET 2 AA6 3 ILE H 203 HIS H 208 -1 O ASN H 205 N SER H 161 SHEET 3 AA6 3 THR H 213 LYS H 218 -1 O THR H 213 N HIS H 208 SHEET 1 AA7 4 LEU L 4 SER L 7 0 SHEET 2 AA7 4 ALA L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA7 4 ASP L 71 ILE L 76 -1 O LEU L 74 N LEU L 21 SHEET 4 AA7 4 PHE L 63 SER L 68 -1 N SER L 64 O THR L 75 SHEET 1 AA8 6 THR L 10 LEU L 13 0 SHEET 2 AA8 6 THR L 103 ILE L 107 1 O ASP L 106 N LEU L 11 SHEET 3 AA8 6 VAL L 86 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AA8 6 LEU L 34 GLN L 39 -1 N TYR L 37 O PHE L 88 SHEET 5 AA8 6 ARG L 46 TYR L 50 -1 O ARG L 46 N GLN L 38 SHEET 6 AA8 6 SER L 54 ARG L 55 -1 O SER L 54 N TYR L 50 SHEET 1 AA9 4 THR L 10 LEU L 13 0 SHEET 2 AA9 4 THR L 103 ILE L 107 1 O ASP L 106 N LEU L 11 SHEET 3 AA9 4 VAL L 86 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AA9 4 THR L 98 PHE L 99 -1 O THR L 98 N GLN L 91 SHEET 1 AB1 4 SER L 115 PHE L 119 0 SHEET 2 AB1 4 THR L 130 PHE L 140 -1 O LEU L 136 N PHE L 117 SHEET 3 AB1 4 TYR L 174 SER L 183 -1 O LEU L 182 N ALA L 131 SHEET 4 AB1 4 SER L 160 VAL L 164 -1 N SER L 163 O SER L 177 SHEET 1 AB2 4 ALA L 154 LEU L 155 0 SHEET 2 AB2 4 LYS L 146 VAL L 151 -1 N VAL L 151 O ALA L 154 SHEET 3 AB2 4 VAL L 192 THR L 198 -1 O GLU L 196 N GLN L 148 SHEET 4 AB2 4 VAL L 206 ASN L 211 -1 O VAL L 206 N VAL L 197 SHEET 1 AB3 4 LEU P 3 ILE P 4 0 SHEET 2 AB3 4 GLU P 9 VAL P 13 -1 O VAL P 10 N LEU P 3 SHEET 3 AB3 4 ALA P 259 LYS P 272 -1 O SER P 270 N LEU P 11 SHEET 4 AB3 4 ILE P 20 LEU P 27 -1 N THR P 21 O LEU P 266 SHEET 1 AB4 5 LEU P 3 ILE P 4 0 SHEET 2 AB4 5 GLU P 9 VAL P 13 -1 O VAL P 10 N LEU P 3 SHEET 3 AB4 5 ALA P 259 LYS P 272 -1 O SER P 270 N LEU P 11 SHEET 4 AB4 5 ASN P 82 ILE P 96 -1 N VAL P 89 O ARG P 265 SHEET 5 AB4 5 THR P 218 VAL P 219 -1 O THR P 218 N VAL P 91 SHEET 1 AB5 3 SER P 65 PRO P 70 0 SHEET 2 AB5 3 SER P 234 THR P 247 -1 O LEU P 235 N ILE P 69 SHEET 3 AB5 3 GLN P 253 GLY P 257 -1 O GLN P 254 N PHE P 246 SHEET 1 AB6 5 SER P 65 PRO P 70 0 SHEET 2 AB6 5 SER P 234 THR P 247 -1 O LEU P 235 N ILE P 69 SHEET 3 AB6 5 ASN P 124 GLY P 131 -1 N GLY P 131 O TYR P 236 SHEET 4 AB6 5 THR P 194 THR P 201 -1 O ARG P 195 N VAL P 130 SHEET 5 AB6 5 VAL O 209 THR O 213 -1 O LEU O 210 N PHE P 200 SHEET 1 AB7 3 LYS P 170 TYR P 172 0 SHEET 2 AB7 3 GLU P 136 GLY P 139 -1 N MET P 137 O ALA P 171 SHEET 3 AB7 3 TRP P 184 PRO P 186 -1 