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HEADER HYDROLASE/HYDROLASE INHIBITOR 21-DEC-99 1DOJ TITLE CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN*RWJ-51438 COMPLEX TITLE 2 AT 1.7 A COMPND MOL_ID: 1; COMPND 2 MOLECULE: ALPHA-THROMBIN; COMPND 3 CHAIN: A; COMPND 4 EC: 3.4.21.5; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HIRUGEN; COMPND 7 CHAIN: B; COMPND 8 FRAGMENT: FRAGMENT OF HIRUDIN; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: PROTEIN (RWJ-51438); COMPND 12 CHAIN: I; COMPND 13 ENGINEERED: YES; COMPND 14 OTHER_DETAILS: RWJ-51438 IS JOINED COVALENTLY TO SER195 OF COMPND 15 HUMAN ALPHA-THROMBIN SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 CELLULAR_LOCATION: PLASMA; SOURCE 5 MOL_ID: 2; SOURCE 6 SYNTHETIC: YES; SOURCE 7 OTHER_DETAILS: HIRUGEN, COMES FROM HIRUDIN; SOURCE 8 MOL_ID: 3; SOURCE 9 SYNTHETIC: YES; SOURCE 10 OTHER_DETAILS: RWJ-51438 WAS CHEMICALLY SYNTHESIZED KEYWDS THROMBIN, SERINE PROTEASE, ENZYME INHIBITION EXPDTA X-RAY DIFFRACTION AUTHOR R.RECACHA,M.J.COSTANZO,B.E.MARYANOFF,M.CARSON,L.DELUCAS, AUTHOR 2 D.CHATTOPADHYAY REVDAT 2 01-APR-03 1DOJ 1 JRNL REVDAT 1 03-NOV-00 1DOJ 0 JRNL AUTH R.RECACHA,M.J.COSTANZO,B.E.MARYANOFF,M.CARSON, JRNL AUTH 2 L.DELUCAS,D.CHATTOPADHYAY JRNL TITL STRUCTURE OF HUMAN ALPHA-THROMBIN COMPLEXED WITH JRNL TITL 2 RWJ-51438 AT 1.7 A: UNUSUAL PERTURBATION OF THE JRNL TITL 3 60A-60I INSERTION LOOP. JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 56 1395 2000 JRNL REFN ASTM ABCRE6 DK ISSN 0907-4449 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH X.QIU,K.P.PADMANABHAN,V.E.CARPEROS,A.TULINSKY, REMARK 1 AUTH 2 T.KLINE,J.M.MARAGANORE,J.W.FENTON II REMARK 1 TITL STRUCTURE OF THE HIRULOG 3-THROMBIN COMPLEX AND REMARK 1 TITL 2 NATURE OF THE S' SUBSITES OF SUBSTRATES AND REMARK 1 TITL 3 INHIBITORS REMARK 1 REF BIOCHEMISTRY V. 31 11689 1992 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 REMARK 1 REFERENCE 2 REMARK 1 AUTH J.H.MATTHEWS,R.KRISHNAN,M.J.COSTANZO,B.E.MARYANOFF, REMARK 1 AUTH 2 A.TULINSKY REMARK 1 TITL CRYSTAL STRUCTURE OF THROMBIN WITH REMARK 1 TITL 2 THIAZOLE-CONTAINING INHIBITORS: PROBES OF THE S1' REMARK 1 TITL 3 BINDING SITE REMARK 1 REF BIOPHYS.J. V. 71 2830 1996 REMARK 1 REFN ASTM BIOJAU US ISSN 0006-3495 REMARK 1 REFERENCE 3 REMARK 1 AUTH W.BODE,D.TURK,A.KARSHIKOV REMARK 1 TITL THE REFINED 1.9-A X-RAY CRYSTAL STRUCTURE OF REMARK 1 TITL 2 D-PRO-PHE-ARG CHLOROMETHYLKETONE-INHIBITED HUMAN REMARK 1 TITL 3 ALPHA-THROMBIN: STRUCTURE ANALYSIS, OVERALL REMARK 1 TITL 4 STRUCTURE, ELECTROSTATIC PROPERTIES, DETAILED REMARK 1 TITL 5 ACTIVE-SITE GEOMETRY, AND STRUCTURE-FUNCTION REMARK 1 TITL 6 RELATIONSHIPS REMARK 1 REF PROTEIN SCI. V. 1 426 1992 REMARK 1 REFN ASTM PRCIEI US ISSN 0961-8368 REMARK 2 REMARK 2 RESOLUTION. 1.