HEADER HYDROLASE/HYDROLASE INHIBITOR 30-NOV-97 1A0H
TITLE THE X-RAY CRYSTAL STRUCTURE OF PPACK-MEIZOTHROMBIN DESF1:
TITLE 2 KRINGLE/THROMBIN AND CARBOHYDRATE/KRINGLE/THROMBIN INTERACTIONS AND
TITLE 3 LOCATION OF THE LINKER CHAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MEIZOTHROMBIN;
COMPND 3 CHAIN: A, D;
COMPND 4 FRAGMENT: F2/THROMBIN DOMAIN;
COMPND 5 SYNONYM: DESF1;
COMPND 6 EC: 3.4.21.5;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: MEIZOTHROMBIN;
COMPND 9 CHAIN: B, E;
COMPND 10 FRAGMENT: F2/THROMBIN DOMAIN;
COMPND 11 SYNONYM: DESF1;
COMPND 12 EC: 3.4.21.5
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 ORGAN: BLOOD;
SOURCE 6 TISSUE: BLOOD PLASMA;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 9 ORGANISM_COMMON: CATTLE;
SOURCE 10 ORGANISM_TAXID: 9913;
SOURCE 11 ORGAN: BLOOD;
SOURCE 12 TISSUE: BLOOD PLASMA
KEYWDS SERINE PROTEASE, COAGULATION, THROMBIN, PROTHROMBIN, MEIZOTHROMBIN,
KEYWDS 2 HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.D.MARTIN,M.G.MALKOWSKI,J.BOX,C.T.ESMON,B.F.P.EDWARDS
REVDAT 6 03-APR-24 1A0H 1 HETSYN
REVDAT 5 29-JUL-20 1A0H 1 COMPND REMARK SEQADV HETNAM
REVDAT 5 2 1 LINK SITE ATOM
REVDAT 4 16-NOV-11 1A0H 1 HETATM
REVDAT 3 13-JUL-11 1A0H 1 VERSN
REVDAT 2 24-FEB-09 1A0H 1 VERSN
REVDAT 1 17-JUN-98 1A0H 0
JRNL AUTH P.D.MARTIN,M.G.MALKOWSKI,J.BOX,C.T.ESMON,B.F.EDWARDS
JRNL TITL NEW INSIGHTS INTO THE REGULATION OF THE BLOOD CLOTTING
JRNL TITL 2 CASCADE DERIVED FROM THE X-RAY CRYSTAL STRUCTURE OF BOVINE
JRNL TITL 3 MEIZOTHROMBIN DES F1 IN COMPLEX WITH PPACK.
JRNL REF STRUCTURE V. 5 1681 1997
JRNL REFN ISSN 0969-2126
JRNL PMID 9438869
JRNL DOI 10.1016/S0969-2126(97)00314-6
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.84
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 99999999.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0001
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.0
REMARK 3 NUMBER OF REFLECTIONS : 30519
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) : 0.205
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
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 : 6698
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 116
REMARK 3 SOLVENT ATOMS : 87
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 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 1A0H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170239.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : MAR-96
REMARK 200 TEMPERATURE (KELVIN) : 273
REMARK 200 PH : 8.0
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 RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE(002)
REMARK 200 OPTICS : 0.3 MM COLLIMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SCALEK, XENGEN
REMARK 200 DATA SCALING SOFTWARE : SCALEK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31648
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 42.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : 0.12000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 60.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.19000
REMARK 200 R SYM FOR SHELL (I) : 0.19000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.84
REMARK 200 STARTING MODEL: THROMBIN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 76.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17 MG/ML PROTEIN, 2% PEG4000, .25 M
REMARK 280 AMMONIUM PHOSPHATE, PH 8.0, 33% SATURATED AMMONIUM SULFATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 60.14500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 93.07500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 93.07500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 30.07250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 93.07500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 93.07500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 90.21750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 93.07500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 93.07500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 30.07250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 93.07500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 93.07500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 90.21750
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 60.14500
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, E, C, F
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 24 LIES ON A SPECIAL POSITION.