O VAL P 185 N GLN P 138 SHEET 1 AB8 5 VAL P 209 THR P 213 0 SHEET 2 AB8 5 THR C 194 THR C 201 -1 O PHE C 200 N LEU P 210 SHEET 3 AB8 5 ASN C 124 GLY C 131 -1 N ASN C 124 O THR C 201 SHEET 4 AB8 5 SER C 234 THR C 247 -1 O TYR C 236 N GLY C 131 SHEET 5 AB8 5 SER C 65 PRO C 70 -1 N ILE C 69 O LEU C 235 SHEET 1 AB9 5 VAL P 209 THR P 213 0 SHEET 2 AB9 5 THR C 194 THR C 201 -1 O PHE C 200 N LEU P 210 SHEET 3 AB9 5 ASN C 124 GLY C 131 -1 N ASN C 124 O THR C 201 SHEET 4 AB9 5 SER C 234 THR C 247 -1 O TYR C 236 N GLY C 131 SHEET 5 AB9 5 GLN C 253 GLY C 257 -1 O GLN C 254 N PHE C 246 SHEET 1 AC1 4 GLN A 3 TRP A 7 0 SHEET 2 AC1 4 LEU A 18 ARG A 26 -1 O ALA A 23 N GLN A 5 SHEET 3 AC1 4 GLN A 77 LEU A 82 -1 O PHE A 78 N CYS A 22 SHEET 4 AC1 4 VAL A 67 ASP A 72 -1 N ASP A 72 O GLN A 77 SHEET 1 AC2 6 LEU A 11 LEU A 12 0 SHEET 2 AC2 6 THR A 115 VAL A 119 1 O THR A 118 N LEU A 12 SHEET 3 AC2 6 ALA A 91 ARG A 99 -1 N ALA A 91 O VAL A 117 SHEET 4 AC2 6 TRP A 34 GLN A 39 -1 N THR A 35 O ALA A 96 SHEET 5 AC2 6 GLU A 46 ILE A 51 -1 O ILE A 51 N TRP A 34 SHEET 6 AC2 6 THR A 57 TYR A 59 -1 O ASN A 58 N GLU A 50 SHEET 1 AC3 4 LEU A 11 LEU A 12 0 SHEET 2 AC3 4 THR A 115 VAL A 119 1 O THR A 118 N LEU A 12 SHEET 3 AC3 4 ALA A 91 ARG A 99 -1 N ALA A 91 O VAL A 117 SHEET 4 AC3 4 TYR A 107 TRP A 111 -1 O PHE A 108 N LEU A 98 SHEET 1 AC4 4 SER A 128 LEU A 132 0 SHEET 2 AC4 4 THR A 143 TYR A 153 -1 O LEU A 149 N PHE A 130 SHEET 3 AC4 4 TYR A 184 PRO A 193 -1 O TYR A 184 N TYR A 153 SHEET 4 AC4 4 VAL A 171 THR A 173 -1 N HIS A 172 O VAL A 189 SHEET 1 AC5 4 SER A 128 LEU A 132 0 SHEET 2 AC5 4 THR A 143 TYR A 153 -1 O LEU A 149 N PHE A 130 SHEET 3 AC5 4 TYR A 184 PRO A 193 -1 O TYR A 184 N TYR A 153 SHEET 4 AC5 4 VAL A 177 LEU A 178 -1 N VAL A 177 O SER A 185 SHEET 1 AC6 3 THR A 159 TRP A 162 0 SHEET 2 AC6 3 ILE A 203 HIS A 208 -1 O ASN A 205 N SER A 161 SHEET 3 AC6 3 THR A 213 LYS A 218 -1 O THR A 213 N HIS A 208 SHEET 1 AC7 4 LEU B 4 SER B 7 0 SHEET 2 AC7 4 ALA B 19 ALA B 25 -1 O ARG B 24 N THR B 5 SHEET 3 AC7 4 ASP B 71 ILE B 76 -1 O LEU B 74 N LEU B 21 SHEET 4 AC7 4 PHE B 63 SER B 68 -1 N SER B 64 O THR B 75 SHEET 1 AC8 6 THR B 10 LEU B 13 0 SHEET 2 AC8 6 THR B 103 ILE B 107 1 O ASP B 106 N LEU B 11 SHEET 3 AC8 6 VAL B 86 GLN B 91 -1 N TYR B 87 O THR B 103 SHEET 4 AC8 6 LEU B 34 GLN B 39 -1 N TYR B 37 O PHE B 88 SHEET 5 AC8 6 ARG B 46 TYR B 50 -1 O ARG B 46 N GLN B 38 SHEET 6 AC8 6 SER B 54 ARG B 55 -1 O SER B 54 N TYR B 50 SHEET 1 AC9 4 THR B 10 LEU B 13 0 SHEET 2 AC9 4 THR B 103 ILE B 107 1 O ASP B 106 N LEU B 11 SHEET 3 AC9 4 VAL B 86 GLN B 91 -1 N TYR B 87 O THR B 103 SHEET 4 AC9 4 THR B 98 PHE B 99 -1 O THR B 98 N GLN B 91 SHEET 1 AD1 4 SER B 115 PHE B 119 0 SHEET 2 AD1 4 THR B 130 PHE B 140 -1 O LEU B 136 N PHE B 117 SHEET 3 AD1 4 TYR B 174 SER B 183 -1 O LEU B 182 N ALA B 131 SHEET 4 AD1 4 SER B 160 VAL B 164 -1 N SER B 163 O SER B 177 SHEET 1 AD2 4 ALA B 154 LEU B 155 0 SHEET 2 AD2 4 LYS B 146 VAL B 151 -1 N VAL B 151 O ALA B 154 SHEET 3 AD2 4 VAL B 192 THR B 198 -1 O GLU B 196 N GLN B 148 SHEET 4 AD2 4 VAL B 206 ASN B 211 -1 O VAL B 206 N VAL B 197 SHEET 1 AD3 4 LEU C 3 ILE C 4 0 SHEET 2 AD3 4 GLU C 9 VAL C 13 -1 O VAL C 10 N LEU C 3 SHEET 3 AD3 4 ALA C 259 LYS C 272 -1 O LYS C 272 N GLU C 9 SHEET 4 AD3 4 ILE C 20 LEU C 27 -1 N LEU C 27 O ARG C 260 SHEET 1 AD4 5 LEU C 3 ILE C 4 0 SHEET 2 AD4 5 GLU C 9 VAL C 13 -1 O VAL C 10 N LEU C 3 SHEET 3 AD4 5 ALA C 259 LYS C 272 -1 O LYS C 272 N GLU C 9 SHEET 4 AD4 5 LEU C 83 ILE C 96 -1 N GLU C 87 O ARG C 267 SHEET 5 AD4 5 THR C 218 VAL C 219 -1 O THR C 218 N VAL C 91 SHEET 1 AD5 3 LYS C 170 TYR C 172 0 SHEET 2 AD5 3 GLU C 136 GLY C 139 -1 N MET C 137 O ALA C 171 SHEET 3 AD5 3 TRP C 184 PRO C 186 -1 O VAL C 185 N GLN C 138 SHEET 1 AD6 5 VAL C 209 THR C 213 0 SHEET 2 AD6 5 THR F 194 THR F 201 -1 O PHE F 200 N LEU C 210 SHEET 3 AD6 5 ASN F 124 GLY F 131 -1 N VAL F 130 O ARG F 195 SHEET 4 AD6 5 SER F 234 THR F 247 -1 O TYR F 236 N GLY F 131 SHEET 5 AD6 5 SER F 65 PRO F 70 -1 N ILE F 69 O LEU F 235 SHEET 1 AD7 5 VAL C 209 THR C 213 0 SHEET 2 AD7 5 THR F 194 THR F 201 -1 O PHE F 200 N LEU C 210 SHEET 3 AD7 5 ASN F 124 GLY F 131 -1 N VAL F 130 O ARG F 195 SHEET 4 AD7 5 SER F 234 THR F 247 -1 O TYR F 236 N GLY F 131 SHEET 5 AD7 5 GLN F 253 GLY F 257 -1 O GLN F 254 N PHE F 246 SHEET 1 AD8 4 GLN D 3 TRP D 7 0 SHEET 2 AD8 4 LEU D 18 ARG D 26 -1 O ALA D 23 N GLN D 5 SHEET 3 AD8 4 GLN D 77 LEU D 82 -1 O PHE D 78 N CYS D 22 SHEET 4 AD8 4 VAL D 67 ASP D 72 -1 N ASP D 72 O GLN D 77 SHEET 1 AD9 6 LEU D 11 LEU D 12 0 SHEET 2 AD9 6 THR D 115 VAL D 119 1 O THR D 118 N LEU D 12 SHEET 3 AD9 6 ALA D 91 ARG D 99 -1 N ALA D 91 O VAL D 117 SHEET 4 AD9 6 TRP D 34 GLN D 39 -1 N THR D 35 O ALA D 96 SHEET 5 AD9 6 GLU D 46 ILE D 