HEADER HYDROLASE 11-MAY-07 2PWA
TITLE CRYSTAL STRUCTURE OF THE COMPLEX OF PROTEINASE K WITH
TITLE 2 ALANINE BORONIC ACID AT 0.83A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEINASE K;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PROTEINASE K;
COMPND 5 SYNONYM: TRITIRACHIUM ALKALINE PROTEINASE, ENDOPEPTIDASE K;
COMPND 6 EC: 3.4.21.64
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENGYODONTIUM ALBUM;
SOURCE 3 ORGANISM_TAXID: 37998
KEYWDS STRUCTURE, PROTEINASE K, ALANINE BORONIC ACID, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.JAIN,N.SINGH,M.PERBANDT,C.BETZEL,S.SHARMA,P.KAUR,
AUTHOR 2 A.SRINIVASAN,T.P.SINGH
REVDAT 2 24-FEB-09 2PWA 1 VERSN
REVDAT 1 29-MAY-07 2PWA 0
JRNL AUTH R.JAIN,N.SINGH,M.PERBANDT,C.BETZEL,S.SHARMA,P.KAUR,
JRNL AUTH 2 A.SRINIVASAN,T.P.SINGH
JRNL TITL CRYSTAL STRUCTURE OF THE COMPLEX OF PROTEINASE K
JRNL TITL 2 WITH ALANINE BORONIC ACID AT 0.83A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 0.83 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 0.83
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.120
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.120
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.136
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 1.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 2215
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 220399
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.108
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.108
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.121
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 1.000
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 1923
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 189749
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2118
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 54
REMARK 3 SOLVENT ATOMS : 535
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2651.40
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 1957.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 24
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 24726
REMARK 3 NUMBER OF RESTRAINTS : 29442
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.021
REMARK 3 ANGLE DISTANCES (A) : 0.055
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.032
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.099
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.108
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.130
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.006
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.043
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.109
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ANISOTROPIC REFINEMENT REDUCED FREE
REMARK 3 R (NO CUTOFF) BY ?
REMARK 4
REMARK 4 2PWA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAY-07.
REMARK 100 THE RCSB ID CODE IS RCSB042845.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-NOV-06
REMARK 200 TEMPERATURE (KELVIN) : 277
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91
REMARK 200 MONOCHROMATOR : MIRROR
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 220399
REMARK 200 RESOLUTION RANGE HIGH (A) : 0.830
REMARK 200 RESOLUTION RANGE LOW (A) : 56.890
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : 27.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 40.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.83
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 0.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.05440
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: AB INITIO
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CACL2 & NANO3,ALANINE BORONIC ACID,
REMARK 280 PH 6.5, VAPOR DIFFUSION, TEMPERATURE 295K, PH 6.50, VAPOR
REMARK 280 DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 53.25300
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 33.65100
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 33.65100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 79.87950
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 33.65100
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 33.65100
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 26.62650
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 33.65100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 33.65100
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 79.87950
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 33.65100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 33.65100
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 26.62650
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 53.25300
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 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 A 46 NE2 HIS A 46 CD2 -0.069
REMARK 500 SER A 143 CB SER A 143 OG -0.097
REMARK 500 ARG A 185 CD ARG A 185 NE -0.138
REMARK 500 ARG A 185 NE ARG A 185 CZ -0.165
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 TYR A 24 N - CA - CB ANGL. DEV. = 13.4 DEGREES
REMARK 500 TYR A 60 CG - CD2 - CE2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 GLN A 103 CA - CB - CG ANGL. DEV. = 22.1 DEGREES
REMARK 500 ARG A 185 CG - CD - NE ANGL. DEV. = 15.4 DEGREES
REMARK 500 ARG A 185 CD - NE - CZ ANGL. DEV. = 15.2 DEGREES
REMARK 500 ARG A 185 NE - CZ - NH1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG A 185 NE - CZ - NH1 ANGL. DEV. = -7.9 DEGREES
REMARK 500 ARG A 188 NE - CZ - NH1 ANGL. DEV. = 17.9 DEGREES
REMARK 500 ARG A 188 NE - CZ - NH2 ANGL. DEV. = -12.6 DEGREES
REMARK 500 ARG A 250 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 TYR A 277 CB - CG - CD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 TYR A 277 CB - CG - CD1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 TYR A 277 CB - CG - CD1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 TYR A 277 CD1 - CE1 - CZ ANGL. DEV. = 5.5 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 ASP A 39 -147.93 -167.31
REMARK 500 ASP A 207 61.05 60.82
REMARK 500 ASN A 270 75.24 -109.20
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 A1280 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PRO A 175 O
REMARK 620 2 VAL A 177 O 89.1
REMARK 620 3 ASP A 200 OD1 150.6 112.4
REMARK 620 4 ASP A 200 OD2 158.0 78.6 51.0
REMARK 620 5 HOH A5005 O 79.8 75.1 123.8 79.4
REMARK 620 6 HOH A5010 O 95.6 149.2 76.3 86.3 75.8
REMARK 620 7 HOH A5023 O 89.6 71.9 79.1 103.5 145.4 138.4
REMARK 620 8 HOH A5026 O 75.8 137.2 74.8 125.3 137.9 73.1 68.3
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1280
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 3001
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 3002
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 3003
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 3004
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 3005
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 3006
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 3007
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 3008
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 3009
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 4001
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B2A A 2001
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B2A A 2002
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IC6 RELATED DB: PDB
REMARK 900 STRUCTURE OF A SERINE PROTEASE PROTEINASE K FROMT
REMARK 900 TRITIRACHIUM ALBUM LIMBER AT 0.98A RESOLUTION
REMARK 900 RELATED ID: 2PWB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF PROTEINASE K WITH
REMARK 900 COUMARIN AT 1.9 A RESOLUTION
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AMINO ACID 207 WAS MUTATED BY PERSUING ELECTRON
REMARK 999 DENSITY AT ATOMIC RESOLUTION AND AFTER REPEATION
REMARK 999 OF MANY REFINEMENT CYCLE.