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 O HOH B 78 O HOH E 40 3545 0.44
REMARK 500
REMARK 500 REMARK: NULL
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),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ILE A 317 CA ILE A 317 CB 0.362
REMARK 500 ILE A 317 CA ILE A 317 C 0.172
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 182 CB - CG - CD1 ANGL. DEV. = 14.5 DEGREES
REMARK 500 LEU A 182 CB - CG - CD2 ANGL. DEV. = -16.1 DEGREES
REMARK 500 CYS A 231 CA - CB - SG ANGL. DEV. = 7.5 DEGREES
REMARK 500 PRO A 297 C - N - CA ANGL. DEV. = 11.6 DEGREES
REMARK 500 LEU D 182 CB - CG - CD1 ANGL. DEV. = -11.9 DEGREES
REMARK 500 PRO D 264 C - N - CA ANGL. DEV. = 12.1 DEGREES
REMARK 500 CYS E 507 CA - CB - SG ANGL. DEV. = 7.7 DEGREES
REMARK 500 TYR E 535 N - CA - C ANGL. DEV. = -16.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 LEU A 166 37.37 -84.14
REMARK 500 ASP A 173 47.87 27.47
REMARK 500 GLU A 177 20.62 -72.35
REMARK 500 ARG A 190 -130.38 -57.46
REMARK 500 CYS A 191 146.99 179.39
REMARK 500 ALA A 193 109.65 -59.90
REMARK 500 LYS A 204 59.91 -66.48
REMARK 500 ASP A 205 -31.48 174.62
REMARK 500 GLN A 206 -162.79 -74.50
REMARK 500 PRO A 210 -102.43 -60.04
REMARK 500 ALA A 211 -69.17 72.31
REMARK 500 LEU A 214 65.69 -101.93
REMARK 500 GLU A 216 -95.54 46.78
REMARK 500 ASN A 217 24.11 -140.78
REMARK 500 CYS A 219 130.54 -38.94
REMARK 500 ALA A 234 -150.08 -145.46
REMARK 500 ASN A 246 62.16 74.48
REMARK 500 CYS A 248 -79.59 -68.13
REMARK 500 ASP A 255 88.77 -46.64
REMARK 500 LEU A 256 -105.85 56.31
REMARK 500 LEU A 260 -78.95 -43.13
REMARK 500 GLU A 262 95.39 -54.94
REMARK 500 PRO A 264 148.91 -19.26
REMARK 500 ILE A 268 110.64 83.13
REMARK 500 GLU A 269 -83.67 -73.26
REMARK 500 ASP A 275 -79.08 -74.75
REMARK 500 HIS A 276 16.87 -154.08
REMARK 500 PHE A 277 -68.92 -135.51
REMARK 500 GLN A 278 108.74 83.42
REMARK 500 PHE A 280 14.37 -141.76
REMARK 500 ASN A 282 -23.26 76.11
REMARK 500 GLU A 283 -48.34 72.50
REMARK 500 ALA A 291 -38.08 -31.85
REMARK 500 PHE A 299 -90.34 -133.67
REMARK 500 GLN A 303 39.10 35.17
REMARK 500 GLN A 307 -54.90 -16.34
REMARK 500 TYR A 316 -72.85 -42.30
REMARK 500 GLU A 318 155.01 90.98
REMARK 500 LEU B 331 -89.70 -48.51
REMARK 500 CYS B 348 -157.99 -153.55
REMARK 500 TYR B 367 80.45 -151.09
REMARK 500 ASN B 373 75.83 -168.98
REMARK 500 HIS B 386 -73.30 -142.33
REMARK 500 ARG B 388 11.11 -65.83
REMARK 500 ARG B 390 107.29 114.05
REMARK 500 ARG B 393 -38.99 -20.71
