HEADER BLOOD CLOTTING, HYDROLASE 06-MAR-03 1O3P
TITLE ELABORATE MANIFOLD OF SHORT HYDROGEN BOND ARRAYS MEDIATING BINDING OF
TITLE 2 ACTIVE SITE-DIRECTED SERINE PROTEASE INHIBITORS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UROKINASE-TYPE PLASMINOGEN ACTIVATOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SHORT CHAIN;
COMPND 5 SYNONYM: UPA, U-PLASMINOGEN ACTIVATOR, UROKINASE-PLASMINOGEN
COMPND 6 ACTIVATOR;
COMPND 7 EC: 3.4.21.73;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: UROKINASE-TYPE PLASMINOGEN ACTIVATOR;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: CATALYTIC DOMAIN;
COMPND 13 SYNONYM: UPA, U-PLASMINOGEN ACTIVATOR, UROKINASE-PLASMINOGEN
COMPND 14 ACTIVATOR;
COMPND 15 EC: 3.4.21.73;
COMPND 16 ENGINEERED: YES;
COMPND 17 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PLAU;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPIC9LMWUPA;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: PLAU;
SOURCE 15 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PPIC9LMWUPA
KEYWDS SERINE PROTEASE, SHORT HYDROGEN BOND, INHIBITION MECHANISM, SHIFT OF
KEYWDS 2 PKA, TRYPSIN, THROMBIN, UROKINASE, FACTOR XA, BLOOD CLOTTING,
KEYWDS 3 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.A.KATZ,K.ELROD,E.VERNER,R.L.MACKMAN,C.LUONG,W.D.SHRADER,M.SENDZIK,
AUTHOR 2 J.R.SPENCER,P.A.SPRENGELER,A.KOLESNIKOV,V.W.TAI,H.C.HUI,
AUTHOR 3 J.G.BREITENBUCHER,D.ALLEN,J.W.JANC
REVDAT 5 27-DEC-23 1O3P 1 REMARK
REVDAT 4 27-OCT-21 1O3P 1 REMARK SEQADV
REVDAT 3 04-OCT-17 1O3P 1 REMARK
REVDAT 2 24-FEB-09 1O3P 1 VERSN
REVDAT 1 02-SEP-03 1O3P 0
JRNL AUTH B.A.KATZ,K.ELROD,E.VERNER,R.L.MACKMAN,C.LUONG,W.D.SHRADER,
JRNL AUTH 2 M.SENDZIK,J.R.SPENCER,P.A.SPRENGELER,A.KOLESNIKOV,V.W.TAI,
JRNL AUTH 3 H.C.HUI,J.G.BREITENBUCHER,D.ALLEN,J.W.JANC
JRNL TITL ELABORATE MANIFOLD OF SHORT HYDROGEN BOND ARRAYS MEDIATING
JRNL TITL 2 BINDING OF ACTIVE SITE-DIRECTED SERINE PROTEASE INHIBITORS.
JRNL REF J.MOL.BIOL. V. 329 93 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12742021
JRNL DOI 10.1016/S0022-2836(03)00399-1
REMARK 2
REMARK 2 RESOLUTION. 1.81 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) : 1.81
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.600
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 69.0
REMARK 3 NUMBER OF REFLECTIONS : 15319
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1531
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 : 2004
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 51
REMARK 3 SOLVENT ATOMS : 341
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) : 0.017
REMARK 3 BOND ANGLES (DEGREES) : 4.200
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:
REMARK 3 ONLY LEU_A9 TO LYS_A16 ARE INCLUDED FOR THE A-CHAIN.
REMARK 3 RESIDUES PRIOR AND AFTER THESE RESIDUES ARE NOT VISIBLE
REMARK 3 (DISORDERED).
REMARK 3 RESIDUES AFTER LYS_B243 ARE NOT VISIBLE (DISORDERED).
REMARK 3
REMARK 3 RESIDUES SIMULTANEOUSLY REFINED IN TWO OR MORE CONFORMATIONS ARE:
REMARK 3 LYS_A10, MET_B47, GLU_B84, GLU_B86, LEU_B123, THR_B139,
REMARK 3 GLN_B192, ARG_B217, LEU_B235.
REMARK 3
REMARK 3 HIS_H57 IS DOUBLY PROTONATED.
