HEADER COMPLEX(PROTEINASE/INHIBITOR) 17-DEC-92 1BRB
TITLE CRYSTAL STRUCTURES OF RAT ANIONIC TRYPSIN COMPLEXED WITH
TITLE 2 THE PROTEIN INHIBITORS APPI AND BPTI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRYPSIN;
COMPND 3 CHAIN: E;
COMPND 4 EC: 3.4.21.4;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PANCREATIC TRYPSIN INHIBITOR;
COMPND 8 CHAIN: I;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 MOL_ID: 2
KEYWDS COMPLEX(PROTEINASE/INHIBITOR)
EXPDTA X-RAY DIFFRACTION
AUTHOR J.J.PERONA,R.J.FLETTERICK
REVDAT 3 24-FEB-09 1BRB 1 VERSN
REVDAT 2 15-JAN-95 1BRB 1 SEQRES
REVDAT 1 31-JUL-94 1BRB 0
JRNL AUTH J.J.PERONA,C.A.TSU,C.S.CRAIK,R.J.FLETTERICK
JRNL TITL CRYSTAL STRUCTURES OF RAT ANIONIC TRYPSIN
JRNL TITL 2 COMPLEXED WITH THE PROTEIN INHIBITORS APPI AND
JRNL TITL 3 BPTI.
JRNL REF J.MOL.BIOL. V. 230 919 1993
JRNL REFN ISSN 0022-2836
JRNL PMID 7683059
JRNL DOI 10.1006/JMBI.1993.1210
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.J.PERONA,C.A.TSU,M.E.MCGRATH,C.S.CRAIK,
REMARK 1 AUTH 2 R.J.FLETTERICK
REMARK 1 TITL RELOCATING A NEGATIVE CHARGE IN THE BINDING POCKET
REMARK 1 TITL 2 OF TRYPSIN
REMARK 1 REF J.MOL.BIOL. V. 230 934 1993
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
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 : NULL
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) : 0.198
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 : 2042
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 142
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) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 2.80
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 1BRB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.54667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 20.77333
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 20.77333
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 41.54667
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: 1400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THE BPTI INHIBITOR IS THE VARIANT C5A/C55A PRODUCED BY
REMARK 400 RECOMBINANT DNA METHODOLOGIES AND EXPRESSED IN ESCHERICHIA
REMARK 400 COLI (ALTMAN,J.; PH. D. THESIS, UNIVERSITY OF CALIFORNIA
REMARK 400 AT SAN FRANCISCO, 1991). THE N-TERMINAL FOUR RESIDUES AND
REMARK 400 THE C-TERMINAL THREE RESIDUES (56 - 58) ARE DISORDERED.
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 ARG I 1
REMARK 465 PRO I 2
REMARK 465 ASP I 3
REMARK 465 PHE I 4
REMARK 465 GLY I 56
REMARK 465 GLY I 57
REMARK 465 ALA I 58
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 97 CG CD CE NZ
REMARK 470 ASP E 178 CG OD1 OD2
REMARK 470 ASN E 202 CG OD1 ND2
REMARK 470 GLN E 239 CG CD OE1 NE2
REMARK 470 ARG I 42 CG CD NE CZ NH1 NH2
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 E 40 NE2 HIS E 40 CD2 -0.066
REMARK 500 HIS E 91 NE2 HIS E 91 CD2 -0.068
