HEADER HYDROLASE 09-MAY-05 1ZLR
TITLE FACTOR XI CATALYTIC DOMAIN COMPLEXED WITH 2-GUANIDINO-1-(4-(4,4,5,5-
TITLE 2 TETRAMETHYL-1,3,2-DIOXABOROLAN-2-YL)PHENYL)ETHYL NICOTINATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COAGULATION FACTOR XI;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 SYNONYM: PLASMA THROMBOPLASTIN ANTECEDENT, PTA, FXI;
COMPND 6 EC: 3.4.21.27;
COMPND 7 ENGINEERED: YES;
COMPND 8 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: F11;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: X-33;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPICZALPHAA
KEYWDS SERINE PROTEASE, BORON, COVALENT INHIBITOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.I.LAZAROVA,L.JIN,M.RYNKIEWICZ,J.C.GORGA,F.BIBBINS,H.V.MEYERS,
AUTHOR 2 R.BABINE,J.STRICKLER
REVDAT 6 23-AUG-23 1ZLR 1 REMARK
REVDAT 5 20-OCT-21 1ZLR 1 REMARK SEQADV LINK
REVDAT 4 13-JUL-11 1ZLR 1 VERSN
REVDAT 3 24-FEB-09 1ZLR 1 VERSN
REVDAT 2 05-SEP-06 1ZLR 1 JRNL
REVDAT 1 09-MAY-06 1ZLR 0
JRNL AUTH T.I.LAZAROVA,L.JIN,M.RYNKIEWICZ,J.C.GORGA,F.BIBBINS,
JRNL AUTH 2 H.V.MEYERS,R.BABINE,J.STRICKLER
JRNL TITL SYNTHESIS AND IN VITRO BIOLOGICAL EVALUATION OF ARYL BORONIC
JRNL TITL 2 ACIDS AS POTENTIAL INHIBITORS OF FACTOR XIA.
JRNL REF BIOORG.MED.CHEM.LETT. V. 16 5022 2006
JRNL REFN ISSN 0960-894X
JRNL PMID 16876411
JRNL DOI 10.1016/J.BMCL.2006.07.043
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX 2002
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,ACCELRYS
REMARK 3 : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2106346.450
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 10323
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) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.100
REMARK 3 FREE R VALUE TEST SET COUNT : 735
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 10349
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1552
REMARK 3 BIN R VALUE (WORKING SET) : 0.2350
REMARK 3 BIN FREE R VALUE : 0.2860
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 122
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.026
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1874
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 49
REMARK 3 SOLVENT ATOMS : 101
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.25
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) : 0.33
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.29
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.650
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) : 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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 34.64
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 : PROTEIN_REP.P
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PAR
REMARK 3 PARAMETER FILE 4 : CARBOHYDRATE.
REMARK 3 PARAMETER FILE 5 : 368.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 4 : CARBOHYDRATE.
REMARK 3 TOPOLOGY FILE 5 : 368.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZLR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000032867.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-OCT-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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 RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10323
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.30400
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: CNX 2002
REMARK 200 STARTING MODEL: PDB ENTRY 1ZHR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 M AMMONIUM SULFATE, 0.1 M TRIS, PH
REMARK 280 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 283K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 15555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 16555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z+1/2,-X+1/2,-Y+1/2
REMARK 290 19555 -Z+1/2,-X+1/2,Y+1/2
REMARK 290 20555 -Z+1/2,X+1/2,-Y+1/2
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z+1/2,-X+1/2
REMARK 290 23555 Y+1/2,-Z+1/2,-X+1/2
REMARK 290 24555 -Y+1/2,-Z+1/2,X+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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 60.50050
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 60.50050
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 60.50050
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 60.50050
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 60.50050
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 60.50050
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 60.50050
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 60.50050
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 60.50050
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 60.50050
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 60.50050
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 60.50050
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 60.50050
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 60.50050
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 60.50050
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 60.50050
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 60.50050
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 60.50050
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 60.50050
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 60.50050
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 60.50050
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 60.50050
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 60.50050
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 60.50050
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 60.50050
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 60.50050
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 60.50050
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 60.50050
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 60.50050
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 60.50050
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 60.50050
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 60.50050
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 60.50050
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 60.50050
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 60.50050
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 60.50050
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: MONOMERIC
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 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 198A N - CA - C ANGL. DEV. = -17.3 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 72 -61.57 -109.49
REMARK 500 ARG A 147 56.56 38.63
REMARK 500 ASP A 148 -133.01 -118.64
REMARK 500 GLU A 202C 7.00 59.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 THE PINACOL ESTER GROUP ORIGINALLY ATTACHED TO THE
REMARK 600 BORON ATOM OF LIGAND 368 WAS REPLACED BY GLYCEROL DURING
REMARK 600 CRYSTALLIZATION, LEADING TO THE DIFFERENCE BETWEEN THE
REMARK 600 LIGAND NAME IN THE TITLE AND THE LIGAND STRUCTURE.
