HEADER SIGNALING PROTEIN 07-MAY-03 1P8T TITLE CRYSTAL STRUCTURE OF NOGO-66 RECEPTOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: RETICULON 4 RECEPTOR; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: NOGO RECEPTOR, NGR, NOGO-66 RECEPTOR SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 CELL_LINE: 293 CELLS KEYWDS NGR, NOGO-66 EXPDTA X-RAY DIFFRACTION AUTHOR W.A.BARTON,B.P.LIU,D.TZVETKOVA,P.D.JEFFREY,A.E.FOURNIER, AUTHOR 2 D.SAH,R.CATE,S.M.STRITTMATTER,D.B.NIKOLOV REVDAT 2 23-DEC-03 1P8T 1 JRNL REVDAT 1 20-MAY-03 1P8T 0 JRNL AUTH W.A.BARTON,B.P.LIU,D.TZVETKOVA,P.D.JEFFREY, JRNL AUTH 2 A.E.FOURNIER,D.SAH,R.CATE,S.M.STRITTMATTER, JRNL AUTH 3 D.B.NIKOLOV JRNL TITL STRUCTURE AND AXON OUTGROWTH INHIBITOR BINDING OF JRNL TITL 2 THE NOGO-66 RECEPTOR AND RELATED PROTEINS JRNL REF EMBO J. V. 22 3291 2003 JRNL REFN ASTM EMJODG UK ISSN 0261-4189 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 3.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 32616 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 SET) : 0.265 REMARK 3 FREE R VALUE : 0.292 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 3133 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2224 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 30 REMARK 3 SOLVENT ATOMS : 0 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 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : NULL REMARK 3 BOND ANGLES (DEGREES) : NULL REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : NULL REMARK 3 KSOL : NULL REMARK 3 BSOL : NULL REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1P8T COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-17) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB019151. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 6.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 8-BM REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.21 REMARK 200 MONOCHROMATOR : SI 111 CHANNEL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34022 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200 REMARK 200 RESOLUTION RANGE LOW (A) : 35.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL 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) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: MAD REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD REMARK 200 SOFTWARE USED: SHARP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NACL, PH 6.5, VAPOR DIFFUSION, REMARK 280 HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,1/3+Z REMARK 290 3555 -X+Y,-X,2/3+Z REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,2/3-Z REMARK 290 6555 -X,-X+Y,1/3-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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.05767 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 80.11533 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 80.11533 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 40.05767 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 APPLY THE FOLLOWING TO CHAINS: A 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 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 REMARK 500 OD1 ASP A 171 CG ARG A 196 1.29 REMARK 500 CB ALA A 75 NE ARG A 78 1.44 REMARK 500 CE1 HIS A 220 OE1 GLU A 244 1.83 REMARK 500 OD1 ASP A 172 CD ARG A 199 1.90 REMARK 500 OE2 GLU A 195 NE2 HIS A 218 1.94 REMARK 500 CG GLU A 195 CD2 HIS A 218 1.95 REMARK 500 CG GLU A 195 NE2 HIS A 218 1.96 REMARK 500 CB SER A 282 NZ LYS A 299 2.04 REMARK 500 OD1 ASP A 171 CD ARG A 196 2.11 REMARK 500 O ARG A 196 CG ARG A 199 2.11 REMARK 500 CD2 LEU A 275 NZ LYS A 299 2.13 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 CB ALA A 310 NH2 ARG