HEADER HYDROLASE 30-NOV-02 1J17
TITLE FACTOR XA SPECIFIC INHIBITOR IN COMPLEX WITH RAT TRYPSIN
TITLE 2 MUTANT X99/175/190RT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRYPSIN II, ANIONIC;
COMPND 3 CHAIN: T;
COMPND 4 SYNONYM: TRYPSINOGEN, BETA-TRYPSIN, PRETRYPSINOGEN II;
COMPND 5 EC: 3.4.21.4;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 TISSUE: PANCREAS;
SOURCE 6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PYT
KEYWDS SERINE PROTEASE, HYDROLASE, SERINE PROTEINASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.T.STUBBS
REVDAT 3 24-FEB-09 1J17 1 VERSN
REVDAT 2 11-FEB-03 1J17 1 JRNL
REVDAT 1 23-DEC-02 1J17 0
JRNL AUTH S.REYDA,C.SOHN,G.KLEBE,K.RALL,D.ULLMANN,
JRNL AUTH 2 H.D.JAKUBKE,M.T.STUBBS
JRNL TITL RECONSTRUCTING THE BINDING SITE OF FACTOR XA IN
JRNL TITL 2 TRYPSIN REVEALS LIGAND-INDUCED STRUCTURAL
JRNL TITL 3 PLASTICITY
JRNL REF J.MOL.BIOL. V. 325 963 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12527302
JRNL DOI 10.1016/S0022-2836(02)01337-2
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.T.STUBBS,S.REYDA,F.DULLWEBER,M.MOELLER,G.KLEBE,
REMARK 1 AUTH 2 D.DORSCH,W.W.K.R.MEDERSKI,H.WURZIGER
REMARK 1 TITL PH-DEPENDENT BINDING MODES OBSERVED IN TRYPSIN
REMARK 1 TITL 2 CRYSTALS: LESSONS FOR STRUCTURE-BASED DRUG DESIGN
REMARK 1 REF CHEMBIOCHEM V. 3 246 2002
REMARK 1 REFN ISSN 1439-4227
REMARK 1 DOI 10.1002/1439-7633(20020301)3:2/3<246::AID-CBIC246>3
REMARK 1 DOI 2 .0.CO;2-#
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.RENATUS,W.BODE,R.HUBER,J.STUERZEBECHER,M.T.STUBBS
REMARK 1 TITL STRUCTURAL AND FUNCTIONAL ANALYSES OF
REMARK 1 TITL 2 BENZAMIDINE-BASED INHIBITORS IN COMPLEX WITH
REMARK 1 TITL 3 TRYPSIN: IMPLICATIONS FOR THE INHIBITION OF FACTOR
REMARK 1 TITL 4 XA, TPA, AND UROKINAS
REMARK 1 REF J.MED.CHEM. V. 41 5445 1998
REMARK 1 REFN ISSN 0022-2623
REMARK 1 DOI 10.1021/JM981068G
REMARK 1 REFERENCE 3
REMARK 1 AUTH M.T.STUBBS
REMARK 1 TITL STRUCTURAL ASPECTS OF FACTOR XA INHIBITION
REMARK 1 REF CURR.PHARM.DES. V. 2 543 1996
REMARK 1 REFN ISSN 1381-6128
REMARK 1 REFERENCE 4
REMARK 1 AUTH M.T.STUBBS,R.HUBER,W.BODE
REMARK 1 TITL CRYSTAL STRUCTURES OF FACTOR XA SPECIFIC
REMARK 1 TITL 2 INHIBITORS IN COMPLEX WITH TRYPSIN: STRUCTURAL
REMARK 1 TITL 3 GROUNDS FOR INHIBITION OF FACTOR XA AND
REMARK 1 TITL 4 SELECTIVITY AGAINST THROMBIN
REMARK 1 REF FEBS LETT. V. 375 103 1995
REMARK 1 REFN ISSN 0014-5793
REMARK 1 DOI 10.1016/0014-5793(95)01190-P
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 21631
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
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 : 1742
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 68
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 1J17 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-DEC-02.