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1520225.350 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.2 REMARK 3 NUMBER OF REFLECTIONS : 33357 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) : 0.174 REMARK 3 FREE R VALUE : 0.217 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT : 3322 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 6 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.70 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.81 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 56.40 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3311 REMARK 3 BIN R VALUE (WORKING SET) : 0.2760 REMARK 3 BIN FREE R VALUE : 0.2980 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 3670 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.016 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2837 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 16.20 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.50 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.02000 REMARK 3 B22 (A**2) : -1.45000 REMARK 3 B33 (A**2) : 0.43000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.18 REMARK 3 ESD FROM SIGMAA (A) : 0.13 REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.21 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.16 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.40 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.30 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.61 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 1.400 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.060 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 2.420 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.480 ; 2.500 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 : TOPPAR:PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : INH3.PARAM REMARK 3 PARAMETER FILE 3 : ION.PARAM REMARK 3 PARAMETER FILE 4 : NAG.PARAM REMARK 3 PARAMETER FILE 5 : NULL REMARK 3 PARAMETER FILE 6 : NULL REMARK 3 TOPOLOGY FILE 1 : TOPPAR:TOPHCSDX.PRO REMARK 3 TOPOLOGY FILE 2 : TOPPAR:TOPH19.SOL REMARK 3 TOPOLOGY FILE 3 : INH2.TOP REMARK 3 TOPOLOGY FILE 4 : NAG.TOP REMARK 3 TOPOLOGY FILE 5 : SULF.TOP REMARK 3 TOPOLOGY FILE 6 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1DOJ 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 (2007-03-16) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB010249. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-MAR-1998 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) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 126549 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.660 REMARK 200 RESOLUTION RANGE LOW (A) : 99.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 87.1 REMARK 200 DATA REDUNDANCY : 5.000 REMARK 200 R MERGE (I) : 0.04000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 16.