HEADER IMMUNE SYSTEM 20-AUG-19 6KR0 TITLE CRYSTAL STRUCTURE OF HL HOMO-DIABODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: HL DIABODY; COMPND 3 CHAIN: A, B, C, D; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS DIABODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR Y.TANAKA REVDAT 1 26-AUG-20 6KR0 0 JRNL AUTH Y.TANAKA JRNL TITL CRYSTAL STRUCTURE OF HL DIABODY JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.14_3260 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.75 REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 47151 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.203 REMARK 3 R VALUE (WORKING SET) : 0.202 REMARK 3 FREE R VALUE : 0.226 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : NULL REMARK 3 SHRINKAGE RADIUS : NULL REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : NULL NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 6KR0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-AUG-19. REMARK 100 THE DEPOSITION ID IS D_1300013489. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 09-APR-15 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 : SPRING-8 REMARK 200 BEAMLINE : BL26B1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47159 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300 REMARK 200 RESOLUTION RANGE LOW (A) : 45.750 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 7.430 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.05800 REMARK 200 FOR THE DATA SET : 27.8500 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.88700 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 41.29 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TIRS-HCL PH 9.0, 0.2 M CALCIUM REMARK 280 CHLORIDE, 3.25 M SODIUM FORMATE, VAPOR DIFFUSION, TEMPERATURE REMARK 280 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-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 43.54000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 67.72000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.24000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 67.72000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.54000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.24000 REMARK 290 SMTRY3 4 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3540 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20330 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3300 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20710 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D 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 MET A 1 REMARK 465 LYS A 2 REMARK 465 TYR A 3 REMARK 465 LEU A 4 REMARK 465 LEU A 5 REMARK 465 PRO A 6 REMARK 465 THR A 7 REMARK 465 ALA A 8 REMARK 465 ALA A 9 REMARK 465 ALA A 10 REMARK 465 GLY A 11 REMARK 465 LEU A 12 REMARK 465 LEU A 13 REMARK 465 LEU A 14 