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 368 A 901
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 368 A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 900
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZHR RELATED DB: PDB
REMARK 900 FACTOR XI CATALYTIC DOMAIN COMPLEXED WITH BENZAMIDINE
DBREF 1ZLR A 16 244 UNP P03951 FA11_HUMAN 388 624
SEQADV 1ZLR ALA A 75 UNP P03951 SER 452 ENGINEERED MUTATION
SEQADV 1ZLR ALA A 78 UNP P03951 LYS 455 ENGINEERED MUTATION
SEQADV 1ZLR ALA A 115 UNP P03951 THR 493 ENGINEERED MUTATION
SEQADV 1ZLR SER A 123 UNP P03951 CYS 500 ENGINEERED MUTATION
SEQRES 1 A 237 ILE VAL GLY GLY THR ALA SER VAL ARG GLY GLU TRP PRO
SEQRES 2 A 237 TRP GLN VAL THR LEU HIS THR THR SER PRO THR GLN ARG
SEQRES 3 A 237 HIS LEU CYS GLY GLY SER ILE ILE GLY ASN GLN TRP ILE
SEQRES 4 A 237 LEU THR ALA ALA HIS CYS PHE TYR GLY VAL GLU SER PRO
SEQRES 5 A 237 LYS ILE LEU ARG VAL TYR SER GLY ILE LEU ASN GLN ALA
SEQRES 6 A 237 GLU ILE ALA GLU ASP THR SER PHE PHE GLY VAL GLN GLU
SEQRES 7 A 237 ILE ILE ILE HIS ASP GLN TYR LYS MET ALA GLU SER GLY
SEQRES 8 A 237 TYR ASP ILE ALA LEU LEU LYS LEU GLU THR THR VAL ASN
SEQRES 9 A 237 TYR ALA ASP SER GLN ARG PRO ILE SER LEU PRO SER LYS
SEQRES 10 A 237 GLY ASP ARG ASN VAL ILE TYR THR ASP CYS TRP VAL THR
SEQRES 11 A 237 GLY TRP GLY TYR ARG LYS LEU ARG ASP LYS ILE GLN ASN
SEQRES 12 A 237 THR LEU GLN LYS ALA LYS ILE PRO LEU VAL THR ASN GLU
SEQRES 13 A 237 GLU CYS GLN LYS ARG TYR ARG GLY HIS LYS ILE THR HIS
SEQRES 14 A 237 LYS MET ILE CYS ALA GLY TYR ARG GLU GLY GLY LYS ASP
SEQRES 15 A 237 ALA CYS LYS GLY ASP SER GLY GLY PRO LEU SER CYS LYS
SEQRES 16 A 237 HIS ASN GLU VAL TRP HIS LEU VAL GLY ILE THR SER TRP
SEQRES 17 A 237 GLY GLU GLY CYS ALA GLN ARG GLU ARG PRO GLY VAL TYR
SEQRES 18 A 237 THR ASN VAL VAL GLU TYR VAL ASP TRP ILE LEU GLU LYS
SEQRES 19 A 237 THR GLN ALA
HET SO4 A1001 5
HET SO4 A1002 5
HET SO4 A1003 5
HET 368 A 901 28
HET GOL A 900 6
HETNAM SO4 SULFATE ION
HETNAM 368 (1R)-2-{[AMINO(IMINO)METHYL]AMINO}-1-{4-[(4R)-4-
HETNAM 2 368 (HYDROXYMETHYL)-1,3,2-DIOXABOROLAN-2-YL]PHENYL}ETHYL
HETNAM 3 368 NICOTINATE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 SO4 3(O4 S 2-)
FORMUL 5 368 C18 H21 B N4 O5