51 -1 O ILE D 51 N TRP D 34 SHEET 6 AD9 6 THR D 57 TYR D 59 -1 O ASN D 58 N GLU D 50 SHEET 1 AE1 4 LEU D 11 LEU D 12 0 SHEET 2 AE1 4 THR D 115 VAL D 119 1 O THR D 118 N LEU D 12 SHEET 3 AE1 4 ALA D 91 ARG D 99 -1 N ALA D 91 O VAL D 117 SHEET 4 AE1 4 TYR D 107 TRP D 111 -1 O PHE D 108 N LEU D 98 SHEET 1 AE2 4 SER D 128 LEU D 132 0 SHEET 2 AE2 4 THR D 143 TYR D 153 -1 O LEU D 149 N PHE D 130 SHEET 3 AE2 4 TYR D 184 PRO D 193 -1 O TYR D 184 N TYR D 153 SHEET 4 AE2 4 VAL D 171 THR D 173 -1 N HIS D 172 O VAL D 189 SHEET 1 AE3 4 THR D 139 SER D 140 0 SHEET 2 AE3 4 THR D 143 TYR D 153 -1 O THR D 143 N SER D 140 SHEET 3 AE3 4 TYR D 184 PRO D 193 -1 O TYR D 184 N TYR D 153 SHEET 4 AE3 4 VAL D 177 LEU D 178 -1 N VAL D 177 O SER D 185 SHEET 1 AE4 3 THR D 159 TRP D 162 0 SHEET 2 AE4 3 TYR D 202 HIS D 208 -1 O ASN D 205 N SER D 161 SHEET 3 AE4 3 THR D 213 VAL D 219 -1 O VAL D 215 N VAL D 206 SHEET 1 AE5 4 LEU E 4 SER E 7 0 SHEET 2 AE5 4 ALA E 19 ALA E 25 -1 O ARG E 24 N THR E 5 SHEET 3 AE5 4 ASP E 71 ILE E 76 -1 O LEU E 74 N LEU E 21 SHEET 4 AE5 4 PHE E 63 SER E 68 -1 N SER E 64 O THR E 75 SHEET 1 AE6 6 THR E 10 LEU E 13 0 SHEET 2 AE6 6 THR E 103 ILE E 107 1 O ASP E 106 N LEU E 11 SHEET 3 AE6 6 VAL E 86 GLN E 91 -1 N TYR E 87 O THR E 103 SHEET 4 AE6 6 LEU E 34 GLN E 39 -1 N TYR E 37 O PHE E 88 SHEET 5 AE6 6 ARG E 46 TYR E 50 -1 O ARG E 46 N GLN E 38 SHEET 6 AE6 6 SER E 54 ARG E 55 -1 O SER E 54 N TYR E 50 SHEET 1 AE7 4 THR E 10 LEU E 13 0 SHEET 2 AE7 4 THR E 103 ILE E 107 1 O ASP E 106 N LEU E 11 SHEET 3 AE7 4 VAL E 86 GLN E 91 -1 N TYR E 87 O THR E 103 SHEET 4 AE7 4 THR E 98 PHE E 99 -1 O THR E 98 N GLN E 91 SHEET 1 AE8 4 SER E 115 PHE E 119 0 SHEET 2 AE8 4 THR E 130 PHE E 140 -1 O LEU E 136 N PHE E 117 SHEET 3 AE8 4 TYR E 174 SER E 183 -1 O LEU E 182 N ALA E 131 SHEET 4 AE8 4 SER E 160 VAL E 164 -1 N SER E 163 O SER E 177 SHEET 1 AE9 4 ALA E 154 LEU E 155 0 SHEET 2 AE9 4 LYS E 146 VAL E 151 -1 N VAL E 151 O ALA E 154 SHEET 3 AE9 4 VAL E 192 THR E 198 -1 O GLU E 196 N GLN E 148 SHEET 4 AE9 4 VAL E 206 ASN E 211 -1 O VAL E 206 N VAL E 197 SHEET 1 AF1 3 GLU F 9 VAL F 13 0 SHEET 2 AF1 3 ALA F 259 LYS F 272 -1 O SER F 270 N LEU F 11 SHEET 3 AF1 3 ILE F 20 LEU F 27 -1 N LEU F 27 O ARG F 260 SHEET 1 AF2 4 GLU F 9 VAL F 13 0 SHEET 2 AF2 4 ALA F 259 LYS F 272 -1 O SER F 270 N LEU F 11 SHEET 3 AF2 4 LEU F 83 ILE F 96 -1 N VAL F 89 O