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 99.00 REMARK 200 COMPLETENESS FOR SHELL (%) : 87.1 REMARK 200 DATA REDUNDANCY IN SHELL : 3.00 REMARK 200 R MERGE FOR SHELL (I) : 0.20000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.21 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.75 SODIUM ACETATE, 0.01% (W/V), REMARK 280 20% POLYETHYLENE GLYCOL 4000 (W/V), PH 6.5, VAPOR DIFFUSION, REMARK 280 HANGING DROP, TEMPERATURE 295.0K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 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 31.49100 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 58.76050 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.49100 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 58.76050 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 3 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, I 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 14L REMARK 465 ARG A 15 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 THR A 1H OG1 CG2 REMARK 470 PHE A 1G CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASP A 14M CB CG OD1 OD2 REMARK 470 GLU A 247 CG CD OE1 OE2 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 LYS A 169 CB LYS A 169 CG 0.087 REMARK 500 LYS A 169 CB LYS A 169 CG 0.101 REMARK 500 ASP A 243 CB ASP A 243 CG 0.061 REMARK 500 ASP A 243 CB ASP A 243 CG 0.056 REMARK 500 CH3 I 400 C DPN I 401 N 0.164 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 14A N - CA - C ANGL. DEV. = 10.0 DEGREES REMARK 500 LEU A 33 N - CA - C ANGL. DEV. = -8.6 DEGREES REMARK 500 GLY A 43 N - CA - C ANGL. DEV. = -8.1 DEGREES REMARK 500 THR A 60I N - CA - C ANGL. DEV. = -7.8 DEGREES REMARK 500 THR A 74 N - CA - C ANGL. DEV. = 8.2 DEGREES REMARK 500 TYR A 76 N - CA - C ANGL. DEV. =-10.3 DEGREES REMARK 500 GLU A 97A N - CA - C ANGL. DEV. = 7.9 DEGREES REMARK 500 LEU A 123 N - CA - C ANGL. DEV. = -9.4 DEGREES REMARK 500 ASP A 125 N - CA - C ANGL. DEV. = -8.7 DEGREES REMARK 500 LEU A 130C N - CA - C ANGL. DEV. = 7.9 DEGREES REMARK 500 LYS A 169 CB - CA - C ANGL. DEV. = 11.6 DEGREES REMARK 500 LYS A 169 CB - CA - C ANGL. DEV. =-11.3 DEGREES REMARK 500 ALA A 190 N - CA - C ANGL. DEV. = -9.8 DEGREES REMARK 500 PHE A 199 N - CA - C ANGL. DEV. =-13.4 DEGREES REMARK 500 ASP A 243 CB - CA - C ANGL. DEV. =-10.2 DEGREES REMARK 500 ASP A 243 CB - CA - C ANGL. DEV. = 10.7 DEGREES REMARK 500 DPN I 401 C - N - CA ANGL. DEV. =-12.1 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 DPN I 401 -130.86 179.34 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1ABJ RELATED DB: PDB REMARK 900 CONTAINS THE SAME PROTEIN COMPLEXED WITH D-PHE-PRO-ARG REMARK 900 CHLOROMETHYLKETONE (PPACK) WITH CHLOROMETHYLKETONE REPLACED REMARK 900 BY A METHYLENE GROUP DBREF 1DOJ A 1H 247 UNP P00734 THRB_HUMAN 328 622 SEQRES 1 A 295 THR PHE GLY SER GLY GLU ALA ASP CYS GLY LEU ARG PRO SEQRES 2 A 295 LEU PHE GLU LYS LYS SER LEU GLU ASP LYS THR GLU ARG SEQRES 3 A 295 GLU LEU LEU GLU SER TYR ILE ASP GLY ARG ILE VAL GLU SEQRES 4 A 295 GLY SER ASP ALA GLU ILE GLY MET SER PRO TRP GLN VAL SEQRES 5 A 295 MET LEU PHE ARG LYS SER PRO GLN GLU LEU LEU CYS GLY SEQRES 6 A 295 ALA SER LEU ILE SER ASP ARG TRP VAL LEU THR ALA ALA SEQRES 7 A 295 HIS CYS LEU LEU TYR PRO PRO TRP ASP LYS ASN PHE THR SEQRES 8 A 295 GLU ASN ASP LEU LEU VAL ARG ILE GLY LYS HIS SER ARG SEQRES 9 A 295 THR ARG TYR GLU ARG ASN ILE GLU LYS ILE SER MET LEU SEQRES 10 A 295 GLU LYS ILE TYR ILE HIS PRO ARG TYR ASN TRP ARG GLU SEQRES 11 A 295 ASN LEU ASP