REMARK 500 LYS B 394 -66.65 -92.00
REMARK 500 LYS B 397 73.53 -159.01
REMARK 500 ASP B 402 -56.56 -138.03
REMARK 500 LYS B 403 -65.31 -90.84
REMARK 500
REMARK 500 THIS ENTRY HAS 147 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR E 540 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 THE UNBOUND FORM OF THE INHIBITOR IS D-PHE-PRO-ARG-
REMARK 600 CHLOROMETHYLKETONE. UPON REACTION WITH PROTEIN IT FORMS TWO
REMARK 600 COVALENT BONDS: 1) A COVALENT BOND TO SER525 (CHAINS B,E) FORMING A
REMARK 600 HEMIKETAL AR7 AND 2) A COVALENT BOND TO NE2 OF HIS363 (CHAINS B,E)
REMARK 630
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE INHIBITOR
REMARK 630 MOLECULE NAME: D-PHENYLALANYL-N-[(2S,3S)-6-{[AMINO(IMINIO)METHYL]
REMARK 630 AMINO}-1-CHLORO-2-HYDROXYHEXAN-3-YL]-L-PROLINAMIDE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 0G6 B 1
REMARK 630 0G6 E 1
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: DPN PRO AR7 0QE
REMARK 630 DETAILS: NULL
DBREF 1A0H A 164 320 UNP P00735 THRB_BOVIN 208 366
DBREF 1A0H B 321 579 UNP P00735 THRB_BOVIN 367 625
DBREF 1A0H D 164 320 UNP P00735 THRB_BOVIN 208 366
DBREF 1A0H E 321 579 UNP P00735 THRB_BOVIN 367 625
SEQADV 1A0H HIS A 187 UNP P00735 SER 231 CONFLICT
SEQADV 1A0H HIS D 187 UNP P00735 SER 231 CONFLICT
SEQRES 1 A 159 SER PRO LEU LEU GLU THR CYS VAL PRO ASP ARG GLY ARG
SEQRES 2 A 159 GLU TYR ARG GLY ARG LEU ALA VAL THR THR HIS GLY SER
SEQRES 3 A 159 ARG CYS LEU ALA TRP SER SER GLU GLN ALA LYS ALA LEU
SEQRES 4 A 159 SER LYS ASP GLN ASP PHE ASN PRO ALA VAL PRO LEU ALA
SEQRES 5 A 159 GLU ASN PHE CYS ARG ASN PRO ASP GLY ASP GLU GLU GLY
SEQRES 6 A 159 ALA TRP CYS TYR VAL ALA ASP GLN PRO GLY ASP PHE GLU
SEQRES 7 A 159 TYR CYS ASP LEU ASN TYR CYS GLU GLU PRO VAL ASP GLY
SEQRES 8 A 159 ASP LEU GLY ASP ARG LEU GLY GLU ASP PRO ASP PRO ASP
SEQRES 9 A 159 ALA ALA ILE GLU GLY ARG THR SER GLU ASP HIS PHE GLN
SEQRES 10 A 159 PRO PHE PHE ASN GLU LYS THR PHE GLY ALA GLY GLU ALA
SEQRES 11 A 159 ASP CYS GLY LEU ARG PRO LEU PHE GLU LYS LYS GLN VAL
SEQRES 12 A 159 GLN ASP GLN THR GLU LYS GLU LEU PHE GLU SER TYR ILE
SEQRES 13 A 159 GLU GLY ARG
SEQRES 1 B 259 ILE VAL GLU GLY GLN ASP ALA GLU VAL GLY LEU SER PRO
SEQRES 2 B 259 TRP GLN VAL MET LEU PHE ARG LYS SER PRO GLN GLU LEU
SEQRES 3 B 259 LEU CYS GLY ALA SER LEU ILE SER ASP ARG TRP VAL LEU
SEQRES 4 B 259 THR ALA ALA HIS CYS LEU LEU TYR PRO PRO TRP ASP LYS
SEQRES 5 B 259 ASN PHE THR VAL ASP ASP LEU LEU VAL ARG ILE GLY LYS
