HEADER HYDROLASE/HYDROLASE INHIBITOR 24-JAN-06 2FTL
TITLE CRYSTAL STRUCTURE OF TRYPSIN COMPLEXED WITH BPTI AT 100K
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATIONIC TRYPSIN;
COMPND 3 CHAIN: E;
COMPND 4 SYNONYM: BETA-TRYPSIN;
COMPND 5 EC: 3.4.21.4;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PANCREATIC TRYPSIN INHIBITOR;
COMPND 8 CHAIN: I;
COMPND 9 FRAGMENT: BPTI;
COMPND 10 SYNONYM: BASIC PROTEASE INHIBITOR, BPI, BPTI, APROTININ;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 7 ORGANISM_COMMON: CATTLE;
SOURCE 8 ORGANISM_TAXID: 9913;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: HB101;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PTI103
KEYWDS PROTEASE-INHIBITOR COMPLEX, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR W.M.HANSON,M.P.HORVATH,D.P.GOLDENBERG
REVDAT 7 30-AUG-23 2FTL 1 REMARK LINK
REVDAT 6 27-JUL-11 2FTL 1 HETNAM HETSYN REMARK
REVDAT 5 13-JUL-11 2FTL 1 VERSN
REVDAT 4 08-SEP-09 2FTL 1 HET
REVDAT 3 24-FEB-09 2FTL 1 VERSN
REVDAT 2 20-FEB-07 2FTL 1 JRNL
REVDAT 1 14-FEB-06 2FTL 0
JRNL AUTH W.M.HANSON,G.J.DOMEK,M.P.HORVATH,D.P.GOLDENBERG
JRNL TITL RIGIDIFICATION OF A FLEXIBLE PROTEASE INHIBITOR VARIANT UPON
JRNL TITL 2 BINDING TO TRYPSIN.
JRNL REF J.MOL.BIOL. V. 366 230 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17157870
JRNL DOI 10.1016/J.JMB.2006.11.003
REMARK 2
REMARK 2 RESOLUTION. 1.62 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.62
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
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) (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 48719
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : TRHOUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM, SAME TEST SET AS FOR
REMARK 3 PDB ID 2FI3, 2FI4, AND 2FI5
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3953
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 : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.62
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.72
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.93
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7341
REMARK 3 BIN R VALUE (WORKING SET) : 0.2510
REMARK 3 BIN FREE R VALUE : 0.2740
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 8.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 667
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 : 2071
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 67
REMARK 3 SOLVENT ATOMS : 260
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.30
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) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.16
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) : 0.23
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.19
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.000
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.979 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.493 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.521 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.167 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 19.45
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: MAXIMUM-LIKELIHOOD USING MEASURED
REMARK 3 INTENSITIES (MLI) TARGET AS IMPLEMENTED WITH CNS SOLVE 1.1
REMARK 4
REMARK 4 2FTL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JAN-06.
REMARK 100 THE DEPOSITION ID IS D_1000036295.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-AUG-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.5
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 : ENRAF-NONIUS FR591
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC CONFOCAL MAX-FLUX (GREEN)
REMARK 200 OPTICS : OSMIC CONFOCAL MAX-FLUX (GREEN)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NONIUS KAPPA CCD2000
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50681
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 10.30
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.24100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.630
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 2PTC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MM CALCIUM CHLORIDE, 0.1 M HEPES,
REMARK 280 1.8 M AMMONIUM SULFATE, 0.02% SODIUM AZIDE; 20% ETHYLENE GLYCOL
REMARK 280 ADDED UPON HARVESTING AND PRIOR TO FREEZING, PH 7.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 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 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 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 1.000000 0.000000 0.000000 37.36300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 40.95300
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 62.13050
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 37.36300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 40.95300
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 62.13050
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 37.36300
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 40.95300
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 62.13050
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 37.36300
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 40.95300
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 62.13050
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
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: 4110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -104.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 24040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -530.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 163.81200
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 163.81200
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -234.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 163.81200
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -235.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 163.81200
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -233.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 163.81200
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 -1.000000 0.000000 163.81200
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 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 CA CA I1003 LIES ON A SPECIAL POSITION.
