HEADER PROTEIN BINDING 25-MAR-24 9ERT TITLE MOUSE CNPASE CATALYTIC DOMAIN WITH NANO BODY 5E COMPND MOL_ID: 1; COMPND 2 MOLECULE: 2',3'-CYCLIC-NUCLEOTIDE 3'-PHOSPHODIESTERASE; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: CNP,CNPASE; COMPND 5 EC: 3.1.4.37; COMPND 6 ENGINEERED: YES; COMPND 7 OTHER_DETAILS: MOUSE CNPASE CATALYTIC DOMAIN; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: CHAINS: B; COMPND 10 CHAIN: B; COMPND 11 ENGINEERED: YES; COMPND 12 OTHER_DETAILS: ANTI-CNPASE NANOBODY 5E SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: CNP, CNP1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 10 ORGANISM_TAXID: 30538; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS CNPASE, MYELIN, NANOBODY, SINGLE-DOMAIN ANTIBODY, COMPLEX, PROTEIN KEYWDS 2 BINDING EXPDTA X-RAY DIFFRACTION AUTHOR S.MARKUSSON,A.RAASAKKA,F.OPAZO,P.KURSULA REVDAT 1 11-DEC-24 9ERT 0 JRNL AUTH S.MARKUSSON,A.RAASAKKA,F.OPAZO,P.KURSULA JRNL TITL MOUSE CNPASE CATALYTIC DOMAIN WITH NANO BODY 5E JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.75 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21RC1_5127 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.99 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 69.9 REMARK 3 NUMBER OF REFLECTIONS : 10949 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.293 REMARK 3 R VALUE (WORKING SET) : 0.289 REMARK 3 FREE R VALUE : 0.323 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.090 REMARK 3 FREE R VALUE TEST SET COUNT : 1105 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 47.9900 - 5.5000 0.99 1828 210 0.2928 0.3111 REMARK 3 2 5.5000 - 4.3700 1.00 1767 198 0.2751 0.2939 REMARK 3 3 4.3700 - 3.8200 1.00 1766 199 0.2530 0.3360 REMARK 3 4 3.8100 - 3.4700 0.99 1720 191 0.3158 0.3106 REMARK 3 5 3.4700 - 3.2200 0.93 1625 181 0.3084 0.3742 REMARK 3 6 3.2200 - 3.0300 0.42 732 83 0.3651 0.4144 REMARK 3 7 3.0300 - 2.8800 0.18 305 33 0.3704 0.5153 REMARK 3 8 2.8800 - 2.7500 0.06 101 10 0.3908 0.3748 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.473 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 43.891 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 68.32 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 74.19 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 : 0.002 2699 REMARK 3 ANGLE : 0.559 3646 REMARK 3 CHIRALITY : 0.038 387 REMARK 3 PLANARITY : 0.005 471 REMARK 3 DIHEDRAL : 16.708 970 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN 'A' AND RESID 163 THROUGH 378) REMARK 3 ORIGIN FOR THE GROUP (A): -9.2300 78.0896 35.5162 REMARK 3 T TENSOR REMARK 3 T11: 0.2997 T22: 0.6277 REMARK 3 T33: 0.4243 T12: 0.3821 REMARK 3 T13: 0.0109 T23: 0.1107 REMARK 3 L TENSOR REMARK 3 L11: 0.4497 L22: 0.2108 REMARK 3 L33: 0.2257 L12: 0.0466 REMARK 3 L13: 0.2702 L23: -0.0317 REMARK 3 S TENSOR REMARK 3 S11: 0.1231 S12: 0.4980 S13: 0.1781 REMARK 3 S21: -0.3810 S22: -0.1268 S23: 0.2693 REMARK 3 S31: -0.1608 S32: -0.0753 S33: -0.1392 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN 'B' AND RESID 1 THROUGH 132) REMARK 3 ORIGIN FOR THE GROUP (A): 18.0121 58.5614 38.2299 REMARK 3 T TENSOR REMARK 3 T11: -0.0233 T22: 0.2625 REMARK 3 T33: 0.0879 T12: 0.3454 REMARK 3 T13: 0.2363 T23: -0.1381 REMARK 3 L TENSOR REMARK 3 L11: 0.0950 L22: 0.1763 REMARK 3 L33: 0.0944 L12: 0.0985 REMARK 3 L13: 0.0117 L23: 0.0194 REMARK 3 S TENSOR REMARK 3 S11: 0.0718 S12: -0.0782 S13: -0.0301 REMARK 3 S21: 0.1095 S22: -0.0165 S23: -0.1004 REMARK 3 S31: -0.0240 S32: -0.1237 S33: 0.1532 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 9ERT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-MAR-24. REMARK 100 THE DEPOSITION ID IS D_1292137541. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-APR-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PETRA III, DESY REMARK 200 BEAMLINE : P11 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.033 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : STARANISO REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10986 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 70.0 REMARK 200 DATA REDUNDANCY : 5.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.15 REMARK 200 COMPLETENESS FOR SHELL (%) : 18.0 REMARK 200 DATA REDUNDANCY IN SHELL : 6.30 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.600 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 (%): 68.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.84 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M NA/K PHOSPHATE PH 7.0, 25% REMARK 280 PEG3350, VAPOR DIFFUSION, SITTING 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,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+2/3 REMARK 290 6555 -X,-X+Y,-Z+1/3 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 27.76033 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 55.52067 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 55.52067 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 27.76033 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA 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 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 GLY A 159 REMARK 465 LEU A 160 REMARK 465 GLU A 161 REMARK 465 LYS A 162 REMARK 465 ILE A 206 REMARK 465 SER A 207 REMARK 465 GLY A 208 REMARK 465 LYS A 295 REMARK 465 PRO A 296 REMARK 465 SER A 297 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 PHE A 164 57.56 -97.86 REMARK 500 LYS A 214 -105.79 54.80 REMARK 500 TYR A 238 107.76 65.33 REMARK 500 LYS A 240 90.51 -51.31 REMARK 500 ALA A 242 60.40 72.82 REMARK 500 THR A 274 -166.78 -129.64 REMARK 500 SER A 291 48.22 -90.15 REMARK 500 LEU A 293 -52.33 -158.95 REMARK 500 ALA A 316 -114.71 53.23 REMARK 500 VAL A 321 68.12 -58.41 REMARK 500 GLU A 341 173.09 59.12 REMARK 500 ALA A 342 86.20 -62.91 REMARK 500 ARG A 348 5.29 81.32 REMARK 500 LYS A 356 97.78 -66.07 REMARK 500 THR A 374 -159.90 -122.80 REMARK 500 SER B 7 -170.47 -170.86 REMARK 500 ASP B 54 -76.40 -94.39 REMARK 500 ASP B 115 99.86 -69.10 REMARK 500 PHE B 116 3.83 -69.74 REMARK 500 REMARK 500 REMARK: NULL DBREF 9ERT A 159 378 UNP P16330 CN37_MOUSE 179 398 DBREF 9ERT B 1 132 PDB 9ERT 9ERT 1 132 SEQRES 1 A 220 GLY LEU GLU LYS ASP PHE LEU PRO LEU TYR PHE GLY TRP SEQRES 2 A 220 PHE LEU THR LYS LYS SER SER GLU THR LEU ARG LYS ALA SEQRES 3 A 220 GLY GLN VAL PHE LEU GLU GLU LEU GLY ASN HIS LYS ALA SEQRES 4 A 220 PHE LYS LYS GLU LEU ARG HIS PHE ILE SER GLY ASP GLU SEQRES 5 A 220 PRO LYS GLU LYS LEU GLU LEU VAL SER TYR PHE GLY LYS SEQRES 6 A 220 ARG PRO PRO GLY VAL LEU HIS CYS THR THR LYS PHE CYS SEQRES 7 A 220 ASP TYR GLY LYS ALA ALA GLY ALA GLU GLU TYR ALA GLN SEQRES 8 A 220 GLN GLU VAL VAL LYS ARG SER TYR GLY LYS ALA PHE LYS