SEQRES 6 B 259 HIS SER ARG THR ARG TYR GLU ARG LYS VAL GLU LYS ILE
SEQRES 7 B 259 SER MET LEU ASP LYS ILE TYR ILE HIS PRO ARG TYR ASN
SEQRES 8 B 259 TRP LYS GLU ASN LEU ASP ARG ASP ILE ALA LEU LEU LYS
SEQRES 9 B 259 LEU LYS ARG PRO ILE GLU LEU SER ASP TYR ILE HIS PRO
SEQRES 10 B 259 VAL CYS LEU PRO ASP LYS GLN THR ALA ALA LYS LEU LEU
SEQRES 11 B 259 HIS ALA GLY PHE LYS GLY ARG VAL THR GLY TRP GLY ASN
SEQRES 12 B 259 ARG ARG GLU THR TRP THR THR SER VAL ALA GLU VAL GLN
SEQRES 13 B 259 PRO SER VAL LEU GLN VAL VAL ASN LEU PRO LEU VAL GLU
SEQRES 14 B 259 ARG PRO VAL CYS LYS ALA SER THR ARG ILE ARG ILE THR
SEQRES 15 B 259 ASP ASN MET PHE CYS ALA GLY TYR LYS PRO GLY GLU GLY
SEQRES 16 B 259 LYS ARG GLY ASP ALA CYS GLU GLY ASP SER GLY GLY PRO
SEQRES 17 B 259 PHE VAL MET LYS SER PRO TYR ASN ASN ARG TRP TYR GLN
SEQRES 18 B 259 MET GLY ILE VAL SER TRP GLY GLU GLY CYS ASP ARG ASP
SEQRES 19 B 259 GLY LYS TYR GLY PHE TYR THR HIS VAL PHE ARG LEU LYS
SEQRES 20 B 259 LYS TRP ILE GLN LYS VAL ILE ASP ARG LEU GLY SER
SEQRES 1 D 159 SER PRO LEU LEU GLU THR CYS VAL PRO ASP ARG GLY ARG
SEQRES 2 D 159 GLU TYR ARG GLY ARG LEU ALA VAL THR THR HIS GLY SER
SEQRES 3 D 159 ARG CYS LEU ALA TRP SER SER GLU GLN ALA LYS ALA LEU
SEQRES 4 D 159 SER LYS ASP GLN ASP PHE ASN PRO ALA VAL PRO LEU ALA
SEQRES 5 D 159 GLU ASN PHE CYS ARG ASN PRO ASP GLY ASP GLU GLU GLY
SEQRES 6 D 159 ALA TRP CYS TYR VAL ALA ASP GLN PRO GLY ASP PHE GLU
SEQRES 7 D 159 TYR CYS ASP LEU ASN TYR CYS GLU GLU PRO VAL ASP GLY
SEQRES 8 D 159 ASP LEU GLY ASP ARG LEU GLY GLU ASP PRO ASP PRO ASP
SEQRES 9 D 159 ALA ALA ILE GLU GLY ARG THR SER GLU ASP HIS PHE GLN
SEQRES 10 D 159 PRO PHE PHE ASN GLU LYS THR PHE GLY ALA GLY GLU ALA
SEQRES 11 D 159 ASP CYS GLY LEU ARG PRO LEU PHE GLU LYS LYS GLN VAL
SEQRES 12 D 159 GLN ASP GLN THR GLU LYS GLU LEU PHE GLU SER TYR ILE
SEQRES 13 D 159 GLU GLY ARG
SEQRES 1 E 259 ILE VAL GLU GLY GLN ASP ALA GLU VAL GLY LEU SER PRO
SEQRES 2 E 259 TRP GLN VAL MET LEU PHE ARG LYS SER PRO GLN GLU LEU
SEQRES 3 E 259 LEU CYS GLY ALA SER LEU ILE SER ASP ARG TRP VAL LEU
SEQRES 4 E 259 THR ALA ALA HIS CYS LEU LEU TYR PRO PRO TRP ASP LYS
SEQRES 5 E 259 ASN PHE THR VAL ASP ASP LEU LEU VAL ARG ILE GLY LYS
SEQRES 6 E 259 HIS SER ARG THR ARG TYR GLU ARG LYS VAL GLU LYS ILE
SEQRES 7 E 259 SER MET LEU ASP LYS ILE TYR ILE HIS PRO ARG TYR ASN
SEQRES 8 E 259 TRP LYS GLU ASN LEU ASP ARG ASP ILE ALA LEU LEU LYS
SEQRES 9 E 259 LEU LYS ARG PRO ILE GLU LEU SER ASP TYR ILE HIS PRO
SEQRES 10 E 259 VAL CYS LEU PRO ASP LYS GLN THR ALA ALA LYS LEU LEU