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 LYS E 145 CD CE NZ
REMARK 470 ARG I 1 N CA CB CG CD NE CZ
REMARK 470 ARG I 1 NH1 NH2
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 E 71 -78.25 -131.17
REMARK 500 SER E 214 -69.57 -122.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 THE RESIDUE IAS 115 IN CHAIN E IS CONNECTED TO
REMARK 600 RESIDUE 116 BY A BETA-PEPTIDE LINKAGE.
REMARK 600 THIS IS A COVALENT BOND BETWEEN CG OF IAS
REMARK 600 AND N OF THE FOLLOWING RESIDUE.
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 E1002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 70 OE2
REMARK 620 2 ASN E 72 O 90.6
REMARK 620 3 VAL E 75 O 165.9 81.6
REMARK 620 4 GLU E 80 OE2 103.1 159.5 87.7
REMARK 620 5 HOH E1019 O 81.0 86.7 110.1 80.6
REMARK 620 6 HOH E1023 O 79.5 103.3 90.8 94.2 158.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA E1001 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 71 OD2
REMARK 620 2 GLU E 77 OE2 126.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA I1003 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR I 32 N
REMARK 620 2 THR I 32 N 120.7
REMARK 620 3 HOH I 922 O 86.7 131.6
REMARK 620 4 HOH I 922 O 131.6 86.7 104.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA E 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 1008
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 1009
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 1010
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 1011
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA I 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 1007
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2PTC RELATED DB: PDB
REMARK 900 WILD-TYPE BPTI COMPLEXED WITH TRYPSIN AT ROOM TEMPERATURE
REMARK 900 RELATED ID: 2FTM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE COMPARISON OF TRYPSIN COMPLEXED WITH BPTI OR THE
REMARK 900 BPTI VARIANT TYR35 -> GLY
DBREF 2FTL E 16 238 UNP P00760 TRY1_BOVIN 21 243
DBREF 2FTL I 1 58 UNP P00974 BPT1_BOVIN 36 93
SEQRES 1 E 223 ILE VAL GLY GLY TYR THR CYS GLY ALA ASN THR VAL PRO
SEQRES 2 E 223 TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY
SEQRES 3 E 223 GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA
SEQRES 4 E 223 HIS CYS TYR LYS SER GLY ILE GLN VAL ARG LEU GLY GLU
SEQRES 5 E 223 ASP ASN ILE ASN VAL VAL GLU GLY ASN GLU GLN PHE ILE
SEQRES 6 E 223 SER ALA SER LYS SER ILE VAL HIS PRO SER TYR ASN SER
SEQRES 7 E 223 ASN THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU LYS
SEQRES 8 E 223 SER ALA ALA SER LEU IAS SER ARG VAL ALA SER ILE SER