REMARK 3 HIS_H91 AND HIS_H119 ARE MONOPROTONATED ON THE EPSILON NITROGEN
REMARK 3
REMARK 3 DISORDERED WATERS ARE:
REMARK 3
REMARK 3 HOH382 WHICH IS CLOSE TO CONFORMATION 1 OF ARG_B217;
REMARK 3 HOH582 WHICH IS CLOSE TO A SYMMETRY-RELATED EQUIVALENT OF ITSELF;
REMARK 3 HOH721 WHICH IS CLOSE TO CONFORMATION 1 OF LYS_A10;
REMARK 3 HOH1010 WHICH IS CLOSE TO A SYMMETRY-RELATED EQUIVALENT OF ITSELF;
REMARK 3
REMARK 3 SOME OF THE WATERS MAY CORRESPOND TO THE DISORDERED OR MOBILE
REMARK 3 TERMINI
REMARK 3 OF THE LIGHT CHAIN.
REMARK 3
REMARK 3 NO ENERGY TERMS BETWEEN CITRATE 1 AND 2 ARE INCLUDED BECAUSE THEY
REMARK 3 ARE
REMARK 3 HYDROGEN-BONDED TO ONE ANOTHER VIA AN UNUSUALLY SHORT HYDROGEN BOND
REMARK 3 BETWEEN CARBOXYLATE / HYDROXYL GROUPS.
REMARK 3
REMARK 3 NO ENERGY TERMS ARE INCLUDED AMONG HOH_849, AND OGSER195, AND O6'
REMARK 3 OF THE
REMARK 3 INHIBITOR. THESE ATOMS FORM A VERY SHORT MULTI-CENTERED HYDROGEN-
REMARK 3 BONDING NETWORK.
REMARK 4
REMARK 4 1O3P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAR-03.
REMARK 100 THE DEPOSITION ID IS D_1000001765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-APR-00
REMARK 200 TEMPERATURE (KELVIN) : 298
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 RU200
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 RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : BIOTEX 1.2
REMARK 200 DATA SCALING SOFTWARE : BIOTEX
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15430
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.810
REMARK 200 RESOLUTION RANGE LOW (A) : 41.660
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.800
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 67.2
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.81
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.89
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.21500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: QUANTA
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2-PROPANOL, PEG 4000, PH 6.5, VAPOR
REMARK 280 DIFFUSION AT 298 K, PH 6.50
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 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-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 40.77000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.08500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 40.77000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.08500
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 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 TOTAL BURIED SURFACE AREA: 1530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 KCAL/MOL
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 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 B 582 LIES ON A SPECIAL POSITION.
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 LYS A 1
REMARK 465 PRO A 2
REMARK 465 SER A 3
REMARK 465 SER A 4
REMARK 465 PRO A 5
REMARK 465 PRO A 6
REMARK 465 GLU A 7
REMARK 465 GLU A 8
REMARK 465 THR A 17
REMARK 465 LEU A 18
REMARK 465 ARG A 19
REMARK 465 PRO A 20
REMARK 465 ARG A 21
REMARK 465 PHE A 22
REMARK 465 LYS A 23
REMARK 465 GLU B 244
REMARK 465 GLU B 245
REMARK 465 ASN B 246
REMARK 465 GLY B 247
REMARK 465 LEU B 248
REMARK 465 ALA B 249
REMARK 465 LEU B 250
