HEADER HYDROLASE/HYDROLASE INHIBITOR 04-JAN-09 3FP7
TITLE ANIONIC TRYPSIN VARIANT S195A IN COMPLEX WITH BOVINE
TITLE 2 PANCREATIC TRYPSIN INHIBITOR (BPTI) CLEAVED AT THE SCISSILE
TITLE 3 BOND (LYS15-ALA16) DETERMINED TO THE 1.46 A RESOLUTION
TITLE 4 LIMIT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANIONIC TRYPSIN-2;
COMPND 3 CHAIN: E;
COMPND 4 SYNONYM: ANIONIC TRYPSIN II, PRETRYPSINOGEN II, SERINE
COMPND 5 PROTEASE 2;
COMPND 6 EC: 3.4.21.4;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: PANCREATIC TRYPSIN INHIBITOR;
COMPND 11 CHAIN: I;
COMPND 12 SYNONYM: BASIC PROTEASE INHIBITOR, BPTI, BPI, APROTININ;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: PANCREATIC TRYPSIN INHIBITOR;
COMPND 16 CHAIN: J;
COMPND 17 SYNONYM: BASIC PROTEASE INHIBITOR, BPTI, BPI, APROTININ;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: BROWN RAT,RAT,RATS;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: PRSS2, TRY2;
SOURCE 6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: DLM101;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PYT;
SOURCE 12 MOL_ID: 2;
SOURCE 13 SYNTHETIC: YES;
SOURCE 14 OTHER_DETAILS: BOVINE PANCREATIC TRYPSIN INHIBITOR WAS
SOURCE 15 OBTAINED IN ITS HYDROLYZED FORM BY PARTIAL REDUCTION AT THE
SOURCE 16 CYS14-CYS38 DISULFIDE, TREATMENT WITH TRYPSIN, PURIFICATION
SOURCE 17 BY HPLC AND RE-OXIDATION OF THE CYS14-CYS38 DISULFIDE;
SOURCE 18 MOL_ID: 3;
SOURCE 19 SYNTHETIC: YES
KEYWDS ENZYME-INHIBITOR COMPLEX, PEPTIDE BOND HYDROLYSIS, CALCIUM,
KEYWDS 2 DIGESTION, HYDROLASE, METAL-BINDING, PROTEASE, SECRETED,
KEYWDS 3 SERINE PROTEASE, ZYMOGEN, PHARMACEUTICAL, PROTEASE
KEYWDS 4 INHIBITOR, SERINE PROTEASE INHIBITOR, HYDROLASE/HYDROLASE
KEYWDS 5 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.ZAKHAROVA,M.P.HORVATH,D.P.GOLDENBERG
REVDAT 2 18-AUG-09 3FP7 1 JRNL
REVDAT 1 17-FEB-09 3FP7 0
JRNL AUTH E.ZAKHAROVA,M.P.HORVATH,D.P.GOLDENBERG
JRNL TITL STRUCTURE OF A SERINE PROTEASE POISED TO
JRNL TITL 2 RESYNTHESIZE A PEPTIDE BOND.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 106 11034 2009
JRNL REFN ISSN 0027-8424
JRNL PMID 19549826
JRNL DOI 10.1073/PNAS.0902463106
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.46 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS1.2
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) : 1.46
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
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) (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 51811
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, BUT IDENTICAL TO
REMARK 3 THOSE IDENTIFIED FOR PDB
REMARK 3 ENTRY 3FP6
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4131
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) : 1.46
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7774
REMARK 3 BIN R VALUE (WORKING SET) : 0.2012
REMARK 3 BIN FREE R VALUE : 0.2152
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 8.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 687
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 : 2245
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 371
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.10
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) : 0.15
REMARK 3 ESD FROM SIGMAA (A) : 0.07
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) : 0.16
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.09
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.38
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.18
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) : 0.085 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.380 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.300 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 1.870 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : CNS SOLVE
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 33.26
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.PARAM
REMARK 3 PARAMETER FILE 2 : WATER.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : LIGAND.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : LIGAND.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SIMULATED ANNEALING TORSION ANGLE
REMARK 3 REFINEMENT, POSITIONAL REFINEMENT, RESTRAINED ISOTROPIC
REMARK 3 INDIVIDUAL B-VALUE REFINEMENT, COUPLED WITH MODEL ADJUSTMENT
REMARK 3 ON THE BASIS OF SIGMA-A WEIGHTED AND COMPOSITE SIMULATED
REMARK 3 ANNEALING OMIT ELECTRON DENSITY MAPS
REMARK 4
REMARK 4 3FP7 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JAN-09.