REMARK 465 LEU A 15 REMARK 465 ALA A 16 REMARK 465 ALA A 17 REMARK 465 GLN A 18 REMARK 465 PRO A 19 REMARK 465 ALA A 20 REMARK 465 MET A 21 REMARK 465 ALA A 22 REMARK 465 GLY A 23 REMARK 465 SER A 24 REMARK 465 ALA A 148 REMARK 465 SER A 149 REMARK 465 GLY A 150 REMARK 465 GLY A 151 REMARK 465 GLY A 152 REMARK 465 GLY A 153 REMARK 465 SER A 154 REMARK 465 ASP A 155 REMARK 465 LYS A 261 REMARK 465 ALA A 262 REMARK 465 ALA A 263 REMARK 465 ALA A 264 REMARK 465 ALA A 265 REMARK 465 GLU A 266 REMARK 465 GLN A 267 REMARK 465 LYS A 268 REMARK 465 LEU A 269 REMARK 465 ILE A 270 REMARK 465 SER A 271 REMARK 465 GLU A 272 REMARK 465 GLU A 273 REMARK 465 ASP A 274 REMARK 465 LEU A 275 REMARK 465 ASN A 276 REMARK 465 LEU A 277 REMARK 465 GLY A 278 REMARK 465 GLY A 279 REMARK 465 GLY A 280 REMARK 465 MET A 281 REMARK 465 ARG A 282 REMARK 465 GLY A 283 REMARK 465 SER A 284 REMARK 465 HIS A 285 REMARK 465 HIS A 286 REMARK 465 HIS A 287 REMARK 465 HIS A 288 REMARK 465 HIS A 289 REMARK 465 HIS A 290 REMARK 465 MET B 1 REMARK 465 LYS B 2 REMARK 465 TYR B 3 REMARK 465 LEU B 4 REMARK 465 LEU B 5 REMARK 465 PRO B 6 REMARK 465 THR B 7 REMARK 465 ALA B 8 REMARK 465 ALA B 9 REMARK 465 ALA B 10 REMARK 465 GLY B 11 REMARK 465 LEU B 12 REMARK 465 LEU B 13 REMARK 465 LEU B 14 REMARK 465 LEU B 15 REMARK 465 ALA B 16 REMARK 465 ALA B 17 REMARK 465 GLN B 18 REMARK 465 PRO B 19 REMARK 465 ALA B 20 REMARK 465 MET B 21 REMARK 465 ALA B 22 REMARK 465 GLY B 23 REMARK 465 SER B 24 REMARK 465 ALA B 148 REMARK 465 SER B 149 REMARK 465 GLY B 150 REMARK 465 GLY B 151 REMARK 465 GLY B 152 REMARK 465 GLY B 153 REMARK 465 SER B 154 REMARK 465 ASP B 155 REMARK 465 ILE B 156 REMARK 465 ALA B 262 REMARK 465 ALA B 263 REMARK 465 ALA B 264 REMARK 465 ALA B 265 REMARK 465 GLU B 266 REMARK 465 GLN B 267 REMARK 465 LYS B 268 REMARK 465 LEU B 269 REMARK 465 ILE B 270 REMARK 465 SER B 271 REMARK 465 GLU B 272 REMARK 465 GLU B 273 REMARK 465 ASP B 274 REMARK 465 LEU B 275 REMARK 465 ASN B 276 REMARK 465 LEU B 277 REMARK 465 GLY B 278 REMARK 465 GLY B 279 REMARK 465 GLY B 280 REMARK 465 MET B 281 REMARK 465 ARG B 282 REMARK 465 GLY B 283 REMARK 465 SER B 284 REMARK 465 HIS B 285 REMARK 465 HIS B 286 REMARK 465 HIS B 287 REMARK 465 HIS B 288 REMARK 465 HIS B 289 REMARK 465 HIS B 290 REMARK 465 MET C 1 REMARK 465 LYS C 2 REMARK 465 TYR C 3 REMARK 465 LEU C 4 REMARK 465 LEU C 5 REMARK 465 PRO C 6 REMARK 465 THR C 7 REMARK 465 ALA C 8 REMARK 465 ALA C 9 REMARK 465 ALA C 10 REMARK 465 GLY C 11 REMARK 465 LEU C 12 REMARK 465 LEU C 13 REMARK 465 LEU C 14 REMARK 465 LEU C 15 REMARK 465 ALA C 16 REMARK 465 ALA C 17 REMARK 465 GLN C 18 REMARK 465 PRO C 19 REMARK 465 ALA C 20 REMARK 465 MET C 21 REMARK 465 ALA C 22 REMARK 465 GLY C 23 REMARK 465 SER C 24 REMARK 465 ALA C 147 REMARK 465 ALA C 148 REMARK 465 SER C 149 REMARK 465 GLY