DBREF 2PWA A 1 279 UNP P06873 PRTK_TRIAL 106 384
SEQADV 2PWA ASP A 207 UNP P06873 SER 312 SEE REMARK 999
SEQRES 1 A 279 ALA ALA GLN THR ASN ALA PRO TRP GLY LEU ALA ARG ILE
SEQRES 2 A 279 SER SER THR SER PRO GLY THR SER THR TYR TYR TYR ASP
SEQRES 3 A 279 GLU SER ALA GLY GLN GLY SER CYS VAL TYR VAL ILE ASP
SEQRES 4 A 279 THR GLY ILE GLU ALA SER HIS PRO GLU PHE GLU GLY ARG
SEQRES 5 A 279 ALA GLN MET VAL LYS THR TYR TYR TYR SER SER ARG ASP
SEQRES 6 A 279 GLY ASN GLY HIS GLY THR HIS CYS ALA GLY THR VAL GLY
SEQRES 7 A 279 SER ARG THR TYR GLY VAL ALA LYS LYS THR GLN LEU PHE
SEQRES 8 A 279 GLY VAL LYS VAL LEU ASP ASP ASN GLY SER GLY GLN TYR
SEQRES 9 A 279 SER THR ILE ILE ALA GLY MET ASP PHE VAL ALA SER ASP
SEQRES 10 A 279 LYS ASN ASN ARG ASN CYS PRO LYS GLY VAL VAL ALA SER
SEQRES 11 A 279 LEU SER LEU GLY GLY GLY TYR SER SER SER VAL ASN SER
SEQRES 12 A 279 ALA ALA ALA ARG LEU GLN SER SER GLY VAL MET VAL ALA
SEQRES 13 A 279 VAL ALA ALA GLY ASN ASN ASN ALA ASP ALA ARG ASN TYR
SEQRES 14 A 279 SER PRO ALA SER GLU PRO SER VAL CYS THR VAL GLY ALA
SEQRES 15 A 279 SER ASP ARG TYR ASP ARG ARG SER SER PHE SER ASN TYR
SEQRES 16 A 279 GLY SER VAL LEU ASP ILE PHE GLY PRO GLY THR ASP ILE
SEQRES 17 A 279 LEU SER THR TRP ILE GLY GLY SER THR ARG SER ILE SER
SEQRES 18 A 279 GLY THR SER MET ALA THR PRO HIS VAL ALA GLY LEU ALA
SEQRES 19 A 279 ALA TYR LEU MET THR LEU GLY LYS THR THR ALA ALA SER
SEQRES 20 A 279 ALA CYS ARG TYR ILE ALA ASP THR ALA ASN LYS GLY ASP
SEQRES 21 A 279 LEU SER ASN ILE PRO PHE GLY THR VAL ASN LEU LEU ALA
SEQRES 22 A 279 TYR ASN ASN TYR GLN ALA
HET CA A1280 1
HET NO3 A3001 4
HET NO3 A3002 4
HET NO3 A3003 4
HET NO3 A3004 4
HET NO3 A3005 4
HET NO3 A3006 4
HET NO3 A3007 4
HET NO3 A3008 4
HET NO3 A3009 4
HET SO4 A4001 5
HET B2A A2001 6
HET B2A A2002 6
HETNAM CA CALCIUM ION
HETNAM NO3 NITRATE ION
HETNAM SO4 SULFATE ION
HETNAM B2A ALANINE BORONIC ACID
FORMUL 2 CA CA 2+
FORMUL 3 NO3 9(N O3 1-)
FORMUL 12 SO4 O4 S 2-
FORMUL 13 B2A 2(C2 H8 B N O2)
FORMUL 14 HOH *535(H2 O)
HELIX 1 1 PRO A 7 SER A 14 1 8
HELIX 2 2 HIS A 46 GLU A 50 5 5
HELIX 3 3 GLY A 68 SER A 79 1 12
HELIX 4 4 GLN A 103 LYS A 118 1 16
HELIX 5 5 ASN A 119 ARG A 121 5 3
HELIX 6 6 SER A 138 SER A 151 1 14
HELIX 7 7 ASP A 165 ARG A 167 5 3
HELIX 8 8 GLY A 222 LEU A 240 1 19
HELIX 9 9 SER A 247 ALA A 256 1 10