FORMUL 6 GOL C3 H8 O3
FORMUL 7 HOH *101(H2 O)
HELIX 1 1 ALA A 55 TYR A 59A 5 6
HELIX 2 2 SER A 61 LYS A 63 5 3
HELIX 3 3 ASN A 73 ILE A 77 5 5
HELIX 4 4 MET A 96 GLY A 100 5 5
HELIX 5 5 SER A 126 ARG A 130 5 5
HELIX 6 6 THR A 164 TYR A 172 1 9
HELIX 7 7 TYR A 234 GLN A 243 1 10
SHEET 1 A 8 THR A 20 ALA A 21 0
SHEET 2 A 8 GLN A 156 LYS A 159 -1 O LYS A 157 N THR A 20
SHEET 3 A 8 CYS A 136 GLY A 140 -1 N GLY A 140 O GLN A 156
SHEET 4 A 8 PRO A 198 HIS A 202A-1 O SER A 198B N TRP A 137
SHEET 5 A 8 VAL A 202D TRP A 215 -1 O VAL A 202D N HIS A 202A
SHEET 6 A 8 GLY A 226 ASN A 230 -1 O VAL A 227 N TRP A 215
SHEET 7 A 8 MET A 180 ALA A 183 -1 N ILE A 181 O TYR A 228
SHEET 8 A 8 LEU A 162 VAL A 163 -1 N VAL A 163 O CYS A 182
SHEET 1 B 7 GLN A 30 THR A 35 0
SHEET 2 B 7 ARG A 37D GLY A 46 -1 O LEU A 39 N LEU A 33
SHEET 3 B 7 TRP A 51 THR A 54 -1 O LEU A 53 N SER A 43
SHEET 4 B 7 ALA A 104 LEU A 108 -1 O ALA A 104 N THR A 54
SHEET 5 B 7 PHE A 83 ILE A 90 -1 N ILE A 89 O LEU A 105
SHEET 6 B 7 LEU A 65 TYR A 68 -1 N VAL A 67 O PHE A 83
SHEET 7 B 7 GLN A 30 THR A 35 -1 N HIS A 34 O ARG A 66
SSBOND 1 CYS A 40 CYS A 58 1555 1555 2.03
SSBOND 2 CYS A 136 CYS A 201 1555 1555 2.03
SSBOND 3 CYS A 168 CYS A 182 1555 1555 2.03
SSBOND 4 CYS A 191 CYS A 219 1555 1555 2.03
LINK OG SER A 195 B07 368 A 901 1555 1555 1.46
CISPEP 1 SER A 37 PRO A 37A 0 -0.63
SITE 1 AC1 5 THR A 20 ALA A 21 GLN A 48 GLN A 86
SITE 2 AC1 5 LYS A 107
SITE 1 AC2 5 ASN A 113 TYR A 143 ARG A 147 LYS A 149
SITE 2 AC2 5 LYS A 192
SITE 1 AC3 5 HIS A 91 LYS A 179 TRP A 237 HOH A1049
SITE 2 AC3 5 HOH A1085
SITE 1 AC4 15 LEU A 39 HIS A 57 SER A 81A LEU A 146
SITE 2 AC4 15 ASP A 189 ALA A 190 CYS A 191 LYS A 192
SITE 3 AC4 15 GLY A 193 ASP A 194 SER A 195 GLY A 216
SITE 4 AC4 15 GLY A 218 CYS A 219 GLY A 226
SITE 1 AC5 8 ARG A 24 GLY A 25 TRP A 27 GLY A 70
SITE 2 AC5 8 ILE A 71 LEU A 72 SER A 117 LEU A 155
CRYST1 121.001 121.001 121.001 90.00 90.00 90.00 I 2 3 24
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 0.008264 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008264 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008264 0.00000
(ATOM LINES ARE NOT SHOWN.)
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