C 150 REMARK 465 GLY C 151 REMARK 465 GLY C 152 REMARK 465 GLY C 153 REMARK 465 SER C 154 REMARK 465 ASP C 155 REMARK 465 ILE C 156 REMARK 465 ALA C 262 REMARK 465 ALA C 263 REMARK 465 ALA C 264 REMARK 465 ALA C 265 REMARK 465 GLU C 266 REMARK 465 GLN C 267 REMARK 465 LYS C 268 REMARK 465 LEU C 269 REMARK 465 ILE C 270 REMARK 465 SER C 271 REMARK 465 GLU C 272 REMARK 465 GLU C 273 REMARK 465 ASP C 274 REMARK 465 LEU C 275 REMARK 465 ASN C 276 REMARK 465 LEU C 277 REMARK 465 GLY C 278 REMARK 465 GLY C 279 REMARK 465 GLY C 280 REMARK 465 MET C 281 REMARK 465 ARG C 282 REMARK 465 GLY C 283 REMARK 465 SER C 284 REMARK 465 HIS C 285 REMARK 465 HIS C 286 REMARK 465 HIS C 287 REMARK 465 HIS C 288 REMARK 465 HIS C 289 REMARK 465 HIS C 290 REMARK 465 MET D 1 REMARK 465 LYS D 2 REMARK 465 TYR D 3 REMARK 465 LEU D 4 REMARK 465 LEU D 5 REMARK 465 PRO D 6 REMARK 465 THR D 7 REMARK 465 ALA D 8 REMARK 465 ALA D 9 REMARK 465 ALA D 10 REMARK 465 GLY D 11 REMARK 465 LEU D 12 REMARK 465 LEU D 13 REMARK 465 LEU D 14 REMARK 465 LEU D 15 REMARK 465 ALA D 16 REMARK 465 ALA D 17 REMARK 465 GLN D 18 REMARK 465 PRO D 19 REMARK 465 ALA D 20 REMARK 465 MET D 21 REMARK 465 ALA D 22 REMARK 465 GLY D 23 REMARK 465 SER D 24 REMARK 465 SER D 145 REMARK 465 SER D 146 REMARK 465 ALA D 147 REMARK 465 ALA D 148 REMARK 465 SER D 149 REMARK 465 GLY D 150 REMARK 465 GLY D 151 REMARK 465 GLY D 152 REMARK 465 GLY D 153 REMARK 465 SER D 154 REMARK 465 ASP D 155 REMARK 465 ILE D 156 REMARK 465 ILE D 260 REMARK 465 LYS D 261 REMARK 465 ALA D 262 REMARK 465 ALA D 263 REMARK 465 ALA D 264 REMARK 465 ALA D 265 REMARK 465 GLU D 266 REMARK 465 GLN D 267 REMARK 465 LYS D 268 REMARK 465 LEU D 269 REMARK 465 ILE D 270 REMARK 465 SER D 271 REMARK 465 GLU D 272 REMARK 465 GLU D 273 REMARK 465 ASP D 274 REMARK 465 LEU D 275 REMARK 465 ASN D 276 REMARK 465 LEU D 277 REMARK 465 GLY D 278 REMARK 465 GLY D 279 REMARK 465 GLY D 280 REMARK 465 MET D 281 REMARK 465 ARG D 282 REMARK 465 GLY D 283 REMARK 465 SER D 284 REMARK 465 HIS D 285 REMARK 465 HIS D 286 REMARK 465 HIS D 287 REMARK 465 HIS D 288 REMARK 465 HIS D 289 REMARK 465 HIS D 290 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O HOH A 351 O HOH A 352 1.85 REMARK 500 O GLY D 220 O HOH D 301 1.95 REMARK 500 O LYS A 89 O HOH A 301 1.96 REMARK 500 O HOH B 323 O HOH B 332 1.99 REMARK 500 OD1 ASP D 128 O HOH D 302 2.05 REMARK 500 OE1 GLN D 243 O HOH D 303 2.08 REMARK 500 O SER B 221 O HOH B 301 2.12 REMARK 500 O TYR D 125 O HOH D 302 2.12 REMARK 500 O HOH A 329 O HOH A 349 2.13 REMARK 500 OE1 GLU B 70 O HOH B 302 2.15 REMARK 500 O HOH C 353 O HOH C 357 2.17 REMARK 500 O GLY A 195 O HOH A 302 2.18 REMARK 500 O LYS C 79 O HOH C 301 2.19 REMARK 500 NH2 ARG B 91 OD2 ASP B 114 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH A 333 O HOH C 351 4566 2.13 