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 DISTANCE
REMARK 500 H2 HOH B 423 H1 HOH B 564 1.27
REMARK 500 HG SER B 195 O6' 655 B 251 1.27
REMARK 500 HZ1 LYS B 92 HE1 TRP B 237 1.35
REMARK 500 O HOH B 521 H1 HOH B 522 1.42
REMARK 500 OG SER B 195 H1 HOH B 521 1.49
REMARK 500 O TYR B 64 H1 HOH B 476 1.55
REMARK 500 O6' 655 B 251 H2 HOH B 521 1.56
REMARK 500 O HOH B 414 H1 HOH B 536 1.56
REMARK 500 O GLY B 79 H1 HOH B 435 1.56
REMARK 500 O HOH B 261 H1 HOH B 287 1.57
REMARK 500 O HOH B 439 H2 HOH B 531 1.57
REMARK 500 O SER B 75 H1 HOH B 483 1.57
REMARK 500 H2 HOH B 457 O HOH B 482 1.58
REMARK 500 H2 HOH B 345 O HOH B 563 1.58
REMARK 500 OH TYR B 64 H1 HOH B 309 1.59
REMARK 500 H2 HOH B 398 O HOH B 550 1.60
REMARK 500 O7 CIT B 1 O7 CIT B 2 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 H2 HOH B 576 H2 HOH B 576 2555 0.99
REMARK 500 O HOH B 380 H2 HOH B 450 2555 1.60
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 HIS B 37 NE2 HIS B 37 CD2 -0.078
REMARK 500 HIS B 57 NE2 HIS B 57 CD2 -0.070
REMARK 500 HIS B 91 NE2 HIS B 91 CD2 -0.070
REMARK 500 HIS B 99 NE2 HIS B 99 CD2 -0.070
REMARK 500 HIS B 165 NE2 HIS B 165 CD2 -0.068
REMARK 500 HIS B 170B NE2 HIS B 170B CD2 -0.067
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 ARG B 37A N - CA - C ANGL. DEV. = -16.8 DEGREES
REMARK 500 VAL B 38 N - CA - C ANGL. DEV. = -17.4 DEGREES
REMARK 500 ARG B 109 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP B 189 CB - CG - OD1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 LEU B 199 N - CA - C ANGL. DEV. = -18.8 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 GLN B 27 53.95 -146.71
REMARK 500 SER B 54 -151.63 -146.49
REMARK 500 TYR B 60B 67.96 -166.96
REMARK 500 PRO B 60C 45.15 -78.40
REMARK 500 ASP B 93 31.04 103.08
REMARK 500 LEU B 97B -61.79 133.15
REMARK 500 CYS B 111 -166.87 -105.98
REMARK 500 MET B 126 127.44 -31.15
REMARK 500 TYR B 127 35.40 35.41
REMARK 500 LYS B 143 147.85 -39.78
REMARK 500 TYR B 171 -99.07 -126.56
REMARK 500 TRP B 186 46.87 36.27
REMARK 500 ASP B 189 -176.65 -175.27
REMARK 500 SER B 240 -38.96 -37.40
REMARK 500 THR B 242 79.33 -115.33
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 ARG B 70 0.24 SIDE CHAIN
REMARK 500 ARG B 110D 0.11 SIDE CHAIN
REMARK 500 ARG B 206 0.20 SIDE CHAIN
REMARK 500 ARG B 217 0.13 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 655 B 251
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1C5X RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH A DIFFERENT INHIBITOR
DBREF 1O3P A 1 23 UNP P00749 UROK_HUMAN 156 178
DBREF 1O3P B 16 250 UNP P00749 UROK_HUMAN 179 431
SEQADV 1O3P ALA B 145 UNP P00749 ASN 322 ENGINEERED MUTATION
SEQRES 1 A 23 LYS PRO SER SER PRO PRO GLU GLU LEU LYS PHE GLN CYS
SEQRES 2 A 23 GLY GLN LYS THR LEU ARG PRO ARG PHE LYS
SEQRES 1 B 253 ILE ILE GLY GLY GLU PHE THR THR ILE GLU ASN GLN PRO
SEQRES 2 B 253 TRP PHE ALA ALA ILE TYR ARG ARG HIS ARG GLY GLY SER
SEQRES 3 B 253 VAL THR TYR VAL CYS GLY GLY SER LEU MET SER PRO CYS
SEQRES 4 B 253 TRP VAL ILE SER ALA THR HIS CYS PHE ILE ASP TYR PRO
SEQRES 5 B 253 LYS LYS GLU ASP TYR ILE VAL TYR LEU GLY ARG SER ARG
SEQRES 6 B 253 LEU ASN SER ASN THR GLN GLY GLU MET LYS PHE GLU VAL