REMARK 100 THE RCSB ID CODE IS RCSB050869.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-DEC-07
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.0
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 : NONIUS FR-591 (6 KW)
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC CONFOCAL MAX-FLUX
REMARK 200 (GREEN)
REMARK 200 OPTICS : OSMIC CONFOCAL MAX-FLUX
REMARK 200 (GREEN)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NONIUS KAPPA CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51853
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.460
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 14.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.46
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.51
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.20500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.700
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 3TGI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M LITHIUM SULFATE, 0.1M TRIS,
REMARK 280 34% (W/V) PEG 4000, PH 8.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K
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 40.66733
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 20.33367
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 20.33367
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 40.66733
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 300 REMARK: AUTHORS STATE THAT THE QUATERNARY STRUCTURE IS A
REMARK 300 HETEROTRIMER.
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, I, J
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 E 806 LIES ON A SPECIAL POSITION.
REMARK 375 HOH E 809 LIES ON A SPECIAL POSITION.
REMARK 375 HOH E 843 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 ARG E 62 NE CZ NH1 NH2
REMARK 470 LYS E 113 CD CE NZ
REMARK 470 LYS E 230 CE NZ
REMARK 470 LYS J 26 CG CD CE NZ
REMARK 470 LYS J 46 CD CE NZ
REMARK 470 GLU J 49 CG CD OE1 OE2
REMARK 470 ALA J 58 C O
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 49 -3.91 -57.83
REMARK 500 HIS E 71 -64.17 -127.68
REMARK 500 SER E 214 -72.86 -124.70
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 E 601 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 70 OE1
REMARK 620 2 ASN E 72 O 89.7
REMARK 620 3 VAL E 75 O 161.3 83.8
REMARK 620 4 GLU E 77 OE1 91.9 87.0 105.2
REMARK 620 5 GLU E 80 OE2 102.9 164.7 86.6 84.1
REMARK 620 6 HOH E 907 O 83.0 92.8 114.8 10.7 80.5
REMARK 620 7 HOH E 708 O 78.5 101.4 85.6 167.1 89.6 156.4
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 501
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 502
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 503
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 504
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 E 506
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 601
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO I 505
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 J 602
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 J 603
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 J 604
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 J 605
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3TGI RELATED DB: PDB
REMARK 900 ANIONIC TRYPSIN COMPLEXED WITH BOVINE PANCREATIC TRYPSIN
REMARK 900 INHIBITOR (BPTI) DETERMINED TO THE 1.8 A RESOLUTION LIMIT
REMARK 900 RELATED ID: 3FP6 RELATED DB: PDB
REMARK 900 ANIONIC TRYPSIN IN COMPLEX WITH BPTI DETERMINED TO THE 1.49
REMARK 900 A RESOLUTION LIMIT
REMARK 900 RELATED ID: 3FP8 RELATED DB: PDB
REMARK 900 ANIONIC TRYPSIN VARIANT S195A IN COMPLEX WITH BPTI
REMARK 900 DETERMINED TO THE 1.46 A RESOLUTION LIMIT
DBREF 3FP7 E 16 245 UNP P00763 TRY2_RAT 24 246