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER A 123 -148.47 -116.50 REMARK 500 ALA A 205 -45.59 72.13 REMARK 500 PRO A 247 -143.46 -88.39 REMARK 500 VAL B 72 -62.84 -104.89 REMARK 500 SER B 123 -147.73 -103.80 REMARK 500 TRP B 131 72.91 -119.15 REMARK 500 ALA B 184 -110.59 52.78 REMARK 500 ALA B 205 -40.57 74.51 REMARK 500 ALA B 238 -172.10 -171.15 REMARK 500 ALA C 184 -114.72 51.29 REMARK 500 ALA C 205 -38.14 71.50 REMARK 500 ALA C 238 -165.98 -175.41 REMARK 500 PRO C 247 -135.30 -102.40 REMARK 500 LYS D 67 -166.44 -102.92 REMARK 500 ALA D 184 -112.93 52.30 REMARK 500 ALA D 205 -41.52 73.44 REMARK 500 ALA D 238 -175.25 -171.61 REMARK 500 GLU D 246 133.84 -170.33 REMARK 500 PRO D 247 -158.28 -92.17 REMARK 500 PRO D 249 31.90 -87.25 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 352 DISTANCE = 6.28 ANGSTROMS DBREF 6KR0 A 1 290 PDB 6KR0 6KR0 1 290 DBREF 6KR0 B 1 290 PDB 6KR0 6KR0 1 290 DBREF 6KR0 C 1 290 PDB 6KR0 6KR0 1 290 DBREF 6KR0 D 1 290 PDB 6KR0 6KR0 1 290 SEQRES 1 A 290 MET LYS TYR LEU LEU PRO THR ALA ALA ALA GLY LEU LEU SEQRES 2 A 290 LEU LEU ALA ALA GLN PRO ALA MET ALA GLY SER GLU VAL SEQRES 3 A 290 GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO GLY SEQRES 4 A 290 GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY TYR SER SEQRES 5 A 290 PHE THR GLY TYR THR MET ASN TRP VAL ARG GLN ALA PRO SEQRES 6 A 290 GLY LYS GLY LEU GLU TRP VAL ALA LEU ILE ASN PRO TYR SEQRES 7 A 290 LYS GLY VAL SER THR TYR ASN GLN LYS PHE LYS ASP ARG SEQRES 8 A 290 PHE THR ILE SER VAL ASP LYS SER LYS ASN THR ALA TYR SEQRES 9 A 290 LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA VAL SEQRES 10 A 290 TYR TYR CYS ALA ARG SER GLY TYR TYR GLY ASP SER ASP SEQRES 11 A 290 TRP TYR PHE ASP VAL TRP GLY GLN GLY THR LEU VAL THR SEQRES 12 A 290 VAL SER SER ALA ALA SER GLY GLY GLY GLY SER ASP ILE SEQRES 13 A 290 GLN MET THR GLN SER PRO SER SER LEU SER ALA SER VAL SEQRES 14 A 290 GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER GLN ASP SEQRES 15 A 290 LEU ALA THR ASP VAL ALA TRP TYR GLN GLN LYS PRO GLY SEQRES 16 A 290 LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER PHE LEU SEQRES 17 A 290 TYR SER GLY VAL PRO SER ARG PHE SER GLY SER GLY SER SEQRES 18 A 290 GLY THR ASP PHE THR LEU THR ILE SER SER LEU GLN PRO SEQRES 19 A 290 GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER GLU PRO SEQRES 20 A 290 GLU PRO TYR THR PHE GLY GLN GLY THR LYS VAL GLU ILE SEQRES 21 A 290 LYS ALA ALA ALA ALA GLU GLN LYS LEU ILE SER GLU GLU SEQRES 22 A 290 ASP LEU ASN LEU GLY GLY GLY MET ARG GLY SER HIS HIS SEQRES 23 A 290 HIS HIS HIS HIS SEQRES 1 B 290 MET LYS TYR LEU LEU PRO THR ALA ALA ALA GLY LEU LEU SEQRES 2 B 290 LEU LEU ALA ALA GLN PRO ALA MET ALA GLY SER GLU VAL SEQRES 3 B 290 GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO GLY SEQRES 4 B 290 GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY TYR SER SEQRES 5 B 290 PHE THR GLY TYR THR MET ASN TRP VAL ARG GLN ALA PRO SEQRES 6 B 290 GLY LYS GLY LEU GLU TRP VAL ALA LEU ILE ASN PRO TYR SEQRES 7 B 290 LYS GLY VAL SER THR TYR ASN GLN LYS PHE LYS ASP ARG SEQRES 8 B 290 PHE THR ILE SER VAL ASP LYS SER LYS ASN THR ALA TYR SEQRES 9 B 290 LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA VAL SEQRES 10 B 290 TYR TYR CYS ALA ARG SER GLY TYR TYR GLY ASP SER ASP SEQRES 11 B 290 TRP TYR PHE ASP VAL TRP GLY GLN GLY THR LEU VAL THR SEQRES 12 B 290 VAL SER SER ALA ALA SER GLY GLY GLY GLY SER ASP ILE SEQRES 13 B 290 GLN MET THR GLN SER PRO SER SER LEU SER ALA SER VAL SEQRES 14 B 290 GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER GLN ASP SEQRES 15 B 290 LEU ALA THR ASP VAL ALA TRP TYR GLN GLN LYS PRO GLY SEQRES 16 B 290 LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER PHE LEU SEQRES 17 B 290 TYR SER GLY VAL PRO SER ARG PHE SER GLY SER GLY SER SEQRES 18 B 290 GLY THR ASP PHE THR LEU THR ILE SER SER LEU GLN PRO SEQRES 19 B 290 GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER GLU PRO SEQRES 20 B 290 GLU PRO TYR THR PHE GLY GLN GLY THR LYS VAL GLU ILE SEQRES 21 B 290 LYS ALA ALA ALA ALA GLU GLN LYS LEU ILE SER GLU GLU SEQRES 22 B 290 ASP LEU ASN LEU GLY GLY GLY MET ARG GLY SER HIS HIS SEQRES 23 B 290 HIS HIS HIS HIS SEQRES 1 C 290 MET LYS TYR LEU LEU PRO THR ALA ALA ALA GLY LEU LEU SEQRES 2 C 290 LEU LEU ALA ALA GLN PRO ALA MET ALA GLY SER GLU VAL SEQRES 3 C 290 GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO GLY SEQRES 4 C 290 GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY TYR SER SEQRES 5 C 290 PHE THR GLY TYR THR MET ASN TRP VAL ARG GLN ALA PRO SEQRES 6 C 290 GLY LYS GLY LEU GLU TRP VAL ALA LEU ILE ASN PRO TYR SEQRES 7 C 290 LYS GLY VAL SER THR TYR ASN GLN LYS PHE LYS ASP ARG SEQRES 8 C 290 PHE THR ILE SER VAL ASP LYS SER LYS ASN THR ALA TYR SEQRES 9 C 290 LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA VAL SEQRES 10 C 290 TYR TYR CYS ALA ARG SER GLY TYR TYR GLY ASP SER ASP SEQRES 11 C 290 TRP TYR PHE ASP VAL TRP GLY GLN GLY THR LEU VAL THR SEQRES 12 C 290 VAL SER SER ALA ALA SER GLY GLY GLY GLY SER ASP ILE SEQRES 13 C 290 GLN MET THR GLN SER PRO SER SER LEU SER ALA SER VAL SEQRES 14 C 290 GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER GLN ASP SEQRES 15 C 290 LEU ALA THR ASP VAL ALA TRP TYR GLN GLN LYS PRO GLY SEQRES 16 C 290 LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER PHE LEU SEQRES 17 C 290 TYR SER GLY VAL PRO SER ARG PHE SER GLY SER GLY SER SEQRES 18 C 290 GLY THR ASP PHE THR LEU THR ILE SER SER LEU GLN PRO SEQRES 19 C 290 GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER GLU PRO SEQRES 20 C 290 GLU PRO TYR THR PHE GLY GLN GLY THR LYS VAL GLU ILE SEQRES 21 C 290 LYS ALA ALA ALA ALA GLU GLN LYS LEU ILE SER GLU GLU