SEQRES 9 E 223 LEU PRO THR SER CYS ALA SER ALA GLY THR GLN CYS LEU
SEQRES 10 E 223 ILE SER GLY TRP GLY ASN THR LYS SER SER GLY THR SER
SEQRES 11 E 223 TYR PRO ASP VAL LEU LYS CYS LEU LYS ALA PRO ILE LEU
SEQRES 12 E 223 SER ASP SER SER CYS LYS SER ALA TYR PRO GLY GLN ILE
SEQRES 13 E 223 THR SER ASN MET PHE CYS ALA GLY TYR LEU GLU GLY GLY
SEQRES 14 E 223 LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL
SEQRES 15 E 223 CYS SER GLY LYS LEU GLN GLY ILE VAL SER TRP GLY SER
SEQRES 16 E 223 GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS
SEQRES 17 E 223 VAL CYS ASN TYR VAL SER TRP ILE LYS GLN THR ILE ALA
SEQRES 18 E 223 SER ASN
SEQRES 1 I 58 ARG PRO ASP PHE CYS LEU GLU PRO PRO TYR THR GLY PRO
SEQRES 2 I 58 CYS LYS ALA ARG ILE ILE ARG TYR PHE TYR ASN ALA LYS
SEQRES 3 I 58 ALA GLY LEU CYS GLN THR PHE VAL TYR GLY GLY CYS ARG
SEQRES 4 I 58 ALA LYS ARG ASN ASN PHE LYS SER ALA GLU ASP CYS MET
SEQRES 5 I 58 ARG THR CYS GLY GLY ALA
HET IAS E 115 8
HET NA E1001 1
HET CA E1002 1
HET SO4 E1008 10
HET SO4 E1009 5
HET SO4 E1010 5
HET SO4 E1011 10
HET EDO E 1 4
HET EDO E 2 4
HET EDO E 3 4
HET EDO E 4 4
HET EDO E 5 4
HET EDO E 6 4
HET CA I1003 1
HET SO4 I1004 5
HET SO4 I1005 5
HET SO4 I1006 10
HET SO4 I1007 5
HETNAM IAS BETA-L-ASPARTIC ACID
HETNAM NA SODIUM ION
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN IAS L-ASPARTIC ACID
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 IAS C4 H7 N O4
FORMUL 3 NA NA 1+
FORMUL 4 CA 2(CA 2+)
FORMUL 5 SO4 8(O4 S 2-)
FORMUL 9 EDO 6(C2 H6 O2)
FORMUL 20 HOH *260(H2 O)
HELIX 1 1 ALA E 55 TYR E 59 5 5
HELIX 2 2 SER E 164 TYR E 172 1 9
HELIX 3 3 TYR E 234 SER E 244 1 11
HELIX 4 4 ASP I 3 GLU I 7 5 5
HELIX 5 5 SER I 47 GLY I 56 1 10
SHEET 1 A 7 TYR E 20 THR E 21 0
SHEET 2 A 7 LYS E 156 PRO E 161 -1 O CYS E 157 N TYR E 20
SHEET 3 A 7 GLN E 135 GLY E 140 -1 N ILE E 138 O LEU E 158
SHEET 4 A 7 PRO E 198 CYS E 201 -1 O VAL E 200 N LEU E 137
SHEET 5 A 7 LYS E 204 TRP E 215 -1 O LYS E 204 N CYS E 201
SHEET 6 A 7 GLY E 226 LYS E 230 -1 O VAL E 227 N TRP E 215
SHEET 7 A 7 MET E 180 ALA E 183 -1 N PHE E 181 O TYR E 228
SHEET 1 B 7 GLN E 30 ASN E 34 0
SHEET 2 B 7 HIS E 40 ASN E 48 -1 O CYS E 42 N LEU E 33
SHEET 3 B 7 TRP E 51 SER E 54 -1 O VAL E 53 N SER E 45
SHEET 4 B 7 MET E 104 LEU E 108 -1 O ILE E 106 N VAL E 52
SHEET 5 B 7 GLN E 81 VAL E 90 -1 N ILE E 89 O LEU E 105
SHEET 6 B 7 GLN E 64 LEU E 67 -1 N VAL E 65 O ILE E 83
SHEET 7 B 7 GLN E 30 ASN E 34 -1 N SER E 32 O ARG E 66
SHEET 1 C 2 ILE I 18 ASN I 24 0
SHEET 2 C 2 LEU I 29 TYR I 35 -1 O TYR I 35 N ILE I 18
SSBOND 1 CYS E 22 CYS E 157 1555 1555 2.03
SSBOND 2 CYS E 42 CYS E 58 1555 1555 2.04