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 TRP E 51 CD1 - CG - CD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 TRP E 51 CE2 - CD2 - CG ANGL. DEV. = -5.2 DEGREES
REMARK 500 THR E 120 N - CA - CB ANGL. DEV. = -13.2 DEGREES
REMARK 500 TRP E 141 CD1 - CG - CD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 TRP E 141 CE2 - CD2 - CG ANGL. DEV. = -5.6 DEGREES
REMARK 500 THR E 144 N - CA - CB ANGL. DEV. = -12.7 DEGREES
REMARK 500 LEU E 162 CA - CB - CG ANGL. DEV. = 15.8 DEGREES
REMARK 500 TRP E 215 CD1 - CG - CD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 TRP E 215 CE2 - CD2 - CG ANGL. DEV. = -5.6 DEGREES
REMARK 500 TRP E 237 CD1 - CG - CD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 TRP E 237 CE2 - CD2 - CG ANGL. DEV. = -5.4 DEGREES
REMARK 500 CYS I 30 CA - CB - SG ANGL. DEV. = -10.9 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 HIS E 71 -55.35 -121.91
REMARK 500 ASN E 115 -163.52 -168.31
REMARK 500 ASN E 150 99.23 -162.05
REMARK 500 SER E 214 -70.71 -130.47
REMARK 500 ALA I 27 -24.65 172.98
REMARK 500 ASN I 44 111.77 -162.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH I 393 DISTANCE = 6.70 ANGSTROMS
REMARK 525 HOH I 397 DISTANCE = 10.72 ANGSTROMS
REMARK 525 HOH I 408 DISTANCE = 5.40 ANGSTROMS
REMARK 525 HOH E 310 DISTANCE = 9.23 ANGSTROMS
REMARK 525 HOH E 323 DISTANCE = 6.39 ANGSTROMS
REMARK 525 HOH E 339 DISTANCE = 7.80 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD RESIDUES, CONSERVED IN ALL
REMARK 800 SERINE PROTEASES OF THE TRYPSIN AND SUBTILISIN STRUCTURAL
REMARK 800 CLASSES
REMARK 999
REMARK 999 SEQUENCE
REMARK 999
REMARK 999 SEQUENCE ADVISORY NOTICE:
REMARK 999 SEQUENCE FOR TRYPSIN IN THIS STRUCTURE WAS TAKEN FROM
REMARK 999 GENEMBL WHICH DIFFERS FROM SWISSPROT SEQUENCE AT POSITIONS
REMARK 999 61 AND 65.
REMARK 999
REMARK 999 SEQUENCE ADVISORY NOTICE
REMARK 999 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE.
REMARK 999
REMARK 999 SWISS-PROT ENTRY NAME: TRY2_RAT
REMARK 999
REMARK 999 SWISS-PROT RESIDUE PDB SEQRES
REMARK 999
REMARK 999 NAME NUMBER NAME CHAIN SEQ/INSERT CODE
REMARK 999 ASP 84 ASN E 79 (SWISSPROT ERROR)
REMARK 999 ILE 88 VAL E 83 (SWISSPROT ERROR)
REMARK 999 ASP 194 GLY E 189 (ENGINEERED)
REMARK 999 GLY 227 ASP E 226 (ENGINEERED)
REMARK 999
REMARK 999 SWISS-PROT ENTRY NAME: BPT1_BOVIN
REMARK 999
REMARK 999 SWISS-PROT RESIDUE PDB SEQRES
REMARK 999
REMARK 999 NAME NUMBER NAME CHAIN SEQ/INSERT CODE
REMARK 999 CYS 40 ALA I 5 (VARIANT)
REMARK 999 LEU 41 GLY I 6
REMARK 999 CYS 90 ALA I 55 (VARIANT)
DBREF 1BRB E 16 245 UNP P00763 TRY2_RAT 24 246
DBREF 1BRB I 1 58 UNP P00974 BPT1_BOVIN 36 93
SEQADV 1BRB GLY E 189 UNP P00763 ASP 194 CONFLICT
SEQADV 1BRB ASP E 226 UNP P00763 GLY 227 CONFLICT
SEQADV 1BRB ALA I 5 UNP P00974 CYS 40 CONFLICT
SEQADV 1BRB GLY I 6 UNP P00974 LEU 41 CONFLICT
SEQADV 1BRB ALA I 55 UNP P00974 CYS 90 CONFLICT
SEQRES 1 E 223 ILE VAL GLY GLY TYR THR CYS GLN GLU ASN SER 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 ASP GLN TRP VAL VAL SER ALA ALA
