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HEADER HYDROLASE 21-JUN-96 1EUT TITLE SIALIDASE, LARGE 68KD FORM, COMPLEXED WITH GALACTOSE COMPND MOL_ID: 1; COMPND 2 MOLECULE: SIALIDASE; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: NEURAMINIDASE; COMPND 5 EC: 3.2.1.18; COMPND 6 OTHER_DETAILS: LARGE 68KD FORM SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MICROMONOSPORA VIRIDIFACIENS; SOURCE 3 ATCC: 31146 KEYWDS HYDROLASE, GLYCOSIDASE EXPDTA X-RAY DIFFRACTION AUTHOR A.GASKELL,S.J.CRENNELL,G.L.TAYLOR REVDAT 1 11-JAN-97 1EUT 0 JRNL AUTH A.GASKELL,S.CRENNELL,G.TAYLOR JRNL TITL THE THREE DOMAINS OF A BACTERIAL SIALIDASE: A JRNL TITL 2 BETA-PROPELLER, AN IMMUNOGLOBULIN MODULE AND A JRNL TITL 3 GALACTOSE-BINDING JELLY-ROLL. JRNL REF STRUCTURE V. 3 1197 1995 JRNL REFN ASTM STRUE6 UK ISSN 0969-2126 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH G.TAYLOR,L.DINELEY,M.GLOWKA,G.LAVER REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC REMARK 1 TITL 2 STUDY OF NEURAMINIDASE FROM MICROMONOSPORA REMARK 1 TITL 3 VIRIDIFACIENS REMARK 1 REF J.MOL.BIOL. V. 225 1135 1992 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00 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 : 18632 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING SET) : 0.214 REMARK 3 FREE R VALUE : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL 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 : 4536 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 1 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) : 20.70 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) : 0.25 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) : 0.016 REMARK 3 BOND ANGLES (DEGREES) : 2.57 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 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 : PARAM19X.PRO REMARK 3 PARAMETER FILE 2 : NULL REMARK 3 TOPOLOGY FILE 1 : TOPH19X.PRO REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1EUT 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 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : MAY-1995 REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG REMARK 200 BEAMLINE : X11 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.993 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE AREA DETECTOR REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20112 REMARK 200 RESOLUTION RANGE HIGH (A) : NULL REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 79.2 REMARK 200 DATA REDUNDANCY : 2.500 REMARK 200 R MERGE (I) : 0.03900 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: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: X-PLOR 3.1 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL 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,1/2+Y,-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 58.65000 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 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 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 VAL A 43 REMARK 465 PRO A 44 REMARK 465 PRO A 45 REMARK 465 GLY A 46 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 ILE A 404 CB ILE A 404 CG2 0.079 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 GLY A 63 N - CA - C ANGL. DEV. = 12.9 DEGREES REMARK 500 GLY A 86 N - CA - C ANGL. DEV. =-15.5 DEGREES REMARK 500 PRO A 94 C - N - CA ANGL. DEV. = 13.0 DEGREES REMARK 500 ILE A 228 N - CA - C ANGL. DEV. =-13.6 DEGREES REMARK 500 ASP A 291 N - CA - C ANGL. DEV. = 13.0 DEGREES REMARK 500 GLY A 293 N - CA - C ANGL. DEV. =-12.9 DEGREES REMARK 500 HIS A 294 N - CA - C ANGL. DEV. = 14.0 DEGREES REMARK 500 GLY A 403 N - CA - C ANGL. DEV. = 12.6 DEGREES REMARK 500 SER A 431 N - CA - C ANGL. DEV. = 13.0 DEGREES REMARK 500 ALA A 434 N - CA - C ANGL. DEV. =-14.3 DEGREES REMARK 500 GLY A 478 N - CA - C ANGL. DEV. = 21.3 DEGREES REMARK 500 ALA A 526 N - CA - C ANGL. DEV. =-18.2 DEGREES REMARK 500 ARG A 544 N - CA - C ANGL. DEV. =-15.1 DEGREES REMARK 500 TYR A 550 N - CA - C ANGL. DEV. = 22.2 DEGREES REMARK 500 PRO A 551 C - N - CA ANGL. DEV. =-16.8 DEGREES REMARK 500 PRO A 551 C - N - CD ANGL. DEV. = 14.0 DEGREES REMARK 500 ASP A 557 N - CA - C ANGL. DEV. =-12.6 DEGREES REMARK 500 LYS A 634 N - CA - C ANGL. DEV. = 14.7 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 ILE A 404 111.91 30.90 REMARK 500 SER A 527 -15.93 141.85 REMARK 500 ALA A 545 102.79 140.47 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: ACT REMARK 800 SITE_DESCRIPTION: ACTIVE SITE. SITE INCLUDES TWO CONTACTS WITH REMARK 800 SYMMETRY-RELATED MOLECULES. DBREF 1EUT A 43 647 UNP Q02834 NANH_MICVI 43 647 SEQRES 1 A 605 VAL PRO PRO GLY GLY GLU PRO LEU TYR THR GLU GLN ASP SEQRES 2 A 605 LEU ALA VAL ASN GLY ARG GLU GLY PHE PRO ASN TYR ARG SEQRES 3 A 605 ILE PRO ALA LEU THR VAL THR PRO ASP GLY ASP LEU LEU SEQRES 4 A 605 ALA SER TYR ASP GLY ARG PRO THR GLY ILE ASP ALA PRO SEQRES 5 A 605 GLY PRO ASN SER ILE LEU GLN ARG ARG SER THR ASP GLY SEQRES 6 A 605 GLY ARG THR TRP GLY GLU GLN GLN VAL VAL SER ALA GLY SEQRES 7 A 605 GLN THR THR ALA PRO ILE LYS GLY PHE SER ASP PRO SER SEQRES 8 A 605 TYR LEU VAL ASP ARG GLU THR GLY THR ILE PHE ASN PHE SEQRES 9 A 605 HIS VAL TYR SER GLN ARG GLN GLY PHE ALA GLY SER ARG SEQRES 10 A 605 PRO GLY THR ASP PRO ALA ASP PRO ASN VAL LEU HIS ALA SEQRES 11 A 605 ASN VAL ALA THR SER THR ASP GLY GLY LEU THR TRP SER SEQRES 12 A 605 HIS ARG THR ILE THR ALA ASP ILE THR PRO ASP PRO GLY SEQRES 13 A 