SSBOND 3 CYS E 128 CYS E 232 1555 1555 2.03
SSBOND 4 CYS E 136 CYS E 201 1555 1555 2.03
SSBOND 5 CYS E 168 CYS E 182 1555 1555 2.04
SSBOND 6 CYS E 191 CYS E 220 1555 1555 2.03
SSBOND 7 CYS I 5 CYS I 55 1555 1555 2.02
SSBOND 8 CYS I 14 CYS I 38 1555 1555 2.02
SSBOND 9 CYS I 30 CYS I 51 1555 1555 2.03
LINK C LEU E 114 N IAS E 115 1555 1555 1.33
LINK CG IAS E 115 N SER E 116 1555 1555 1.33
LINK OE2 GLU E 70 CA CA E1002 1555 1555 2.26
LINK OD2 ASP E 71 NA NA E1001 1555 1555 2.41
LINK O ASN E 72 CA CA E1002 1555 1555 2.36
LINK O VAL E 75 CA CA E1002 1555 1555 2.23
LINK OE2 GLU E 77 NA NA E1001 1555 1555 2.74
LINK OE2 GLU E 80 CA CA E1002 1555 1555 2.28
LINK CA CA E1002 O HOH E1019 1555 1555 2.40
LINK CA CA E1002 O HOH E1023 1555 1555 2.34
LINK N THR I 32 CA CA I1003 1555 1555 2.91
LINK N THR I 32 CA CA I1003 4575 1555 2.91
LINK O BHOH I 922 CA CA I1003 1555 1555 2.83
LINK O BHOH I 922 CA CA I1003 4575 1555 2.83
SITE 1 AC1 2 ASP E 71 GLU E 77
SITE 1 AC2 6 GLU E 70 ASN E 72 VAL E 75 GLU E 80
SITE 2 AC2 6 HOH E1019 HOH E1023
SITE 1 AC3 9 TYR E 59 LYS E 60 SER E 61 HOH E1074
SITE 2 AC3 9 HOH E1129 HOH E1161 HOH E1180 HOH E1192
SITE 3 AC3 9 LYS I 46
SITE 1 AC4 4 LYS E 169 PRO E 173 GLY E 174 HOH E1057
SITE 1 AC5 5 LYS E 107 SER E 164 ASP E 165 SER E 166
SITE 2 AC5 5 HOH E1094
SITE 1 AC6 9 SER E 93 ASN E 95 THR E 98 ASN E 100
SITE 2 AC6 9 ASN E 101 SER E 178 ASN E 179 HOH E1095
SITE 3 AC6 9 HOH E1151
SITE 1 AC7 5 ALA E 129 PHE E 181 GLN E 210 LYS E 230
SITE 2 AC7 5 HOH E1037
SITE 1 AC8 6 ASN E 34 TYR E 39 HIS E 40 ILE E 73
SITE 2 AC8 6 HOH E1022 HOH E1139
SITE 1 AC9 3 TYR E 20 CYS E 22 THR E 26
SITE 1 BC1 3 ASP E 153 VAL E 154 LYS E 156
SITE 1 BC2 5 SER E 49 ALA E 112 SER E 113 LEU E 114
SITE 2 BC2 5 HOH E1146
SITE 1 BC3 4 ILE E 47 ASN E 48 ILE E 242 HOH E1145
SITE 1 BC4 3 GLN I 31 THR I 32 HOH I 922
SITE 1 BC5 9 ARG I 20 TYR I 35 GLY I 37 ALA I 40
SITE 2 BC5 9 HOH I 216 HOH I 445 HOH I 521 HOH I 538
SITE 3 BC5 9 HOH I 554
SITE 1 BC6 8 GLU I 7 ARG I 42 HOH I 135 HOH I 412
SITE 2 BC6 8 HOH I 430 HOH I 573 HOH I 897 HOH I 898
SITE 1 BC7 7 LYS E 87 LYS E 107 HOH E1126 ARG I 42
SITE 2 BC7 7 HOH I 317 HOH I 594 HOH I 947
SITE 1 BC8 7 PRO I 9 TYR I 10 THR I 11 GLY I 12
SITE 2 BC8 7 HOH I 326 HOH I 679 HOH I 923
CRYST1 74.726 81.906 124.261 90.00 90.00 90.00 I 2 2 2 8
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 0.013382 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012209 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008048 0.00000
(ATOM LINES ARE NOT SHOWN.)
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