A 139 2545 1.79 REMARK 500 O GLN A 276 OE1 GLU A 36 2545 2.04 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 MET A 229 SD MET A 229 CE 0.092 REMARK 500 PHE A 278 N PHE A 278 CA 0.163 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 LYS A 38 CB - CA - C ANGL. DEV. = 11.3 DEGREES REMARK 500 SER A 42 N - CA - C ANGL. DEV. = 11.5 DEGREES REMARK 500 VAL A 72 N - CA - C ANGL. DEV. =-12.3 DEGREES REMARK 500 ASN A 236 N - CA - C ANGL. DEV. = 11.5 DEGREES REMARK 500 PHE A 278 N - CA - C ANGL. DEV. = 17.4 DEGREES REMARK 500 PHE A 278 C - N - CA ANGL. DEV. =-14.6 DEGREES 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 M RES CSSEQI PSI PHI REMARK 500 ALA A 100 -104.98 40.83 DBREF 1P8T A 27 311 UNP Q9BZR6 RTN4R_HUMAN 27 311 SEQRES 1 A 285 CYS PRO GLY ALA CYS VAL CYS TYR ASN GLU PRO LYS VAL SEQRES 2 A 285 THR THR SER CYS PRO GLN GLN GLY LEU GLN ALA VAL PRO SEQRES 3 A 285 VAL GLY ILE PRO ALA ALA SER GLN ARG ILE PHE LEU HIS SEQRES 4 A 285 GLY ASN ARG ILE SER HIS VAL PRO ALA ALA SER PHE ARG SEQRES 5 A 285 ALA CYS ARG ASN LEU THR ILE LEU TRP LEU HIS SER ASN SEQRES 6 A 285 VAL LEU ALA ARG ILE ASP ALA ALA ALA PHE THR GLY LEU SEQRES 7 A 285 ALA LEU LEU GLU GLN LEU ASP LEU SER ASP ASN ALA GLN SEQRES 8 A 285 LEU ARG SER VAL ASP PRO ALA THR PHE HIS GLY LEU GLY SEQRES 9 A 285 ARG LEU HIS THR LEU HIS LEU ASP ARG CYS GLY LEU GLN SEQRES 10 A 285 GLU LEU GLY PRO GLY LEU PHE ARG GLY LEU ALA ALA LEU SEQRES 11 A 285 GLN TYR LEU TYR LEU GLN ASP ASN ALA LEU GLN ALA LEU SEQRES 12 A 285 PRO ASP ASP THR PHE ARG ASP LEU GLY ASN LEU THR HIS SEQRES 13 A 285 LEU PHE LEU HIS GLY ASN ARG ILE SER SER VAL PRO GLU SEQRES 14 A 285 ARG ALA PHE ARG GLY LEU HIS SER LEU ASP ARG LEU LEU SEQRES 15 A 285 LEU HIS GLN ASN ARG VAL ALA HIS VAL HIS PRO HIS ALA SEQRES 16 A 285 PHE ARG ASP LEU GLY ARG LEU MET THR LEU TYR LEU PHE SEQRES 17 A 285 ALA ASN ASN LEU SER ALA LEU PRO THR GLU ALA LEU ALA SEQRES 18 A 285 PRO LEU ARG ALA LEU GLN TYR LEU ARG LEU ASN ASP ASN SEQRES 19 A 285 PRO TRP VAL CYS ASP CYS ARG ALA ARG PRO LEU TRP ALA SEQRES 20 A 285 TRP LEU GLN LYS PHE ARG GLY SER SER SER GLU VAL PRO SEQRES 21 A 285 CYS SER LEU PRO GLN ARG LEU ALA GLY ARG ASP LEU LYS SEQRES 22 A 285 ARG LEU ALA ALA ASN ASP LEU GLN GLY CYS ALA VAL HET NAG 401 15 HET NDG 402 15 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE HETSYN NAG NAG FORMUL 2 NAG C8 H15 N O6 FORMUL 3 NDG C8 H15 N O6 HELIX 1 1 ASP A 265 ARG A 267 5 3 HELIX 2 2 ALA A 268 PHE A 278 1 11 HELIX 3 3 ASP A 297 LEU A 301 5 5 HELIX 4 4 ALA A 302 LEU A 306 5 5 SHEET 1 A 9 ARG A 61 PHE A 63 0 SHEET 2 A 9 ILE A 85 TRP A 87 1 O ILE A 85 N ILE A 62 SHEET 3 A 9 GLN A 109 ASP A 111 1 O ASP A 111 N LEU A 86 SHEET 4 A 9 THR A 134 HIS A 136 1 O THR A 134 N LEU A 110 SHEET 5 A 9 TYR A 158 TYR A 160 1 O TYR A 158 N LEU A 135 SHEET 6 A 9 HIS A 182 PHE A 184 1 O HIS A 182 N LEU A 159 SHEET 7 A 9 ARG A 206 LEU A 208 1 O LEU A 208 N LEU A 183 SHEET 8 A 9 THR A 230 TYR A 232 1 O TYR A 232 N LEU A 207 SHEET 9 A 9 TYR A 254 ARG A 256 1 O TYR A 254 N LEU A 231 SHEET 1 B 2 HIS A 71 VAL A 72 0 SHEET 2 B 2 ARG A 95 ILE A 96 1 O ARG A 95 N VAL A 72 SHEET 1 C 2 SER A 192 VAL A 193 0 SHEET 2 C 2 HIS A 216 VAL A 217 1 O HIS A 216 N VAL A 193 SHEET 1 D 2 TRP A 262 VAL A 263 0 SHEET 2 D 2 CYS A 287 LEU A 289 1 O SER A 288 N TRP A 262 SSBOND 1 CYS A 27 CYS A 33 SSBOND 2 CYS A 31 CYS A 43 SSBOND 3 CYS A 264 CYS A 287 SSBOND 4 CYS A 266 CYS A 309 CISPEP 1 LEU A 289 PRO A 290 0 0.67 CRYST1 123.958 123.958 120.173 90.00 90.00 120.00 P 31 2 1 6 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 0.008067 0.004658 0.000000 0.00000 SCALE2 0.000000 0.009315 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008321 0.00000