ARG ASP ILE ALA LEU MET LYS LEU LYS LYS SEQRES 12 A 295 PRO VAL ALA PHE SER ASP TYR ILE HIS PRO VAL CYS LEU SEQRES 13 A 295 PRO ASP ARG GLU THR ALA ALA SER LEU LEU GLN ALA GLY SEQRES 14 A 295 TYR LYS GLY ARG VAL THR GLY TRP GLY ASN LEU LYS GLU SEQRES 15 A 295 THR TRP THR ALA ASN VAL GLY LYS GLY GLN PRO SER VAL SEQRES 16 A 295 LEU GLN VAL VAL ASN LEU PRO ILE VAL GLU ARG PRO VAL SEQRES 17 A 295 CYS LYS ASP SER THR ARG ILE ARG ILE THR ASP ASN MET SEQRES 18 A 295 PHE CYS ALA GLY TYR LYS PRO ASP GLU GLY LYS ARG GLY SEQRES 19 A 295 ASP ALA CYS GLU GLY ASP SER GLY GLY PRO PHE VAL MET SEQRES 20 A 295 LYS SER PRO PHE ASN ASN ARG TRP TYR GLN MET GLY ILE SEQRES 21 A 295 VAL SER TRP GLY GLU GLY CYS ASP ARG ASP GLY LYS TYR SEQRES 22 A 295 GLY PHE TYR THR HIS VAL PHE ARG LEU LYS LYS TRP ILE SEQRES 23 A 295 GLN LYS VAL ILE ASP GLN PHE GLY GLU SEQRES 1 B 11 ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU GLN SEQRES 1 I 4 CH3 DPN PRO AR2 MODRES 1DOJ AR2 I 403 ARG ARGINYL-BENZOTHIAZOLE-6-CARBOXYLIC ACID MODRES 1DOJ TYS B 363 TYR SULFONATED TYROSINE MODRES 1DOJ CH3 I 400 METHYL GROUP MODRES 1DOJ DPN I 401 PHE D-PHENYLALANINE MODRES 1DOJ ASN A 60G ASN GLYCOSYLATION SITE HET TYS B 363 16 HET CH3 I 400 1 HET DPN I 401 11 HET AR2 I 403 23 HET NAG A 250 14 HET NA 300 1 HET NA 301 1 HETNAM TYS SULFONATED TYROSINE HETNAM CH3 METHYL GROUP HETNAM DPN D-PHENYLALANINE HETNAM AR2 ARGINYL-BENZOTHIAZOLE-6-CARBOXYLIC ACID HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM NA SODIUM ION HETSYN NAG NAG FORMUL 2 TYS C9 H11 N O6 S FORMUL 3 CH3 C H4 FORMUL 3 DPN C9 H11 N O2 FORMUL 3 AR2 C14 H17 N5 O3 S FORMUL 4 NAG C8 H15 N O6 FORMUL 5 NA 2(NA 1+) FORMUL 7 HOH *349(H2 O) HELIX 1 1 PHE A 7 SER A 11 5 5 HELIX 2 3 ALA A 55 LEU A 59 1 5 HELIX 3 5 ASP A 125 LEU A 130 1 9 HELIX 4 6 GLU A 164 SER A 171 1 8 HELIX 5 8 VAL A 231 PHE A 245 1 15 SHEET 1 A 7 SER A 20 ASP A 21 0 SHEET 2 A 7 GLN A 156 PRO A 161 -1 N VAL A 157 O SER A 20 SHEET 3 A 7 LYS A 135 GLY A 140 -1 N GLY A 136 O LEU A 160 SHEET 4 A 7 PRO A 198 LYS A 202 -1 O PRO A 198 N THR A 139 SHEET 5 A 7 TRP A 207 TRP A 215 -1 N TYR A 208 O MET A 201 SHEET 6 A 7 GLY A 226 HIS A 230 -1 N PHE A 227 O TRP A 215 SHEET 7 A 7 MET A 180 ALA A 183 -1 O PHE A 181 N TYR A 228 SHEET 1 B 7 GLN A 30 ARG A 35 0 SHEET 2 B 7 GLU A 39 LEU A 46 -1 O GLU A 39 N ARG A 35 SHEET 3 B 7 TRP A 51 THR A 54 -1 N LEU A 53 O SER A 45 SHEET 4 B 7 ALA A 104 LEU A 108 -1 N ALA A 104 O THR A 54 SHEET 5 B 7 LYS A 81 ILE A 90 -1 N GLU A 86 O LYS A 107 SHEET 6 B 7 LEU A 64 ILE A 68 -1 O LEU A 64 N LEU A 85 SHEET 7 B 7 GLN A 30 ARG A 35 -1 O MET A 32 N ARG A 67 SSBOND 1 CYS A 1 CYS A 122 SSBOND 2 CYS A 42 CYS A 58 SSBOND 3 CYS A 168 CYS A 182 SSBOND 4 CYS A 191 CYS A 220 LINK OG SER A 195 C AR2 I 403 LINK ND2 ASN A 60G C1 NAG A 250 CISPEP 1 SER A 36A PRO A 37 0 -0.07 CRYST1 62.982 117.521 47.989 90.00 90.00 90.00 P 21 21 2 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 0.015878 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008509 0.000000 0.00000 SCALE3 0.000000 0.000000 0.020838 0.00000