ARG F 265 SHEET 4 AF2 4 THR F 218 VAL F 219 -1 O THR F 218 N VAL F 91 SHEET 1 AF3 3 LYS F 170 TYR F 172 0 SHEET 2 AF3 3 GLU F 136 GLY F 139 -1 N MET F 137 O ALA F 171 SHEET 3 AF3 3 TRP F 184 PRO F 186 -1 O VAL F 185 N GLN F 138 SHEET 1 AF4 5 VAL F 209 THR F 213 0 SHEET 2 AF4 5 THR K 194 THR K 201 -1 O GLY K 198 N VAL F 212 SHEET 3 AF4 5 ASN K 124 GLY K 131 -1 N VAL K 130 O ARG K 195 SHEET 4 AF4 5 SER K 234 THR K 247 -1 O TYR K 236 N GLY K 131 SHEET 5 AF4 5 SER K 65 PRO K 70 -1 N ILE K 69 O LEU K 235 SHEET 1 AF5 5 VAL F 209 THR F 213 0 SHEET 2 AF5 5 THR K 194 THR K 201 -1 O GLY K 198 N VAL F 212 SHEET 3 AF5 5 ASN K 124 GLY K 131 -1 N VAL K 130 O ARG K 195 SHEET 4 AF5 5 SER K 234 THR K 247 -1 O TYR K 236 N GLY K 131 SHEET 5 AF5 5 GLN K 253 GLY K 257 -1 O GLN K 254 N PHE K 246 SHEET 1 AF6 4 GLN G 3 GLY G 8 0 SHEET 2 AF6 4 LEU G 18 TYR G 25 -1 O ALA G 23 N GLN G 5 SHEET 3 AF6 4 GLN G 77 LEU G 82 -1 O PHE G 78 N CYS G 22 SHEET 4 AF6 4 VAL G 67 ASP G 72 -1 N ASP G 72 O GLN G 77 SHEET 1 AF7 6 LEU G 11 LEU G 12 0 SHEET 2 AF7 6 THR G 115 VAL G 119 1 O THR G 118 N LEU G 12 SHEET 3 AF7 6 ALA G 91 ARG G 99 -1 N ALA G 91 O VAL G 117 SHEET 4 AF7 6 TRP G 34 GLN G 39 -1 N THR G 35 O ALA G 96 SHEET 5 AF7 6 GLU G 46 ILE G 51 -1 O ILE G 51 N TRP G 34 SHEET 6 AF7 6 THR G 57 TYR G 59 -1 O ASN G 58 N GLU G 50 SHEET 1 AF8 4 LEU G 11 LEU G 12 0 SHEET 2 AF8 4 THR G 115 VAL G 119 1 O THR G 118 N LEU G 12 SHEET 3 AF8 4 ALA G 91 ARG G 99 -1 N ALA G 91 O VAL G 117 SHEET 4 AF8 4 TYR G 107 TRP G 111 -1 O PHE G 108 N LEU G 98 SHEET 1 AF9 4 SER G 128 LEU G 132 0 SHEET 2 AF9 4 THR G 143 TYR G 153 -1 O LEU G 149 N PHE G 130 SHEET 3 AF9 4 TYR G 184 PRO G 193 -1 O TYR G 184 N TYR G 153 SHEET 4 AF9 4 VAL G 171 THR G 173 -1 N HIS G 172 O VAL G 189 SHEET 1 AG1 4 THR G 139 SER G 140 0 SHEET 2 AG1 4 THR G 143 TYR G 153 -1 O THR G 143 N SER G 140 SHEET 3 AG1 4 TYR G 184 PRO G 193 -1 O TYR G 184 N TYR G 153 SHEET 4 AG1 4 VAL G 177 LEU G 178 -1 N VAL G 177 O SER G 185 SHEET 1 AG2 3 THR G 159 TRP G 162 0 SHEET 2 AG2 3 ILE G 203 HIS G 208 -1 O ASN G 205 N SER G 161 SHEET 3 AG2 3 THR G 213 LYS G 218 -1 O THR G 213 N HIS G 208 SHEET 1 AG3 4 LEU J 4 SER J 7 0 SHEET 2 AG3 4 ALA J 19 ALA J 25 -1 O ARG J 24 N THR J 5 SHEET 3 AG3 4 ASP J 71 ILE J 76 -1 O LEU J 74 N LEU J 21 SHEET 4 AG3 4 PHE J 63 SER J 68 -1 N SER J 64 O THR J 75 SHEET 1 AG4 6 THR J 10 LEU J 13 0 