605 TRP ARG SER ARG PHE ALA ALA SER GLY GLU GLY ILE GLN SEQRES 14 A 605 LEU ARG TYR GLY PRO HIS ALA GLY ARG LEU ILE GLN GLN SEQRES 15 A 605 TYR THR ILE ILE ASN ALA ALA GLY ALA PHE GLN ALA VAL SEQRES 16 A 605 SER VAL TYR SER ASP ASP HIS GLY ARG THR TRP ARG ALA SEQRES 17 A 605 GLY GLU ALA VAL GLY VAL GLY MET ASP GLU ASN LYS THR SEQRES 18 A 605 VAL GLU LEU SER ASP GLY ARG VAL LEU LEU ASN SER ARG SEQRES 19 A 605 ASP SER ALA ARG SER GLY TYR ARG LYS VAL ALA VAL SER SEQRES 20 A 605 THR ASP GLY GLY HIS SER TYR GLY PRO VAL THR ILE ASP SEQRES 21 A 605 ARG ASP LEU PRO ASP PRO THR ASN ASN ALA SER ILE ILE SEQRES 22 A 605 ARG ALA PHE PRO ASP ALA PRO ALA GLY SER ALA ARG ALA SEQRES 23 A 605 LYS VAL LEU LEU PHE SER ASN ALA ALA SER GLN THR SER SEQRES 24 A 605 ARG SER GLN GLY THR ILE ARG MET SER CYS ASP ASP GLY SEQRES 25 A 605 GLN THR TRP PRO VAL SER LYS VAL PHE GLN PRO GLY SER SEQRES 26 A 605 MET SER TYR SER THR LEU THR ALA LEU PRO ASP GLY THR SEQRES 27 A 605 TYR GLY LEU LEU TYR GLU PRO GLY THR GLY ILE ARG TYR SEQRES 28 A 605 ALA ASN PHE ASN LEU ALA TRP LEU GLY GLY ILE CYS ALA SEQRES 29 A 605 PRO PHE THR ILE PRO ASP VAL ALA LEU GLU PRO GLY GLN SEQRES 30 A 605 GLN VAL THR VAL PRO VAL ALA VAL THR ASN GLN SER GLY SEQRES 31 A 605 ILE ALA VAL PRO LYS PRO SER LEU GLN LEU ASP ALA SER SEQRES 32 A 605 PRO ASP TRP GLN VAL GLN GLY SER VAL GLU PRO LEU MET SEQRES 33 A 605 PRO GLY ARG GLN ALA LYS GLY GLN VAL THR ILE THR VAL SEQRES 34 A 605 PRO ALA GLY THR THR PRO GLY ARG TYR ARG VAL GLY ALA SEQRES 35 A 605 THR LEU ARG THR SER ALA GLY ASN ALA SER THR THR PHE SEQRES 36 A 605 THR VAL THR VAL GLY LEU LEU ASP GLN ALA ARG MET SER SEQRES 37 A 605 ILE ALA ASP VAL ASP SER GLU GLU THR ALA ARG GLU ASP SEQRES 38 A 605 GLY ARG ALA SER ASN VAL ILE ASP GLY ASN PRO SER THR SEQRES 39 A 605 PHE TRP HIS THR GLU TRP SER ARG ALA ASP ALA PRO GLY SEQRES 40 A 605 TYR PRO HIS ARG ILE SER LEU ASP LEU GLY GLY THR HIS SEQRES 41 A 605 THR ILE SER GLY LEU GLN TYR THR ARG ARG GLN ASN SER SEQRES 42 A 605 ALA ASN GLU GLN VAL ALA ASP TYR GLU ILE TYR THR SER SEQRES 43 A 605 LEU ASN GLY THR THR TRP ASP GLY PRO VAL ALA SER GLY SEQRES 44 A 605 ARG PHE THR THR SER LEU ALA PRO GLN ARG ALA VAL PHE SEQRES 45 A 605 PRO ALA ARG ASP ALA ARG TYR ILE ARG LEU VAL ALA LEU SEQRES 46 A 605 SER GLU GLN THR GLY HIS LYS TYR ALA ALA VAL ALA GLU SEQRES 47 A 605 LEU GLU VAL GLU GLY GLN ARG HET NA 1 1 HETNAM NA SODIUM ION FORMUL 2 NA NA 1+ HELIX 1 1 ARG A 61 GLY A 63 5 3 HELIX 2 2 GLY A 215 HIS A 217 5 3 HELIX 3 3 ARG A 327 LYS A 329 5 3 HELIX 4 4 LEU A 398 TRP A 400 5 3 HELIX 5 5 GLN A 506 ARG A 508 5 3 SHEET 1 A 4 ALA A 71 VAL A 74 0 SHEET 2 A 4 LEU A 80 GLY A 86 -1 N SER A 83 O ALA A 71 SHEET 3 A 4 SER A 98 SER A 104 -1 N SER A 104 O LEU A 