SEQRES 22 C 290 ASP LEU ASN LEU GLY GLY GLY MET ARG GLY SER HIS HIS SEQRES 23 C 290 HIS HIS HIS HIS SEQRES 1 D 290 MET LYS TYR LEU LEU PRO THR ALA ALA ALA GLY LEU LEU SEQRES 2 D 290 LEU LEU ALA ALA GLN PRO ALA MET ALA GLY SER GLU VAL SEQRES 3 D 290 GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO GLY SEQRES 4 D 290 GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY TYR SER SEQRES 5 D 290 PHE THR GLY TYR THR MET ASN TRP VAL ARG GLN ALA PRO SEQRES 6 D 290 GLY LYS GLY LEU GLU TRP VAL ALA LEU ILE ASN PRO TYR SEQRES 7 D 290 LYS GLY VAL SER THR TYR ASN GLN LYS PHE LYS ASP ARG SEQRES 8 D 290 PHE THR ILE SER VAL ASP LYS SER LYS ASN THR ALA TYR SEQRES 9 D 290 LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA VAL SEQRES 10 D 290 TYR TYR CYS ALA ARG SER GLY TYR TYR GLY ASP SER ASP SEQRES 11 D 290 TRP TYR PHE ASP VAL TRP GLY GLN GLY THR LEU VAL THR SEQRES 12 D 290 VAL SER SER ALA ALA SER GLY GLY GLY GLY SER ASP ILE SEQRES 13 D 290 GLN MET THR GLN SER PRO SER SER LEU SER ALA SER VAL SEQRES 14 D 290 GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER GLN ASP SEQRES 15 D 290 LEU ALA THR ASP VAL ALA TRP TYR GLN GLN LYS PRO GLY SEQRES 16 D 290 LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER PHE LEU SEQRES 17 D 290 TYR SER GLY VAL PRO SER ARG PHE SER GLY SER GLY SER SEQRES 18 D 290 GLY THR ASP PHE THR LEU THR ILE SER SER LEU GLN PRO SEQRES 19 D 290 GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER GLU PRO SEQRES 20 D 290 GLU PRO TYR THR PHE GLY GLN GLY THR LYS VAL GLU ILE SEQRES 21 D 290 LYS ALA ALA ALA ALA GLU GLN LYS LEU ILE SER GLU GLU SEQRES 22 D 290 ASP LEU ASN LEU GLY GLY GLY MET ARG GLY SER HIS HIS SEQRES 23 D 290 HIS HIS HIS HIS FORMUL 5 HOH *185(H2 O) HELIX 1 AA1 GLN A 86 LYS A 89 5 4 HELIX 2 AA2 LYS A 98 LYS A 100 5 3 HELIX 3 AA3 ARG A 111 THR A 115 5 5 HELIX 4 AA4 GLN A 233 PHE A 237 5 5 HELIX 5 AA5 ARG B 111 THR B 115 5 5 HELIX 6 AA6 GLN B 233 PHE B 237 5 5 HELIX 7 AA7 SER C 52 TYR C 56 5 5 HELIX 8 AA8 GLN C 86 LYS C 89 5 4 HELIX 9 AA9 ARG C 111 THR C 115 5 5 HELIX 10 AB1 GLN C 233 PHE C 237 5 5 HELIX 11 AB2 SER D 52 TYR D 56 5 5 HELIX 12 AB3 LYS D 98 LYS D 100 5 3 HELIX 13 AB4 ARG D 111 THR D 115 5 5 HELIX 14 AB5 GLN D 233 PHE D 237 5 5 SHEET 1 AA1 4 GLN A 27 SER A 31 0 SHEET 2 AA1 4 LEU A 42 SER A 49 -1 O SER A 45 N SER A 31 SHEET 3 AA1 4 THR A 102 MET A 107 -1 O MET A 107 N LEU A 42 SHEET 4 AA1 4 PHE A 92 ASP A 97 -1 N SER A 95 O TYR A 104 SHEET 1 AA2 6 GLY A 34 VAL A 36 0 SHEET 2 AA2 6 THR A 140 VAL A 144 1 O THR A 143 N GLY A 34 SHEET 3 AA2 6 ALA A 116 TYR A 125 -1 N TYR A 118 O THR A 140 SHEET 4 AA2 6 TYR A 56 GLN A 63 -1 N VAL A 61 O TYR A 119 SHEET 5 AA2 6 LEU A 69 ASN A 76 -1 O VAL A 72 N TRP A 60 SHEET 6 AA2 6 VAL A 81 TYR A 84 -1 O VAL A 81 N ASN A 76 SHEET 1 AA3 4 GLY A 34 VAL A 36 0 SHEET 2 AA3 4 THR A 140 VAL A 144 1 