[Scop | Full Entry | Seq (local cached copy) | More Options ]
HEADER HYDROLASE 21-OCT-05 2BDY TITLE THROMBIN IN COMPLEX WITH INHIBITOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: THROMBIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: HEAVY AND LIGHT CHAIN, RESIDUES 334-622; COMPND 5 EC: 3.4.21.5; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: HIRUDIN IIIB'; COMPND 8 CHAIN: B; COMPND 9 FRAGMENT: RESIDUES 55-64; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 MOL_ID: 2; SOURCE 5 SYNTHETIC: YES; SOURCE 6 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HIRUDO SOURCE 7 MEDICINALIS (MEDICINAL LEECH). KEYWDS THROMBIN, COMPLEX STRUCTURE EXPDTA X-RAY DIFFRACTION AUTHOR Y.XUE REVDAT 1 24-OCT-06 2BDY 0 JRNL AUTH S.HANESSIAN,E.THERRIEN,W.A.VAN OTTERLO, JRNL AUTH 2 M.BAYRAKDARIAN,I.NILSSON,Y.XUE JRNL TITL PHENOLIC P2/P3 CORE MOTIF AS THROMBIN JRNL TITL 2 INHIBITORS--DESIGN, SYNTHESIS, AND X-RAY JRNL TITL 3 CO-CRYSTAL STRUCTURE. JRNL REF BIOORG.MED.CHEM.LETT. V. 16 1032 2006 JRNL REFN ASTM BMCLE8 UK ISSN 0960-894X REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.61 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.1.24 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.61 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 70.71 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8 REMARK 3 NUMBER OF REFLECTIONS : 43773 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) : 0.194 REMARK 3 R VALUE (WORKING SET) : 0.193 REMARK 3 FREE R VALUE : 0.225 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.500 REMARK 3 FREE R VALUE TEST SET COUNT : 1530 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH : 1.61 REMARK 3 BIN RESOLUTION RANGE LOW : 1.65 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2773 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.3170 REMARK 3 BIN FREE R VALUE SET COUNT : 99 REMARK 3 BIN FREE R VALUE : 0.3390 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 ALL ATOMS : 2719 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.50 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.16000 REMARK 3 B22 (A**2) : -0.69000 REMARK 3 B33 (A**2) : 0.27000 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): 0.093 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.094 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.079 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.390 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2425 ; 0.012 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): 2135 ; 0.002 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3278 ; 1.426 ; 1.986 REMARK 3 BOND ANGLES OTHERS (DEGREES): 4982 ; 0.793 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 282 ; 6.408 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 334 ; 0.082 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2651 ; 0.006 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 489 ; 0.003 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 459 ; 0.204 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2613 ; 0.245 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): 1369 ; 0.083 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 252 ; 0.189 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 3 ; 0.073 ; 0.200 REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 5 ; 0.241 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 46 ; 0.335 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 21 ; 0.242 ; 0.200 