SEQRES 7 B 253 GLU ASN LEU ILE LEU HIS LYS ASP TYR SER ALA ASP THR
SEQRES 8 B 253 LEU ALA HIS HIS ASN ASP ILE ALA LEU LEU LYS ILE ARG
SEQRES 9 B 253 SER LYS GLU GLY ARG CYS ALA GLN PRO SER ARG THR ILE
SEQRES 10 B 253 GLN THR ILE CYS LEU PRO SER MET TYR ASN ASP PRO GLN
SEQRES 11 B 253 PHE GLY THR SER CYS GLU ILE THR GLY PHE GLY LYS GLU
SEQRES 12 B 253 ALA SER THR ASP TYR LEU TYR PRO GLU GLN LEU LYS MET
SEQRES 13 B 253 THR VAL VAL LYS LEU ILE SER HIS ARG GLU CYS GLN GLN
SEQRES 14 B 253 PRO HIS TYR TYR GLY SER GLU VAL THR THR LYS MET LEU
SEQRES 15 B 253 CYS ALA ALA ASP PRO GLN TRP LYS THR ASP SER CYS GLN
SEQRES 16 B 253 GLY ASP SER GLY GLY PRO LEU VAL CYS SER LEU GLN GLY
SEQRES 17 B 253 ARG MET THR LEU THR GLY ILE VAL SER TRP GLY ARG GLY
SEQRES 18 B 253 CYS ALA LEU LYS ASP LYS PRO GLY VAL TYR THR ARG VAL
SEQRES 19 B 253 SER HIS PHE LEU PRO TRP ILE ARG SER HIS THR LYS GLU
SEQRES 20 B 253 GLU ASN GLY LEU ALA LEU
HET CIT B 1 18
HET CIT B 2 18
HET 655 B 251 45
HETNAM CIT CITRIC ACID
HETNAM 655 2-{5-[AMINO(IMINIO)METHYL]-1H-BENZIMIDAZOL-2-YL}-6-
HETNAM 2 655 (CYCLOPENTYLOXY)BENZENOLATE
HETSYN 655 CRA_10655
FORMUL 3 CIT 2(C6 H8 O7)
FORMUL 5 655 C19 H20 N4 O2
FORMUL 6 HOH *341(H2 O)
HELIX 1 1 THR B 23 GLN B 27 5 5
HELIX 2 2 ALA B 55 PHE B 59 5 5
HELIX 3 3 LYS B 61 GLU B 62A 5 3
HELIX 4 4 SER B 164 GLN B 169 1 6
HELIX 5 5 TYR B 172 VAL B 176 5 5
HELIX 6 6 PHE B 234 THR B 242 1 9
SHEET 1 A 8 GLU B 20 PHE B 21 0
SHEET 2 A 8 LYS B 156 LEU B 162 -1 O MET B 157 N GLU B 20
SHEET 3 A 8 MET B 180 ALA B 184 -1 O ALA B 184 N LYS B 161
SHEET 4 A 8 GLY B 226 ARG B 230 -1 N GLY B 226 O ALA B 183
SHEET 5 A 8 ARG B 206 TRP B 215 -1 O ILE B 212 N THR B 229
SHEET 6 A 8 PRO B 198 LEU B 203 -1 O LEU B 199 N THR B 210
SHEET 7 A 8 SER B 135 GLY B 140 -1 O GLU B 137 N VAL B 200
SHEET 8 A 8 LYS B 156 LEU B 162 -1 N LYS B 156 O GLY B 140
SHEET 1 B 7 PHE B 30 ARG B 36 0
SHEET 2 B 7 VAL B 38 SER B 48 -1 N THR B 39 O ARG B 35
SHEET 3 B 7 TRP B 51 SER B 54 -1 O TRP B 51 N MET B 47
SHEET 4 B 7 ALA B 104 ARG B 109 -1 O ALA B 104 N SER B 54
SHEET 5 B 7 MET B 81 ILE B 89 -1 N GLU B 84 O ARG B 109
SHEET 6 B 7 TYR B 64 LEU B 68 -1 O TYR B 64 N VAL B 85
SHEET 7 B 7 PHE B 30 ARG B 36 -1 O ALA B 32 N TYR B 67
SHEET 1 C 2 SER B 95 ALA B 96 0
SHEET 2 C 2 HIS B 99 HIS B 100 -1 N HIS B 100 O SER B 95
SSBOND 1 CYS A 13 CYS B 122 1555 1555 2.03
SSBOND 2 CYS B 42 CYS B 58 1555 1555 2.03
SSBOND 3 CYS B 50 CYS B 111 1555 1555 2.03
SSBOND 4 CYS B 136 CYS B 201 1555 1555 2.01
SSBOND 5 CYS B 168 CYS B 182 1555 1555 2.01
SSBOND 6 CYS B 191 CYS B 220 1555 1555 2.02
SITE 1 AC1 9 CIT B 2 TYR B 67 ASN B 76 GLU B 80
SITE 2 AC1 9 LYS B 82 SER B 164 HIS B 165 ARG B 166
SITE 3 AC1 9 HOH B 498
SITE 1 AC2 8 CIT B 1 ARG B 36 LYS B 82 LYS B 110A
SITE 2 AC2 8 HIS B 165 ARG B 230 HOH B 276 HOH B 382
SITE 1 AC3 14 HIS B 57 CYS B 58 GLN B 185B SER B 190
SITE 2 AC3 14 CYS B 191 GLN B 192 SER B 195 VAL B 213
SITE 3 AC3 14 TRP B 215 GLY B 219 HOH B 419 HOH B 464
SITE 4 AC3 14 HOH B 521 HOH B 534
CRYST1 81.540 50.170 66.440 90.00 113.49 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 0.012264 0.000000 0.005330 0.00000
SCALE2 0.000000 0.019932 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016411 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