O THR A 143 N GLY A 34 SHEET 3 AA3 4 ALA A 116 TYR A 125 -1 N TYR A 118 O THR A 140 SHEET 4 AA3 4 VAL A 135 TRP A 136 -1 O VAL A 135 N ARG A 122 SHEET 1 AA4 4 MET A 158 SER A 161 0 SHEET 2 AA4 4 VAL A 173 ALA A 179 -1 O ARG A 178 N THR A 159 SHEET 3 AA4 4 ASP A 224 ILE A 229 -1 O LEU A 227 N ILE A 175 SHEET 4 AA4 4 PHE A 216 SER A 221 -1 N SER A 217 O THR A 228 SHEET 1 AA5 6 SER A 164 SER A 166 0 SHEET 2 AA5 6 THR A 256 GLU A 259 1 O GLU A 259 N LEU A 165 SHEET 3 AA5 6 THR A 239 GLN A 244 -1 N TYR A 240 O THR A 256 SHEET 4 AA5 6 VAL A 187 GLN A 192 -1 N TYR A 190 O TYR A 241 SHEET 5 AA5 6 LYS A 199 TYR A 203 -1 O LEU A 201 N TRP A 189 SHEET 6 AA5 6 PHE A 207 LEU A 208 -1 O PHE A 207 N TYR A 203 SHEET 1 AA6 4 GLN B 27 SER B 31 0 SHEET 2 AA6 4 LEU B 42 SER B 49 -1 O SER B 49 N GLN B 27 SHEET 3 AA6 4 THR B 102 MET B 107 -1 O MET B 107 N LEU B 42 SHEET 4 AA6 4 PHE B 92 ASP B 97 -1 N THR B 93 O GLN B 106 SHEET 1 AA7 6 LEU B 35 VAL B 36 0 SHEET 2 AA7 6 THR B 140 VAL B 144 1 O THR B 143 N VAL B 36 SHEET 3 AA7 6 ALA B 116 TYR B 125 -1 N TYR B 118 O THR B 140 SHEET 4 AA7 6 TYR B 56 GLN B 63 -1 N VAL B 61 O TYR B 119 SHEET 5 AA7 6 GLU B 70 ASN B 76 -1 O ILE B 75 N MET B 58 SHEET 6 AA7 6 VAL B 81 TYR B 84 -1 O THR B 83 N LEU B 74 SHEET 1 AA8 4 LEU B 35 VAL B 36 0 SHEET 2 AA8 4 THR B 140 VAL B 144 1 O THR B 143 N VAL B 36 SHEET 3 AA8 4 ALA B 116 TYR B 125 -1 N TYR B 118 O THR B 140 SHEET 4 AA8 4 VAL B 135 TRP B 136 -1 O VAL B 135 N ARG B 122 SHEET 1 AA9 4 MET B 158 SER B 161 0 SHEET 2 AA9 4 VAL B 173 ALA B 179 -1 O ARG B 178 N THR B 159 SHEET 3 AA9 4 ASP B 224 ILE B 229 -1 O LEU B 227 N ILE B 175 SHEET 4 AA9 4 PHE B 216 SER B 221 -1 N SER B 217 O THR B 228 SHEET 1 AB1 6 SER B 164 ALA B 167 0 SHEET 2 AB1 6 THR B 256 ILE B 260 1 O GLU B 259 N LEU B 165 SHEET 3 AB1 6 THR B 239 GLN B 244 -1 N TYR B 240 O THR B 256 SHEET 4 AB1 6 VAL B 187 GLN B 192 -1 N TYR B 190 O TYR B 241 SHEET 5 AB1 6 LYS B 199 TYR B 203 -1 O LEU B 201 N TRP B 189 SHEET 6 AB1 6 PHE B 207 LEU B 208 -1 O PHE B 207 N TYR B 203 SHEET 1 AB2 4 GLN C 27 SER C 31 0 SHEET 2 AB2 4 LEU C 42 SER C 49 -1 O SER C 49 N GLN C 27 SHEET 3 AB2 4 THR C 102 MET C 107 -1 O LEU C 105 N LEU C 44 SHEET 4 AB2 4 PHE C 92 ASP C 97 -1 N SER C 95 O TYR C 104 SHEET 1 AB3 6 GLY C 34 VAL C 36 0 SHEET 2 AB3 6 THR C 140 VAL C 144 1 O THR C 143 N GLY C 34 SHEET 3 AB3 6 ALA C 116 TYR C 125 -1 N TYR C 118 O THR C 140 SHEET 4 AB3 6 THR C 57 GLN C 63 -1 N VAL C 61 O TYR C 119 SHEET 5 AB3 6 LEU C 69 ASN C 76 -1 O VAL C 72 N TRP C 60 SHEET 6 AB3 6 VAL C 81 TYR C 84 -1 O VAL C 81 N ASN C 76 SHEET 1 AB4 4 GLY C 34 VAL C 36 0 SHEET 2 AB4 4 THR C 140 VAL C 144 1 O THR C 143 N GLY C 34 SHEET 3 AB4 4 ALA C 116 TYR C 125 -1 N TYR C 118 O THR C 140 SHEET 4 AB4 4 TRP C 131 TRP C 136 -1 O TYR C 132 N GLY C 124 SHEET 1 AB5 4 MET C 158 SER C 161 0 SHEET 2 AB5 4 VAL