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): 1422 ; 0.879 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2292 ; 1.606 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1003 ; 2.204 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 986 ; 3.646 ; 4.500 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 NUMBER OF DIFFERENT NCS GROUPS : 0 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 0 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 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 REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 2BDY 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 3.101 (2007-05-29) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE RCSB ID CODE IS RCSB034980. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 07-JUN-2004 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.30 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.54179 REMARK 200 MONOCHROMATOR : MIRROR REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA) REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43774 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.610 REMARK 200 RESOLUTION RANGE LOW (A) : 70.710 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9 REMARK 200 DATA REDUNDANCY : 3.700 REMARK 200 R MERGE (I) : 0.13200 REMARK 200 R SYM (I) : 0.13200 REMARK 200 FOR THE DATA SET : 3.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.61 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70 REMARK 200 COMPLETENESS FOR SHELL (%) : 91.9 REMARK 200 DATA REDUNDANCY IN SHELL : 3.60 REMARK 200 R MERGE FOR SHELL (I) : 0.35500 REMARK 200 R SYM FOR SHELL (I) : 0.35500 REMARK 200 FOR SHELL : 2.100 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLECULAR REPLACEMENT REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.64 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 27% PEG8000, 0.1M SODIUM PHOSPHATE, REMARK 280 PH 7.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 1/2+X,1/2+Y,Z REMARK 290 4555 1/2-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 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 34.95900 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.82450 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 34.95900 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 35.82450 REMARK 290 SMTRY3 4 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 2 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, 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 ASP A 34 REMARK 465 GLY A 35 REMARK 465 ARG A 36 REMARK 465 TRP A 183A REMARK 465 THR A 183B REMARK 465 ALA A 183C REMARK 465 ASN A 183D REMARK 465 VAL A 183E REMARK 465 GLY A 183F REMARK 465 LYS A 183G REMARK 465 PHE A 287 REMARK 465 GLY A 288 REMARK 465 GLU A 289 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLU B 361 CB CG CD OE1 OE2 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 O HOH 68 O HOH 378 2.05 REMARK 500 O HOH 227 O HOH 381 2.15 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 53 SD MET A 53 CE -0.104 REMARK 500 ARG A 106 CB ARG A 106 CG 0.106 REMARK 500 MET A 252 CG MET A 252 SD -0.081 REMARK 500 MET A 252 SD MET A 252 CE -0.114 REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH 392 DISTANCE = 5.01 ANGSTROMS REMARK 525 HOH 417 DISTANCE = 5.47 ANGSTROMS DBREF 2BDY A 7 289 UNP P00734 THRB_HUMAN 334 622 DBREF 2BDY B 355 364 UNP P28511 ITHK_HIRME 55 64 SEQADV 2BDY TYS B 363 UNP P28511 TYR 63 MODIFIED RESIDUE SEQRES 1 A 