REMARK 100 THE RCSB ID CODE IS RCSB005501.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-FEB-00
REMARK 200 TEMPERATURE (KELVIN) : 287
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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) : 1.5418
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25095
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 29.410
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.0
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 62.39000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 62.39000
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 62.39000
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 62.39000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 62.39000
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 62.39000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 62.39000
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 62.39000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 62.39000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 62.39000
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 62.39000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 62.39000
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 62.39000
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 62.39000
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 62.39000
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 62.39000
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 62.39000
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 62.39000
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 62.39000
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 62.39000
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 62.39000
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 62.39000
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 62.39000
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 62.39000
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 62.39000
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 62.39000
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 62.39000
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 62.39000
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 62.39000
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 62.39000
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 62.39000
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 62.39000
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 62.39000
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 62.39000
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 62.39000
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 62.39000
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: T
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: 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 ASP T 49 -7.42 -56.70
REMARK 500 HIS T 71 -64.71 -130.15
REMARK 500 ASN T 115 -159.55 -154.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA T 480 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU T 80 OE2
REMARK 620 2 HOH T 261 O 95.1
REMARK 620 3 GLU T 70 OE1 99.0 80.9
REMARK 620 4 ASN T 72 O 166.0 98.8 84.9
REMARK 620 5 VAL T 75 O 92.7 92.3 166.9 85.1
REMARK 620 6 GLU T 77 OE1 82.6 177.3 98.0 83.5 89.2
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA T 480
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 T 600
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZEN T 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QL7 RELATED DB: PDB
REMARK 900 RELATED ID: 1QL8 RELATED DB: PDB
REMARK 900 RELATED ID: 1QL9 RELATED DB: PDB
REMARK 900 RELATED ID: 1J14 RELATED DB: PDB
REMARK 900 BENZAMIDINE IN COMPLEX WITH RAT TRYPSIN MUTANT X99RT
REMARK 900 RELATED ID: 1J15 RELATED DB: PDB
REMARK 900 BENZAMIDINE IN COMPLEX WITH RAT TRYPSIN MUTANT X99/175/
REMARK 900 190RT AT ROOM TEMPERATURE
REMARK 900 RELATED ID: 1J16 RELATED DB: PDB
REMARK 900 BENZAMIDINE IN COMPLEX WITH RAT TRYPSIN MUTANT X99/175/
REMARK 900 190RT AT 100K