SHEET 2 AG4 6 THR J 103 ILE J 107 1 O LYS J 104 N LEU J 11 SHEET 3 AG4 6 VAL J 86 GLN J 91 -1 N TYR J 87 O THR J 103 SHEET 4 AG4 6 LEU J 34 GLN J 39 -1 N TYR J 37 O PHE J 88 SHEET 5 AG4 6 ARG J 46 TYR J 50 -1 O ARG J 46 N GLN J 38 SHEET 6 AG4 6 SER J 54 ARG J 55 -1 O SER J 54 N TYR J 50 SHEET 1 AG5 4 THR J 10 LEU J 13 0 SHEET 2 AG5 4 THR J 103 ILE J 107 1 O LYS J 104 N LEU J 11 SHEET 3 AG5 4 VAL J 86 GLN J 91 -1 N TYR J 87 O THR J 103 SHEET 4 AG5 4 THR J 98 PHE J 99 -1 O THR J 98 N GLN J 91 SHEET 1 AG6 4 SER J 115 PHE J 119 0 SHEET 2 AG6 4 THR J 130 PHE J 140 -1 O LEU J 136 N PHE J 117 SHEET 3 AG6 4 TYR J 174 SER J 183 -1 O LEU J 182 N ALA J 131 SHEET 4 AG6 4 SER J 160 VAL J 164 -1 N SER J 163 O SER J 177 SHEET 1 AG7 4 ALA J 154 LEU J 155 0 SHEET 2 AG7 4 LYS J 146 VAL J 151 -1 N VAL J 151 O ALA J 154 SHEET 3 AG7 4 VAL J 192 THR J 198 -1 O GLU J 196 N GLN J 148 SHEET 4 AG7 4 VAL J 206 ASN J 211 -1 O VAL J 206 N VAL J 197 SHEET 1 AG8 3 VAL K 10 VAL K 13 0 SHEET 2 AG8 3 ALA K 259 LYS K 272 -1 O SER K 270 N LEU K 11 SHEET 3 AG8 3 ILE K 20 LEU K 27 -1 N LEU K 27 O ARG K 260 SHEET 1 AG9 4 VAL K 10 VAL K 13 0 SHEET 2 AG9 4 ALA K 259 LYS K 272 -1 O SER K 270 N LEU K 11 SHEET 3 AG9 4 ASN K 82 ILE K 96 -1 N VAL K 89 O ARG K 265 SHEET 4 AG9 4 THR K 218 VAL K 219 -1 O THR K 218 N VAL K 91 SHEET 1 AH1 3 LYS K 170 TYR K 172 0 SHEET 2 AH1 3 GLU K 136 GLY K 139 -1 N MET K 137 O ALA K 171 SHEET 3 AH1 3 TRP K 184 PRO K 186 -1 O VAL K 185 N GLN K 138 SHEET 1 AH2 5 VAL K 209 THR K 213 0 SHEET 2 AH2 5 THR O 194 THR O 201 -1 O GLY O 198 N VAL K 212 SHEET 3 AH2 5 ASN O 124 GLY O 131 -1 N VAL O 130 O ARG O 195 SHEET 4 AH2 5 SER O 234 THR O 247 -1 O TYR O 236 N GLY O 131 SHEET 5 AH2 5 SER O 65 PRO O 70 -1 N ILE O 69 O LEU O 235 SHEET 1 AH3 5 VAL K 209 THR K 213 0 SHEET 2 AH3 5 THR O 194 THR O 201 -1 O GLY O 198 N VAL K 212 SHEET 3 AH3 5 ASN O 124 GLY O 131 -1 N VAL O 130 O ARG O 195 SHEET 4 AH3 5 SER O 234 THR O 247 -1 O TYR O 236 N GLY O 131 SHEET 5 AH3 5 GLN O 253 GLY O 257 -1 O GLN O 254 N PHE O 246 SHEET 1 AH4 4 GLN M 3 TRP M 7 0 SHEET 2 AH4 4 LEU M 18 ARG M 26 -1 O ALA M 23 N GLN M 5 SHEET 3 AH4 4 GLN M 77 LEU M 82 -1 O PHE M 78 N CYS M 22 SHEET 4 AH4 4 VAL M 67 ASP M 72 -1 N ASP M 72 O GLN M 77 SHEET 1 AH5 6 LEU M 11 LEU M 12 0 SHEET 2 AH5 6 THR M 115 VAL M 119 1 O THR M 118 N LEU M 12 SHEET 3 AH5 6 ALA M 91 ARG M 99 -1 N ALA M 