SEQRES 4 E 223 HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU
SEQRES 5 E 223 HIS ASN ILE ASN VAL LEU GLU GLY ASN GLU GLN PHE VAL
SEQRES 6 E 223 ASN ALA ALA LYS ILE ILE LYS HIS PRO ASN PHE ASP ARG
SEQRES 7 E 223 LYS THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU SER
SEQRES 8 E 223 SER PRO VAL LYS LEU ASN ALA ARG VAL ALA THR VAL ALA
SEQRES 9 E 223 LEU PRO SER SER CYS ALA PRO ALA GLY THR GLN CYS LEU
SEQRES 10 E 223 ILE SER GLY TRP GLY ASN THR LEU SER SER GLY VAL ASN
SEQRES 11 E 223 GLU PRO ASP LEU LEU GLN CYS LEU ASP ALA PRO LEU LEU
SEQRES 12 E 223 PRO GLN ALA ASP CYS GLU ALA SER TYR PRO GLY LYS ILE
SEQRES 13 E 223 THR ASP ASN MET VAL CYS VAL GLY PHE LEU GLU GLY GLY
SEQRES 14 E 223 LYS GLY SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL
SEQRES 15 E 223 CYS ASN GLY GLU LEU GLN GLY ILE VAL SER TRP GLY TYR
SEQRES 16 E 223 GLY CYS ALA LEU PRO ASP ASN PRO ASP VAL TYR THR LYS
SEQRES 17 E 223 VAL CYS ASN TYR VAL ASP TRP ILE GLN ASP THR ILE ALA
SEQRES 18 E 223 ALA ASN
SEQRES 1 I 58 ARG PRO ASP PHE ALA GLY 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 ALA GLY GLY ALA
FORMUL 3 HOH *142(H2 O)
HELIX 1 SHA PRO E 164 TYR E 172 1IRREGULAR AFTER CYS 168 9
HELIX 2 31A LYS E 230 VAL E 235 5LEADS INTO TERMINAL ALPHA-HLX 6
HELIX 3 TEA TYR E 234 ASN E 245 1C-TERMINAL HELIX 12
HELIX 4 H2 SER I 47 ALA I 55 1ALL DONOR, ACCEPTORS INCLUDED 9
SHEET 1 S1A 7 TYR E 20 TYR E 20 0
SHEET 2 S1A 7 GLN E 156 PRO E 161 -1 O CYS E 157 N TYR E 20
SHEET 3 S1A 7 CYS E 136 GLY E 140 -1 O CYS E 136 N ALA E 160
SHEET 4 S1A 7 GLY E 197 CYS E 201 -1 N VAL E 200 O LEU E 137
SHEET 5 S1A 7 GLU E 204 TRP E 215 -1 N VAL E 213 O GLY E 197
SHEET 6 S1A 7 ASP E 226 VAL E 231 -1 N VAL E 227 O TRP E 215
SHEET 7 S1A 7 ASN E 179 VAL E 183 -1 N VAL E 183 O ASP E 226
SHEET 1 S2A 4 GLY E 43 SER E 45 0
SHEET 2 S2A 4 VAL E 52 ALA E 55 -1 N VAL E 53 O SER E 45
SHEET 3 S2A 4 ILE E 103 LYS E 107 -1 O MET E 104 N SER E 54
SHEET 4 S2A 4 LYS E 87 HIS E 91 -1 N HIS E 91 O ILE E 103
SHEET 1 S3A 2 ILE E 63 VAL E 66 0
SHEET 2 S3A 2 GLN E 81 ALA E 85 -1 N GLN E 81 O VAL E 66
SHEET 1 S4 3 LEU I 29 TYR I 35 0
SHEET 2 S4 3 ILE I 18 ASN I 24 -1 N ILE I 18 O TYR I 35
SHEET 3 S4 3 PHE I 45 PHE I 45 -1 N PHE I 45 N TYR I 21
SSBOND 1 CYS E 22 CYS E 157 1555 1555 2.01
SSBOND 2 CYS E 42 CYS E 58 1555 1555 2.00
SSBOND 3 CYS E 128 CYS E 232 1555 1555 2.01
SSBOND 4 CYS E 136 CYS E 201 1555 1555 2.01
SSBOND 5 CYS E 168 CYS E 182 1555 1555 1.99
SSBOND 6 CYS E 191 CYS E 220 1555 1555 1.99
SSBOND 7 CYS I 14 CYS I 38 1555 1555 2.04
SSBOND 8 CYS I 30 CYS I 51 1555 1555 2.00
SITE 1 CAT 3 HIS E 57 ASP E 102 SER E 195
CRYST1 92.650 92.650 62.320 90.00 90.00 120.00 P 32 2 1 6
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 0.010793 0.006232 0.000000 0.00000
SCALE2 0.000000 0.012463 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016046 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