DBREF 1J17 T 16 245 UNP P00763 TRY2_RAT 24 246
SEQADV 1J17 GLU T 97 UNP P00763 LYS 102 ENGINEERED
SEQADV 1J17 TYR T 99 UNP P00763 LEU 104 ENGINEERED
SEQADV 1J17 SER T 172 UNP P00763 TYR 175 ENGINEERED
SEQADV 1J17 SER T 173 UNP P00763 PRO 176 ENGINEERED
SEQADV 1J17 PHE T 174 UNP P00763 GLY 177 ENGINEERED
SEQADV 1J17 ILE T 175 UNP P00763 LYS 178 ENGINEERED
SEQADV 1J17 ALA T 190 UNP P00763 SER 195 ENGINEERED
SEQRES 1 T 223 ILE VAL GLY GLY TYR THR CYS GLN GLU ASN SER VAL PRO
SEQRES 2 T 223 TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY
SEQRES 3 T 223 GLY SER LEU ILE ASN ASP GLN TRP VAL VAL SER ALA ALA
SEQRES 4 T 223 HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU
SEQRES 5 T 223 HIS ASN ILE ASN VAL LEU GLU GLY ASN GLU GLN PHE VAL
SEQRES 6 T 223 ASN ALA ALA LYS ILE ILE LYS HIS PRO ASN PHE ASP ARG
SEQRES 7 T 223 GLU THR TYR ASN ASN ASP ILE MET LEU ILE LYS LEU SER
SEQRES 8 T 223 SER PRO VAL LYS LEU ASN ALA ARG VAL ALA THR VAL ALA
SEQRES 9 T 223 LEU PRO SER SER CYS ALA PRO ALA GLY THR GLN CYS LEU
SEQRES 10 T 223 ILE SER GLY TRP GLY ASN THR LEU SER SER GLY VAL ASN
SEQRES 11 T 223 GLU PRO ASP LEU LEU GLN CYS LEU ASP ALA PRO LEU LEU
SEQRES 12 T 223 PRO GLN ALA ASP CYS GLU ALA SER SER SER PHE ILE ILE
SEQRES 13 T 223 THR ASP ASN MET VAL CYS VAL GLY PHE LEU GLU GLY GLY
SEQRES 14 T 223 LYS ASP ALA CYS GLN GLY ASP SER GLY GLY PRO VAL VAL
SEQRES 15 T 223 CYS ASN GLY GLU LEU GLN GLY ILE VAL SER TRP GLY TYR
SEQRES 16 T 223 GLY CYS ALA LEU PRO ASP ASN PRO GLY VAL TYR THR LYS
SEQRES 17 T 223 VAL CYS ASN TYR VAL ASP TRP ILE GLN ASP THR ILE ALA
SEQRES 18 T 223 ALA ASN
HET CA T 480 1
HET SO4 T 600 5
HET ZEN T 1 34
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
HETNAM ZEN [4-(6-CHLORO-NAPHTHALENE-2-SULFONYL)-PIPERAZIN-1-YL]-
HETNAM 2 ZEN (3,4,5,6-TETRAHYDRO-2H-[1,4']BIPYRIDINYL-4-YL)-
HETNAM 3 ZEN METHANONE
FORMUL 2 CA CA 2+
FORMUL 3 SO4 O4 S 2-
FORMUL 4 ZEN C25 H27 CL N4 O3 S
FORMUL 5 HOH *68(H2 O)
HELIX 1 1 ALA T 55 TYR T 59 5 5
HELIX 2 2 PRO T 164 SER T 172 1 9
HELIX 3 3 TYR T 234 ALA T 244 1 11
SHEET 1 A 7 TYR T 20 THR T 21 0
SHEET 2 A 7 GLN T 156 PRO T 161 -1 O CYS T 157 N TYR T 20
SHEET 3 A 7 GLN T 135 GLY T 140 -1 N CYS T 136 O ALA T 160
SHEET 4 A 7 PRO T 198 CYS T 201 -1 O VAL T 200 N LEU T 137
SHEET 5 A 7 GLU T 204 TRP T 215 -1 O GLU T 204 N CYS T 201
SHEET 6 A 7 GLY T 226 LYS T 230 -1 O VAL T 227 N TRP T 215
SHEET 7 A 7 MET T 180 VAL T 183 -1 N VAL T 181 O TYR T 228
SHEET 1 B 7 GLN T 30 ASN T 34 0
SHEET 2 B 7 HIS T 40 ASN T 48 -1 O CYS T 42 N LEU T 33
SHEET 3 B 7 TRP T 51 SER T 54 -1 O VAL T 53 N SER T 45
SHEET 4 B 7 MET T 104 LEU T 108 -1 O MET T 104 N SER T 54
SHEET 5 B 7 GLN T 81 LYS T 90 -1 N ILE T 89 O LEU T 105
SHEET 6 B 7 GLN T 64 LEU T 68 -1 N VAL T 66 O VAL T 83
SHEET 7 B 7 GLN T 30 ASN T 34 -1 N ASN T 34 O GLN T 64
SSBOND 1 CYS T 22 CYS T 157 1555 1555 2.03
SSBOND 2 CYS T 42 CYS T 58 1555 1555 2.03
SSBOND 3 CYS T 128 CYS T 232 1555 1555 2.03
SSBOND 4 CYS T 136 CYS T 201 1555 1555 2.02
SSBOND 5 CYS T 168 CYS T 182 1555 1555 2.02
SSBOND 6 CYS T 191 CYS T 220 1555 1555 2.02
LINK CA CA T 480 OE2 GLU T 80 1555 1555 2.38
LINK CA CA T 480 O HOH T 261 1555 1555 2.26
LINK CA CA T 480 OE1 GLU T 70 1555 1555 2.33
LINK CA CA T 480 O ASN T 72 1555 1555 2.28
LINK CA CA T 480 O VAL T 75 1555 1555 2.24
LINK CA CA T 480 OE1 GLU T 77 1555 1555 2.73
SITE 1 AC1 6 GLU T 70 ASN T 72 VAL T 75 GLU T 77
SITE 2 AC1 6 GLU T 80 HOH T 261
SITE 1 AC2 6 ZEN T 1 HIS T 57 GLN T 192 GLY T 193
SITE 2 AC2 6 SER T 195 HOH T 726
SITE 1 AC3 21 GLU T 97 THR T 98 TYR T 99 LEU T 145
SITE 2 AC3 21 GLY T 148 VAL T 149 PHE T 174 ALA T 190
SITE 3 AC3 21 GLN T 192 SER T 195 VAL T 213 TRP T 215
SITE 4 AC3 21 GLY T 216 GLY T 219 CYS T 220 GLY T 226
SITE 5 AC3 21 VAL T 227 TYR T 228 SO4 T 600 HOH T 723
SITE 6 AC3 21 HOH T 729
CRYST1 124.780 124.780 124.780 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 0.008014 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008014 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008014 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