91 O VAL M 117 SHEET 4 AH5 6 TRP M 34 GLN M 39 -1 N THR M 35 O ALA M 96 SHEET 5 AH5 6 GLU M 46 ILE M 51 -1 O ILE M 51 N TRP M 34 SHEET 6 AH5 6 THR M 57 TYR M 59 -1 O ASN M 58 N GLU M 50 SHEET 1 AH6 4 LEU M 11 LEU M 12 0 SHEET 2 AH6 4 THR M 115 VAL M 119 1 O THR M 118 N LEU M 12 SHEET 3 AH6 4 ALA M 91 ARG M 99 -1 N ALA M 91 O VAL M 117 SHEET 4 AH6 4 TYR M 107 TRP M 111 -1 O PHE M 108 N LEU M 98 SHEET 1 AH7 4 SER M 128 LEU M 132 0 SHEET 2 AH7 4 THR M 143 TYR M 153 -1 O LEU M 149 N PHE M 130 SHEET 3 AH7 4 TYR M 184 PRO M 193 -1 O TYR M 184 N TYR M 153 SHEET 4 AH7 4 VAL M 171 THR M 173 -1 N HIS M 172 O VAL M 189 SHEET 1 AH8 4 THR M 139 SER M 140 0 SHEET 2 AH8 4 THR M 143 TYR M 153 -1 O THR M 143 N SER M 140 SHEET 3 AH8 4 TYR M 184 PRO M 193 -1 O TYR M 184 N TYR M 153 SHEET 4 AH8 4 VAL M 177 LEU M 178 -1 N VAL M 177 O SER M 185 SHEET 1 AH9 3 THR M 159 TRP M 162 0 SHEET 2 AH9 3 ILE M 203 HIS M 208 -1 O ASN M 205 N SER M 161 SHEET 3 AH9 3 THR M 213 LYS M 218 -1 O THR M 213 N HIS M 208 SHEET 1 AI1 4 LEU N 4 SER N 7 0 SHEET 2 AI1 4 ALA N 19 ALA N 25 -1 O ARG N 24 N THR N 5 SHEET 3 AI1 4 ASP N 71 ILE N 76 -1 O LEU N 74 N LEU N 21 SHEET 4 AI1 4 PHE N 63 SER N 68 -1 N SER N 64 O THR N 75 SHEET 1 AI2 6 THR N 10 LEU N 13 0 SHEET 2 AI2 6 THR N 103 ILE N 107 1 O ASP N 106 N LEU N 11 SHEET 3 AI2 6 VAL N 86 GLN N 91 -1 N TYR N 87 O THR N 103 SHEET 4 AI2 6 LEU N 34 GLN N 39 -1 N TYR N 37 O PHE N 88 SHEET 5 AI2 6 ARG N 46 TYR N 50 -1 O ARG N 46 N GLN N 38 SHEET 6 AI2 6 SER N 54 ARG N 55 -1 O SER N 54 N TYR N 50 SHEET 1 AI3 4 THR N 10 LEU N 13 0 SHEET 2 AI3 4 THR N 103 ILE N 107 1 O ASP N 106 N LEU N 11 SHEET 3 AI3 4 VAL N 86 GLN N 91 -1 N TYR N 87 O THR N 103 SHEET 4 AI3 4 THR N 98 PHE N 99 -1 O THR N 98 N GLN N 91 SHEET 1 AI4 4 SER N 115 PHE N 119 0 SHEET 2 AI4 4 THR N 130 PHE N 140 -1 O LEU N 136 N PHE N 117 SHEET 3 AI4 4 TYR N 174 SER N 183 -1 O LEU N 176 N LEU N 137 SHEET 4 AI4 4 SER N 160 VAL N 164 -1 N SER N 163 O SER N 177 SHEET 1 AI5 4 ALA N 154 LEU N 155 0 SHEET 2 AI5 4 ALA N 145 VAL N 151 -1 N VAL N 151 O ALA N 154 SHEET 3 AI5 4 VAL N 192 HIS N 199 -1 O GLU N 196 N GLN N 148 SHEET 4 AI5 4 VAL N 206 ASN N 211 -1 O VAL N 206 N VAL N 197 SHEET 1 AI6 3 VAL O 10 VAL O 13 0 SHEET 2 AI6 3 ALA O 259 LYS O 272 -1 O SER O 270 N LEU O 11 SHEET 3 AI6 3 ILE O 20 LEU O 27 -1 N LEU O 27 O ARG O 260 SHEET 1 AI7 4 VAL O 10 VAL O 13 0 SHEET 