C 173 ALA C 179 -1 O THR C 176 N SER C 161 SHEET 3 AB5 4 ASP C 224 ILE C 229 -1 O LEU C 227 N ILE C 175 SHEET 4 AB5 4 PHE C 216 SER C 221 -1 N SER C 217 O THR C 228 SHEET 1 AB6 6 SER C 164 ALA C 167 0 SHEET 2 AB6 6 THR C 256 ILE C 260 1 O GLU C 259 N LEU C 165 SHEET 3 AB6 6 ALA C 238 GLN C 244 -1 N ALA C 238 O VAL C 258 SHEET 4 AB6 6 VAL C 187 GLN C 192 -1 N TYR C 190 O TYR C 241 SHEET 5 AB6 6 LYS C 199 TYR C 203 -1 O LYS C 199 N GLN C 191 SHEET 6 AB6 6 PHE C 207 LEU C 208 -1 O PHE C 207 N TYR C 203 SHEET 1 AB7 4 GLN D 27 SER D 31 0 SHEET 2 AB7 4 SER D 41 SER D 49 -1 O SER D 45 N SER D 31 SHEET 3 AB7 4 THR D 102 ASN D 108 -1 O MET D 107 N LEU D 42 SHEET 4 AB7 4 THR D 93 ASP D 97 -1 N THR D 93 O GLN D 106 SHEET 1 AB8 5 VAL D 81 TYR D 84 0 SHEET 2 AB8 5 GLU D 70 ASN D 76 -1 N ASN D 76 O VAL D 81 SHEET 3 AB8 5 THR D 57 GLN D 63 -1 N TRP D 60 O VAL D 72 SHEET 4 AB8 5 ALA D 116 SER D 123 -1 O TYR D 119 N VAL D 61 SHEET 5 AB8 5 VAL D 135 TRP D 136 -1 O VAL D 135 N ARG D 122 SHEET 1 AB9 5 VAL D 81 TYR D 84 0 SHEET 2 AB9 5 GLU D 70 ASN D 76 -1 N ASN D 76 O VAL D 81 SHEET 3 AB9 5 THR D 57 GLN D 63 -1 N TRP D 60 O VAL D 72 SHEET 4 AB9 5 ALA D 116 SER D 123 -1 O TYR D 119 N VAL D 61 SHEET 5 AB9 5 THR D 140 VAL D 142 -1 O THR D 140 N TYR D 118 SHEET 1 AC1 4 MET D 158 SER D 161 0 SHEET 2 AC1 4 VAL D 173 ALA D 179 -1 O ARG D 178 N THR D 159 SHEET 3 AC1 4 ASP D 224 ILE D 229 -1 O LEU D 227 N ILE D 175 SHEET 4 AC1 4 PHE D 216 SER D 221 -1 N SER D 217 O THR D 228 SHEET 1 AC2 6 SER D 164 SER D 166 0 SHEET 2 AC2 6 THR D 256 GLU D 259 1 O GLU D 259 N LEU D 165 SHEET 3 AC2 6 THR D 239 GLN D 244 -1 N TYR D 240 O THR D 256 SHEET 4 AC2 6 VAL D 187 GLN D 192 -1 N TYR D 190 O TYR D 241 SHEET 5 AC2 6 LYS D 199 TYR D 203 -1 O LEU D 201 N TRP D 189 SHEET 6 AC2 6 PHE D 207 LEU D 208 -1 O PHE D 207 N TYR D 203 SSBOND 1 CYS A 46 CYS A 120 1555 1555 2.03 SSBOND 2 CYS A 177 CYS A 242 1555 1555 2.04 SSBOND 3 CYS B 46 CYS B 120 1555 1555 2.03 SSBOND 4 CYS B 177 CYS B 242 1555 1555 2.04 SSBOND 5 CYS C 46 CYS C 120 1555 1555 2.03 SSBOND 6 CYS C 177 CYS C 242 1555 1555 2.04 SSBOND 7 CYS D 46 CYS D 120 1555 1555 2.03 SSBOND 8 CYS D 177 CYS D 242 1555 1555 2.04 CISPEP 1 SER A 161 PRO A 162 0 -3.63 CISPEP 2 GLU A 246 PRO A 247 0 -15.26 CISPEP 3 GLU A 248 PRO A 249 0 5.98 CISPEP 4 SER B 161 PRO B 162 0 -4.11 CISPEP 5 GLU B 248 PRO B 249 0 1.02 CISPEP 6 SER C 161 PRO C 162 0 -4.30 CISPEP 7 GLU C 246 PRO C 247 0 -10.99 CISPEP 8 GLU C 248 PRO C 249 0 0.37 CISPEP 9 SER D 161 PRO D 162 0 -1.09 CISPEP 10 GLU D 246 PRO D 247 0 -2.51 CISPEP 11 GLU D 248 PRO D 249 0 2.59 CRYST1 87.080 88.480 135.440 90.00 90.00 90.00 P 21 21 21 16 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 0.011484 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011302 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007383 0.00000