SEQRES 11 E 259 HIS ALA GLY PHE LYS GLY ARG VAL THR GLY TRP GLY ASN
SEQRES 12 E 259 ARG ARG GLU THR TRP THR THR SER VAL ALA GLU VAL GLN
SEQRES 13 E 259 PRO SER VAL LEU GLN VAL VAL ASN LEU PRO LEU VAL GLU
SEQRES 14 E 259 ARG PRO VAL CYS LYS ALA SER THR ARG ILE ARG ILE THR
SEQRES 15 E 259 ASP ASN MET PHE CYS ALA GLY TYR LYS PRO GLY GLU GLY
SEQRES 16 E 259 LYS ARG GLY ASP ALA CYS GLU GLY ASP SER GLY GLY PRO
SEQRES 17 E 259 PHE VAL MET LYS SER PRO TYR ASN ASN ARG TRP TYR GLN
SEQRES 18 E 259 MET GLY ILE VAL SER TRP GLY GLU GLY CYS ASP ARG ASP
SEQRES 19 E 259 GLY LYS TYR GLY PHE TYR THR HIS VAL PHE ARG LEU LYS
SEQRES 20 E 259 LYS TRP ILE GLN LYS VAL ILE ASP ARG LEU GLY SER
MODRES 1A0H ASN B 373 ASN GLYCOSYLATION SITE
MODRES 1A0H ASN E 373 ASN GLYCOSYLATION SITE
HET NAG C 1 14
HET NAG C 2 14
HET NAG F 1 14
HET NAG F 2 14
HET 0G6 B 1 30
HET 0G6 E 1 30
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM 0G6 D-PHENYLALANYL-N-[(2S,3S)-6-{[AMINO(IMINIO)
HETNAM 2 0G6 METHYL]AMINO}-1-CHLORO-2-HYDROXYHEXAN-3-YL]-L-
HETNAM 3 0G6 PROLINAMIDE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN 0G6 PPACK
FORMUL 5 NAG 4(C8 H15 N O6)
FORMUL 7 0G6 2(C21 H34 CL N6 O3 1+)
FORMUL 9 HOH *87(H2 O)
HELIX 1 1 ASP A 173 GLY A 175 5 3
HELIX 2 2 ALA A 199 LEU A 202 1 4
HELIX 3 3 GLU A 290 ASP A 292 5 3
HELIX 4 4 GLU A 309 TYR A 316 1 8
HELIX 5 5 ALA B 362 CYS B 364 5 3
HELIX 6 6 PRO B 368 TRP B 370 5 3
HELIX 7 7 VAL B 376 ASP B 378 5 3
HELIX 8 8 LYS B 443 LEU B 449 1 7
HELIX 9 9 VAL B 472 VAL B 475 5 4
HELIX 10 10 ARG B 490 SER B 496 1 7
HELIX 11 11 TYR B 535 ASN B 537 5 3
HELIX 12 12 VAL B 563 ARG B 576 1 14
HELIX 13 13 ASP D 173 GLY D 175 5 3
HELIX 14 14 GLU D 197 SER D 203 1 7
HELIX 15 15 LEU D 256 ARG D 259 5 4
HELIX 16 16 GLU D 290 ASP D 292 5 3
HELIX 17 17 GLU D 300 LYS D 302 5 3
HELIX 18 18 GLU D 309 ILE D 317 1 9
HELIX 19 19 ALA E 362 CYS E 364 5 3
HELIX 20 20 PRO E 368 TRP E 370 5 3
HELIX 21 21 VAL E 376 ASP E 378 5 3
HELIX 22 22 LYS E 443 LEU E 449 1 7
HELIX 23 23 VAL E 472 VAL E 475 5 4
HELIX 24 24 ARG E 490 SER E 496 1 7
HELIX 25 25 VAL E 563 ARG E 576 5 14
SHEET 1 A 2 TRP A 230 TYR A 232 0
SHEET 2 A 2 PHE A 240 TYR A 242 -1 N GLU A 241 O CYS A 231
SHEET 1 B 4 LYS B 397 MET B 400 0
SHEET 2 B 4 LEU B 379 ILE B 383 -1 N ILE B 383 O LYS B 397
SHEET 3 B 4 GLN B 335 ARG B 340 -1 N PHE B 339 O LEU B 380
SHEET 4 B 4 GLU B 345 SER B 351 -1 N ALA B 350 O VAL B 336
SHEET 1 C 2 LYS B 455 THR B 459 0