80 SHEET 4 A 4 GLN A 115 SER A 118 -1 N SER A 118 O ILE A 99 SHEET 1 B 4 GLY A 128 SER A 130 0 SHEET 2 B 4 ILE A 143 SER A 150 -1 N SER A 150 O GLY A 128 SHEET 3 B 4 HIS A 171 SER A 177 -1 N SER A 177 O ILE A 143 SHEET 4 B 4 SER A 185 THR A 188 -1 N ARG A 187 O VAL A 174 SHEET 1 C 2 SER A 133 VAL A 136 0 SHEET 2 C 2 ILE A 143 PHE A 146 -1 N PHE A 146 O SER A 133 SHEET 1 D 3 SER A 201 ALA A 204 0 SHEET 2 D 3 LEU A 221 ILE A 228 -1 N ILE A 228 O SER A 201 SHEET 3 D 3 PHE A 234 SER A 241 -1 N SER A 241 O LEU A 221 SHEET 1 E 4 ASN A 261 GLU A 265 0 SHEET 2 E 4 VAL A 271 SER A 275 -1 N ASN A 274 O LYS A 262 SHEET 3 E 4 TYR A 283 SER A 289 -1 N SER A 289 O VAL A 271 SHEET 4 E 4 THR A 300 PRO A 306 -1 N LEU A 305 O ARG A 284 SHEET 1 F 4 SER A 313 ARG A 316 0 SHEET 2 F 4 LEU A 331 ALA A 336 -1 N SER A 334 O SER A 313 SHEET 3 F 4 GLY A 345 SER A 350 -1 N SER A 350 O LEU A 331 SHEET 4 F 4 VAL A 359 GLN A 364 -1 N GLN A 364 O GLY A 345 SHEET 1 G 4 SER A 371 ALA A 375 0 SHEET 2 G 4 TYR A 381 TYR A 385 -1 N LEU A 384 O THR A 372 SHEET 3 G 4 GLY A 390 PHE A 396 -1 N PHE A 396 O TYR A 381 SHEET 4 G 4 TYR A 51 VAL A 58 -1 N ALA A 57 O ILE A 391 SHEET 1 H 4 PHE A 408 ILE A 410 0 SHEET 2 H 4 GLN A 419 THR A 428 -1 N ALA A 426 O THR A 409 SHEET 3 H 4 GLN A 462 VAL A 471 -1 N VAL A 471 O GLN A 419 SHEET 4 H 4 TRP A 448 VAL A 454 -1 N SER A 453 O GLN A 466 SHEET 1 I 4 VAL A 413 LEU A 415 0 SHEET 2 I 4 GLY A 491 VAL A 501 1 N THR A 500 O VAL A 413 SHEET 3 I 4 TYR A 480 THR A 488 -1 N THR A 488 O GLY A 491 SHEET 4 I 4 SER A 439 ASP A 443 -1 N ASP A 443 O GLY A 483 SHEET 1 J 5 ALA A 599 ARG A 602 0 SHEET 2 J 5 ASP A 582 SER A 588 -1 N ILE A 585 O ALA A 599 SHEET 3 J 5 TYR A 621 ALA A 626 -1 N VAL A 625 O GLU A 584 SHEET 4 J 5 HIS A 552 ASP A 557 -1 N LEU A 556 O ILE A 622 SHEET 5 J 5 SER A 510 VAL A 514 -1 N ASP A 513 O SER A 555 SHEET 1 K 3 ARG A 617 ALA A 619 0 SHEET 2 K 3 HIS A 562 THR A 570 -1 N ILE A 564 O ARG A 617 SHEET 3 K 3 GLU A 640 GLY A 645 -1 N GLU A 644 O SER A 565 SHEET 1 L 2 GLY A 566 TYR A 569 0 SHEET 2 L 2 GLN A 610 VAL A 613 -1 N ALA A 612 O LEU A 567 SSBOND 1 CYS A 351 CYS A 405 LINK NA NA 1 O ASN A 528 LINK NA NA 1 O ASN A 533 LINK NA NA 1 O THR A 536 LINK NA NA 1 OG1 THR A 536 LINK NA NA 1 O ALA A 639 CISPEP 1 ALA A 93 PRO A 94 0 0.52 CISPEP 2 ALA A 124 PRO A 125 0 -0.08 CISPEP 3 GLY A 596 PRO A 597 0 0.08 SITE 1 ACT 9 GLN A 224 GLY A 245 ALA A 250 GLY A 292 SITE 2 ACT 9 ASN A 311 PHE A 318 ALA A 619 TYR A 635 SITE 3 ACT 9 ALA A 637 CRYST1 51.280 117.300 60.240 90.00 96.17 90.00 P 1 21 1 2 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 0.019501 0.000000 0.002108 0.00000 SCALE2 0.000000 0.008525 0.000000 0.00000 SCALE3 0.000000 0.000000 0.016697 0.00000