2 AI7 4 ALA O 259 LYS O 272 -1 O SER O 270 N LEU O 11 SHEET 3 AI7 4 ASN O 82 ILE O 96 -1 N VAL O 89 O ARG O 265 SHEET 4 AI7 4 THR O 218 VAL O 219 -1 O THR O 218 N VAL O 91 SHEET 1 AI8 3 LYS O 170 TYR O 172 0 SHEET 2 AI8 3 GLU O 136 GLY O 139 -1 N MET O 137 O ALA O 171 SHEET 3 AI8 3 TRP O 184 PRO O 186 -1 O VAL O 185 N GLN O 138 SSBOND 1 CYS H 22 CYS H 95 1555 1555 2.08 SSBOND 2 CYS H 148 CYS H 204 1555 1555 2.04 SSBOND 3 CYS L 23 CYS L 89 1555 1555 2.09 SSBOND 4 CYS L 135 CYS L 195 1555 1555 2.05 SSBOND 5 CYS A 22 CYS A 95 1555 1555 2.10 SSBOND 6 CYS A 148 CYS A 204 1555 1555 2.03 SSBOND 7 CYS B 23 CYS B 89 1555 1555 2.07 SSBOND 8 CYS B 135 CYS B 195 1555 1555 2.05 SSBOND 9 CYS D 22 CYS D 95 1555 1555 2.09 SSBOND 10 CYS D 148 CYS D 204 1555 1555 2.04 SSBOND 11 CYS E 23 CYS E 89 1555 1555 2.07 SSBOND 12 CYS E 135 CYS E 195 1555 1555 2.05 SSBOND 13 CYS G 22 CYS G 95 1555 1555 2.09 SSBOND 14 CYS G 148 CYS G 204 1555 1555 2.03 SSBOND 15 CYS J 23 CYS J 89 1555 1555 2.08 SSBOND 16 CYS J 135 CYS J 195 1555 1555 2.04 SSBOND 17 CYS M 22 CYS M 95 1555 1555 2.10 SSBOND 18 CYS M 148 CYS M 204 1555 1555 2.03 SSBOND 19 CYS N 23 CYS N 89 1555 1555 2.08 SSBOND 20 CYS N 135 CYS N 195 1555 1555 2.05 CISPEP 1 PHE H 154 PRO H 155 0 -8.48 CISPEP 2 GLU H 156 PRO H 157 0 -2.51 CISPEP 3 SER L 7 PRO L 8 0 -11.66 CISPEP 4 SER L 95 PRO L 96 0 -0.32 CISPEP 5 TYR L 141 PRO L 142 0 3.99 CISPEP 6 PHE A 154 PRO A 155 0 -8.95 CISPEP 7 GLU A 156 PRO A 157 0 -1.57 CISPEP 8 SER B 7 PRO B 8 0 -8.00 CISPEP 9 SER B 95 PRO B 96 0 0.52 CISPEP 10 TYR B 141 PRO B 142 0 1.99 CISPEP 11 PHE D 154 PRO D 155 0 -8.09 CISPEP 12 GLU D 156 PRO D 157 0 -4.15 CISPEP 13 SER E 7 PRO E 8 0 -14.93 CISPEP 14 SER E 95 PRO E 96 0 -1.89 CISPEP 15 TYR E 141 PRO E 142 0 1.35 CISPEP 16 PHE G 154 PRO G 155 0 -8.57 CISPEP 17 GLU G 156 PRO G 157 0 -0.36 CISPEP 18 SER J 7 PRO J 8 0 -11.62 CISPEP 19 SER J 95 PRO J 96 0 1.94 CISPEP 20 TYR J 141 PRO J 142 0 1.27 CISPEP 21 PHE M 154 PRO M 155 0 -9.34 CISPEP 22 GLU M 156 PRO M 157 0 -1.48 CISPEP 23 SER N 7 PRO N 8 0 -10.24 CISPEP 24 SER N 95 PRO N 96 0 -0.65 CISPEP 25 TYR N 141 PRO N 142 0 0.46 CRYST1 109.349 172.078 113.144 90.00 97.64 90.00 P 1 21 1 10 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 0.009145 0.000000 0.001226 0.00000 SCALE2 0.000000 0.005811 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008917 0.00000