SHEET 2 C 2 VAL B 482 PRO B 486 -1 N LEU B 485 O GLY B 456
SHEET 1 D 4 MET B 505 ALA B 508 0
SHEET 2 D 4 GLY B 558 HIS B 562 -1 N TYR B 560 O PHE B 506
SHEET 3 D 4 TRP B 539 TRP B 547 -1 N TRP B 547 O PHE B 559
SHEET 4 D 4 PRO B 528 LYS B 532 -1 N MET B 531 O TYR B 540
SHEET 1 E 2 TRP D 230 TYR D 232 0
SHEET 2 E 2 PHE D 240 TYR D 242 -1 N GLU D 241 O CYS D 231
SHEET 1 F 4 LYS E 397 SER E 399 0
SHEET 2 F 4 LEU E 379 ILE E 383 -1 N ILE E 383 O LYS E 397
SHEET 3 F 4 VAL E 336 ARG E 340 -1 N PHE E 339 O LEU E 380
SHEET 4 F 4 GLU E 345 CYS E 348 -1 N CYS E 348 O LEU E 338
SHEET 1 G 2 TRP E 357 THR E 360 0
SHEET 2 G 2 ALA E 421 LYS E 424 -1 N LEU E 423 O VAL E 358
SHEET 1 H 2 LYS E 455 THR E 459 0
SHEET 2 H 2 VAL E 482 PRO E 486 -1 N LEU E 485 O GLY E 456
SHEET 1 I 4 MET E 505 ALA E 508 0
SHEET 2 I 4 GLY E 558 THR E 561 -1 N TYR E 560 O PHE E 506
SHEET 3 I 4 TRP E 539 TRP E 547 -1 N TRP E 547 O PHE E 559
SHEET 4 I 4 PRO E 528 LYS E 532 -1 N MET E 531 O TYR E 540
SSBOND 1 CYS A 170 CYS A 248 1555 1555 2.03
SSBOND 2 CYS A 191 CYS A 231 1555 1555 2.03
SSBOND 3 CYS A 219 CYS A 243 1555 1555 2.04
SSBOND 4 CYS A 293 CYS B 439 1555 1555 2.01
SSBOND 5 CYS B 348 CYS B 364 1555 1555 2.01
SSBOND 6 CYS B 493 CYS B 507 1555 1555 2.05
SSBOND 7 CYS B 521 CYS B 551 1555 1555 2.02
SSBOND 8 CYS D 170 CYS D 248 1555 1555 2.02
SSBOND 9 CYS D 191 CYS D 231 1555 1555 2.01
SSBOND 10 CYS D 219 CYS D 243 1555 1555 2.04
SSBOND 11 CYS D 293 CYS E 439 1555 1555 2.04
SSBOND 12 CYS E 348 CYS E 364 1555 1555 2.02
SSBOND 13 CYS E 493 CYS E 507 1555 1555 2.02
SSBOND 14 CYS E 521 CYS E 551 1555 1555 2.03
LINK C3 0G6 B 1 NE2 HIS B 363 1555 1555 1.46
LINK C2 0G6 B 1 OG SER B 525 1555 1555 1.40
LINK ND2 ASN B 373 C1 NAG C 1 1555 1555 1.45
LINK C3 0G6 E 1 NE2 HIS E 363 1555 1555 1.46
LINK C2 0G6 E 1 OG SER E 525 1555 1555 1.38
LINK ND2 ASN E 373 C1 NAG F 1 1555 1555 1.45
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.39
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.38
CISPEP 1 SER B 342 PRO B 343 0 1.38
CISPEP 2 SER E 342 PRO E 343 0 0.78
CRYST1 186.150 186.150 120.290 90.00 90.00 90.00 P 41 21 2 16
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 0.005372 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005372 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008313 0.00000
MTRIX1 1 -0.900240 -0.435360 -0.005550 178.65675 1
MTRIX2 1 -0.433810 0.897970 -0.073910 42.02666 1
MTRIX3 1 0.037160 -0.064130 -0.997250 32.13877 1
(ATOM LINES ARE NOT SHOWN.)
END