DBREF 3FP7 I 1 15 UNP P00974 BPT1_BOVIN 36 50
DBREF 3FP7 J 16 58 UNP P00974 BPT1_BOVIN 51 93
SEQADV 3FP7 ALA E 195 UNP P00763 SER 200 ENGINEERED
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 ASP SER CYS GLN GLY ASP ALA 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 GLY 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 15 ARG PRO ASP PHE CYS LEU GLU PRO PRO TYR THR GLY PRO
SEQRES 2 I 15 CYS LYS
SEQRES 1 J 43 ALA ARG ILE ILE ARG TYR PHE TYR ASN ALA LYS ALA GLY
SEQRES 2 J 43 LEU CYS GLN THR PHE VAL TYR GLY GLY CYS ARG ALA LYS
SEQRES 3 J 43 ARG ASN ASN PHE LYS SER ALA GLU ASP CYS MET ARG THR
SEQRES 4 J 43 CYS GLY GLY ALA
HET EDO E 501 4
HET EDO E 502 4
HET EDO E 503 8
HET EDO E 504 4
HET PG4 E 506 13
HET CA E 601 1
HET EDO I 505 4
HET SO4 J 602 5
HET SO4 J 603 5
HET SO4 J 604 5
HET SO4 J 605 5
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 4 EDO 5(C2 H6 O2)
FORMUL 8 PG4 C8 H18 O5
FORMUL 9 CA CA 2+
FORMUL 11 SO4 4(O4 S 2-)
FORMUL 15 HOH *358(H2 O)
HELIX 1 1 ALA E 55 TYR E 59 5 5
HELIX 2 2 PRO E 164 TYR E 172 1 9
HELIX 3 3 TYR E 234 ASN E 245 1 12
HELIX 4 4 PRO I 2 GLU I 7 5 6
HELIX 5 5 SER J 47 GLY J 56 1 10
SHEET 1 A 7 TYR E 20 THR E 21 0
SHEET 2 A 7 GLN 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 GLU E 204 TRP E 215 -1 O GLU 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 VAL E 183 -1 N VAL 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 MET E 104 N SER E 54
SHEET 5 B 7 GLN E 81 LYS E 90 -1 N ILE E 89 O LEU E 105
SHEET 6 B 7 GLN E 64 LEU E 68 -1 N VAL E 66 O VAL E 83
SHEET 7 B 7 GLN E 30 ASN E 34 -1 N ASN E 34 O GLN E 64
SHEET 1 C 2 ILE J 18 ASN J 24 0
SHEET 2 C 2 LEU J 29 TYR J 35 -1 O TYR J 35 N ILE J 18
SSBOND 1 CYS E 22 CYS E 157 1555 1555 2.03
SSBOND 2 CYS E 42 CYS E 58 1555 1555 2.03
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 2.03
SSBOND 6 CYS E 191 CYS E 220 1555 1555 2.04
SSBOND 7 CYS I 5 CYS J 55 1555 1555 2.03
SSBOND 8 CYS I 14 CYS J 38 1555 1555 2.04
SSBOND 9 CYS J 30 CYS J 51 1555 1555 2.03
LINK OE1 GLU E 70 CA CA E 601 1555 1555 2.26
LINK O ASN E 72 CA CA E 601 1555 1555 2.30
LINK O VAL E 75 CA CA E 601 1555 1555 2.27
LINK OE1AGLU E 77 CA CA E 601 1555 1555 2.43
LINK OE2 GLU E 80 CA CA E 601 1555 1555 2.32
LINK CA CA E 601 O BHOH E 907 1555 1555 2.33
LINK CA CA E 601 O HOH E 708 1555 1555 2.30
SITE 1 AC1 9 ASN E 34 GLY E 38 TYR E 39 HIS E 40
SITE 2 AC1 9 ARG E 67 ILE E 73 ASN E 74 HOH E 794
SITE 3 AC1 9 HOH E 843
SITE 1 AC2 7 ILE E 47 ASN E 48 LEU E 123 GLN E 239
SITE 2 AC2 7 ILE E 242 HOH E 793 HOH E 830
SITE 1 AC3 10 LYS E 97 THR E 98 LYS E 175 TYR E 217
SITE 2 AC3 10 HOH E 799 HOH E 818 HOH E 927 HOH E 961
SITE 3 AC3 10 PRO I 13 ARG J 39
SITE 1 AC4 10 GLY E 216 TYR E 217 GLY E 219 ASP I 3
SITE 2 AC4 10 TYR I 10 GLY I 12 EDO I 505 HOH I 707
SITE 3 AC4 10 HOH I 709 HOH I 723
SITE 1 AC5 7 GLY E 18 PHE E 184A GLU E 186 GLY E 187
SITE 2 AC5 7 GLY E 188 LYS E 188A HOH E 739
SITE 1 AC6 7 GLU E 70 ASN E 72 VAL E 75 GLU E 77
SITE 2 AC6 7 GLU E 80 HOH E 708 HOH E 907
SITE 1 AC7 6 EDO E 504 ASP I 3 PHE I 4 TYR I 10
SITE 2 AC7 6 LYS J 41 SO4 J 603
SITE 1 AC8 9 HOH E 808 ARG J 20 TYR J 35 GLY J 37
SITE 2 AC8 9 ALA J 40 HOH J 711 HOH J 717 HOH J 719
SITE 3 AC8 9 HOH J 735
SITE 1 AC9 7 EDO I 505 LYS J 41 ARG J 42 HOH J 703
SITE 2 AC9 7 HOH J 708 HOH J 731 HOH J 746
SITE 1 BC1 4 LYS E 175 HOH I 711 ARG J 39 ARG J 42
SITE 1 BC2 6 ILE J 18 ILE J 19 ARG J 20 HOH J 745
SITE 2 BC2 6 HOH J 748 HOH J 749
CRYST1 91.969 91.969 61.001 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 0.010873 0.006278 0.000000 0.00000
SCALE2 0.000000 0.012555 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016393 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