SEQRES 9 A 220 LEU SER ILE SER ALA LEU PHE VAL THR PRO LYS THR ALA SEQRES 10 A 220 GLY ALA GLN VAL VAL LEU THR ASP GLN GLU LEU GLN LEU SEQRES 11 A 220 TRP PRO SER ASP LEU ASP LYS PRO SER ALA SER GLU GLY SEQRES 12 A 220 LEU PRO PRO GLY SER ARG ALA HIS VAL THR LEU GLY CYS SEQRES 13 A 220 ALA ALA ASP VAL GLN PRO VAL GLN THR GLY LEU ASP LEU SEQRES 14 A 220 LEU ASP ILE LEU GLN GLN VAL LYS GLY GLY SER GLN GLY SEQRES 15 A 220 GLU ALA VAL GLY GLU LEU PRO ARG GLY LYS LEU TYR SER SEQRES 16 A 220 LEU GLY LYS GLY ARG TRP MET LEU SER LEU THR LYS LYS SEQRES 17 A 220 MET GLU VAL LYS ALA ILE PHE THR GLY TYR TYR GLY SEQRES 1 B 132 GLU VAL GLN LEU LEU GLU SER GLY GLY GLY SER VAL GLN SEQRES 2 B 132 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 B 132 PHE THR VAL GLY ASP TYR ALA ILE GLY TRP PHE ARG GLN SEQRES 4 B 132 ALA PRO GLY GLN GLN ARG GLU ALA VAL ALA CYS ILE SER SEQRES 5 B 132 THR ASP ASP GLY ASP THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 B 132 GLY ARG PHE THR ILE SER SER ASP ASN ALA LYS LYS THR SEQRES 7 B 132 ALA TYR LEU GLU MET ASN ASN LEU LYS PRO GLU ASP THR SEQRES 8 B 132 ALA VAL TYR HIS CYS ALA VAL ASP GLY TRP ASP SER SER SEQRES 9 B 132 CYS THR PHE TYR SER PRO SER TYR TYR ARG ASP PHE SER SEQRES 10 B 132 ASP HIS GLY ALA TRP GLY GLN GLY THR GLN VAL THR VAL SEQRES 11 B 132 SER SER HET PO4 A 401 5 HETNAM PO4 PHOSPHATE ION FORMUL 3 PO4 O4 P 3- HELIX 1 AA1 THR A 174 HIS A 195 1 22 HELIX 2 AA2 HIS A 195 GLU A 201 1 7 HELIX 3 AA3 GLU A 216 PHE A 221 1 6 HELIX 4 AA4 GLY A 243 GLN A 249 1 7 HELIX 5 AA5 GLN A 250 TYR A 257 1 8 HELIX 6 AA6 THR A 282 GLN A 287 1 6 HELIX 7 AA7 VAL A 321 GLY A 336 1 16 HELIX 8 AA8 ASP B 62 LYS B 65 5 4 HELIX 9 AA9 LYS B 87 THR B 91 5 5 HELIX 10 AB1 CYS B 105 SER B 109 5 5 SHEET 1 AA1 6 HIS A 230 PHE A 235 0 SHEET 2 AA1 6 TYR A 168 LEU A 173 -1 N TRP A 171 O CYS A 231 SHEET 3 AA1 6 TRP A 359 GLY A 375 -1 O ILE A 372 N PHE A 172 SHEET 4 AA1 6 LYS A 259 VAL A 270 -1 N LEU A 263 O VAL A 369 SHEET 5 AA1 6 THR A 274 VAL A 279 -1 O GLN A 278 N ALA A 267 SHEET 6 AA1 6 HIS A 309 CYS A 314 -1 O LEU A 312 N ALA A 275 SHEET 1 AA2 4 HIS A 230 PHE A 235 0 SHEET 2 AA2 4 TYR A 168 LEU A 173 -1 N TRP A 171 O CYS A 231 SHEET 3 AA2 4 TRP A 359 GLY A 375 -1 O ILE A 372 N PHE A 172 SHEET 4 AA2 4 GLY A 349 SER A 353 -1 N LYS A 350 O SER A 362 SHEET 1 AA3 4 GLN B 3 SER B 7 0 SHEET 2 AA3 4 GLY B 16 SER B 25 -1 O ALA B 23 N LEU B 5 SHEET 3 AA3 4 THR B 78 LEU B 86 -1 O LEU B 81 N LEU B 20 SHEET 4 AA3 4 ILE B 70 ASP B 73 -1 N ASP B 73 O THR B 78 SHEET 1 AA4 6 SER B 11 GLN B 13 0 SHEET 2 AA4 6 THR B 126 SER B 131 1 O THR B 129 N VAL B 12 SHEET 3 AA4 6 ALA B 92 ASP B 99 -1 N ALA B 92 O VAL B 128 SHEET 4 AA4 6 ALA B 33 GLN B 39 -1 N PHE B 37 O HIS B 95 SHEET 5 AA4 6 ALA B 49 SER B 52 -1 O ILE B 51 N ILE B 34 SHEET 6 AA4 6 THR B 58 TYR B 60 -1 O TYR B 59 N CYS B 50 SHEET 1 AA5 4 GLU B 46 ALA B 47 0 SHEET 2 AA5 4 ALA B 33 GLN B 39 -1 N ARG B 38 O GLU B 46 SHEET 3 AA5 4 ALA B 92 ASP B 99 -1 O HIS B 95 N PHE B 37 SHEET 4 AA5 4 GLY B 120 TRP B 122 -1 O ALA B 121 N VAL B 98 SSBOND 1 CYS B 22 CYS B 96 1555 1555 2.02 SSBOND 2 CYS B 50 CYS B 105 1555 1555 2.03 CRYST1 110.832 110.832 83.281 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 0.009023 0.005209 0.000000 0.00000 SCALE2 0.000000 0.010418 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012008 0.00000