289 ALA ASP CYS GLY LEU ARG PRO LEU PHE GLU LYS LYS SER SEQRES 2 A 289 LEU GLU ASP LYS THR GLU ARG GLU LEU LEU GLU SER TYR SEQRES 3 A 289 ILE ASP GLY ARG ILE VAL GLU GLY SER ASP ALA GLU ILE SEQRES 4 A 289 GLY MET SER PRO TRP GLN VAL MET LEU PHE ARG LYS SER SEQRES 5 A 289 PRO GLN GLU LEU LEU CYS GLY ALA SER LEU ILE SER ASP SEQRES 6 A 289 ARG TRP VAL LEU THR ALA ALA HIS CYS LEU LEU TYR PRO SEQRES 7 A 289 PRO TRP ASP LYS ASN PHE THR GLU ASN ASP LEU LEU VAL SEQRES 8 A 289 ARG ILE GLY LYS HIS SER ARG THR ARG TYR GLU ARG ASN SEQRES 9 A 289 ILE GLU LYS ILE SER MET LEU GLU LYS ILE TYR ILE HIS SEQRES 10 A 289 PRO ARG TYR ASN TRP ARG GLU ASN LEU ASP ARG ASP ILE SEQRES 11 A 289 ALA LEU MET LYS LEU LYS LYS PRO VAL ALA PHE SER ASP SEQRES 12 A 289 TYR ILE HIS PRO VAL CYS LEU PRO ASP ARG GLU THR ALA SEQRES 13 A 289 ALA SER LEU LEU GLN ALA GLY TYR LYS GLY ARG VAL THR SEQRES 14 A 289 GLY TRP GLY ASN LEU LYS GLU THR TRP THR ALA ASN VAL SEQRES 15 A 289 GLY LYS GLY GLN PRO SER VAL LEU GLN VAL VAL ASN LEU SEQRES 16 A 289 PRO ILE VAL GLU ARG PRO VAL CYS LYS ASP SER THR ARG SEQRES 17 A 289 ILE ARG ILE THR ASP ASN MET PHE CYS ALA GLY TYR LYS SEQRES 18 A 289 PRO ASP GLU GLY LYS ARG GLY ASP ALA CYS GLU GLY ASP SEQRES 19 A 289 SER GLY GLY PRO PHE VAL MET LYS SER PRO PHE ASN ASN SEQRES 20 A 289 ARG TRP TYR GLN MET GLY ILE VAL SER TRP GLY GLU GLY SEQRES 21 A 289 CYS ASP ARG ASP GLY LYS TYR GLY PHE TYR THR HIS VAL SEQRES 22 A 289 PHE ARG LEU LYS LYS TRP ILE GLN LYS VAL ILE ASP GLN SEQRES 23 A 289 PHE GLY GLU SEQRES 1 B 10 ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU MODRES 2BDY TYS B 363 TYR SULFONATED TYROSINE HET TYS B 363 16 HET NA 402 1 HET UNB 401 36 HETNAM TYS SULFONATED TYROSINE HETNAM NA SODIUM ION HETNAM UNB N-(4-CARBAMIMIDOYL-BENZYL)-2-[2-HYDROXY-6-METHYL-3- HETNAM 2 UNB (NAPHTHALENE-1-SULFONYLAMINO)-PHENYL]-ACETAMIDE FORMUL 2 TYS C9 H11 N O6 S FORMUL 3 NA NA 1+ FORMUL 4 UNB C27 H26 N4 O4 S FORMUL 5 HOH *357(H2 O) HELIX 1 1 PHE A 15 SER A 19 5 5 HELIX 2 2 THR A 24 TYR A 32 1 9 HELIX 3 3 ALA A 77 CYS A 80 5 4 HELIX 4 4 PRO A 84 ASP A 87 5 4 HELIX 5 5 THR A 91 ASN A 93 5 3 HELIX 6 6 ASP A 158 LEU A 166 1 9 HELIX 7 7 GLU A 199 SER A 206 1 8 HELIX 8 8 LYS A 221 GLY A 225 5 5 HELIX 9 9 LEU A 276 GLN A 286 1 11 HELIX 10 10 PRO B 360 LEU B 364 5 5 SHEET 1 A 7 SER A 41 ASP A 42 0 SHEET 2 A 7 GLN A 191 PRO A 196 -1 O VAL A 192 N SER A 41 SHEET 3 A 7 LYS A 171 GLY A 176 -1 N VAL A 174 O VAL A 193 SHEET 4 A 7 PRO A 238 LYS A 242 -1 O VAL A 240 N ARG A 173 SHEET 5 A 7 TRP A 249 TRP A 257 -1 O TYR A 250 N MET A 241 SHEET 6 A 7 GLY A 268 HIS A 272 -1 O PHE A 269 N TRP A 257 SHEET 7 A 7 MET A 215 ALA A 218 -1 N PHE A 216 O TYR A 270 SHEET 1 B 7 GLN A 51 ARG A 56 0 SHEET 2 B 7 GLU A 61 LEU A 68 -1 O CYS A 64 N LEU A 54 SHEET 3 B 7 TRP A 73 THR A 76 -1 O LEU A 75 N SER A 67 SHEET 4 B 7 ALA A 137 LEU A 141 -1 O ALA A 137 N THR A 76 SHEET 5 B 7 LYS A 113 ILE A 122 -1 N TYR A 121 O LEU A 138 SHEET 6 B 7 LEU A 95 ILE A 99 -1 N ILE A 99 O LYS A 113 SHEET 7 B 7 GLN A 51 ARG A 56 -1 N PHE A 55 O LEU A 96 SHEET 1 C 2 LEU A 82 TYR A 83 0 SHEET 2 C 2 LYS A 88 ASN A 89 -1 O LYS A 88 N TYR A 83 SSBOND 1 CYS A 9 CYS A 155 SSBOND 2 CYS A 64 CYS A 80 SSBOND 3 CYS A 203 CYS A 217 SSBOND 4 CYS A 231 CYS A 261 CRYST1 69.918 71.649 71.234 90.00 99.56 90.00 C 1 2 1 4 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 0.014300 0.000000 0.002410 0.00000 SCALE2 0.000000 0.013960 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014240 0.00000