SHEET 1 A 2 ALA A 2 GLN A 3 0
SHEET 2 A 2 TYR A 23 TYR A 24 -1 O TYR A 23 N GLN A 3
SHEET 1 B 7 ALA A 53 THR A 58 0
SHEET 2 B 7 GLN A 89 LYS A 94 1 O GLY A 92 N VAL A 56
SHEET 3 B 7 SER A 33 ASP A 39 1 N VAL A 35 O GLN A 89
SHEET 4 B 7 GLY A 126 LEU A 131 1 O VAL A 128 N TYR A 36
SHEET 5 B 7 VAL A 153 ALA A 158 1 O MET A 154 N ALA A 129
SHEET 6 B 7 CYS A 178 SER A 183 1 O CYS A 178 N VAL A 157
SHEET 7 B 7 ILE A 201 PRO A 204 1 O ILE A 201 N GLY A 181
SHEET 1 C 2 GLY A 135 GLY A 136 0
SHEET 2 C 2 TYR A 169 SER A 170 -1 O SER A 170 N GLY A 135
SHEET 1 D 2 ILE A 208 TRP A 212 0
SHEET 2 D 2 SER A 216 ILE A 220 -1 O ILE A 220 N ILE A 208
SHEET 1 E 2 ASN A 257 LYS A 258 0
SHEET 2 E 2 LEU A 271 LEU A 272 -1 O LEU A 272 N ASN A 257
SSBOND 1 CYS A 34 CYS A 123 1555 1555 2.02
SSBOND 2 CYS A 178 CYS A 249 1555 1555 2.04
LINK O PRO A 175 CA CA A1280 1555 1555 2.38
LINK O VAL A 177 CA CA A1280 1555 1555 2.37
LINK OD1 ASP A 200 CA CA A1280 1555 1555 2.62
LINK OD2 ASP A 200 CA CA A1280 1555 1555 2.43
LINK CA CA A1280 O HOH A5005 1555 1555 2.40
LINK CA CA A1280 O HOH A5010 1555 1555 2.41
LINK CA CA A1280 O HOH A5023 1555 1555 2.41
LINK CA CA A1280 O HOH A5026 1555 1555 2.48
CISPEP 1 SER A 170 PRO A 171 0 2.18
SITE 1 AC1 7 PRO A 175 VAL A 177 ASP A 200 HOH A5005
SITE 2 AC1 7 HOH A5010 HOH A5023 HOH A5026
SITE 1 AC2 8 ALA A 1 ALA A 2 TYR A 24 LYS A 57
SITE 2 AC2 8 ASN A 120 TYR A 277 HOH A5192 HOH A5408
SITE 1 AC3 8 ASP A 184 TYR A 186 ARG A 188 THR A 244
SITE 2 AC3 8 HOH A5100 HOH A5224 HOH A5346 HOH A5487
SITE 1 AC4 7 TYR A 104 SER A 105 ILE A 108 SER A 140
SITE 2 AC4 7 HOH A5099 HOH A5299 HOH A5306
SITE 1 AC5 7 TYR A 60 TYR A 61 LYS A 94 ASP A 97
SITE 2 AC5 7 ASP A 98 HOH A5022 HOH A5442
SITE 1 AC6 7 LYS A 118 VAL A 127 GLY A 152 HOH A5039
SITE 2 AC6 7 HOH A5111 HOH A5291 HOH A5307
SITE 1 AC7 6 SER A 191 ALA A 246 SER A 247 ARG A 250
SITE 2 AC7 6 HOH A5270 HOH A5500
SITE 1 AC8 9 SER A 101 GLY A 102 TYR A 104 ILE A 107
SITE 2 AC8 9 LEU A 133 GLY A 134 HOH A5250 HOH A5385
SITE 3 AC8 9 HOH A5455
SITE 1 AC9 7 ARG A 64 ASP A 165 ARG A 167 ASN A 168
SITE 2 AC9 7 GLY A 214 HOH A5485 HOH A5489
SITE 1 BC1 6 PRO A 124 LYS A 125 HOH A5249 HOH A5295
SITE 2 BC1 6 HOH A5314 HOH A5322
SITE 1 BC2 12 MET A 55 VAL A 56 LYS A 57 THR A 58
SITE 2 BC2 12 SER A 63 HOH A5066 HOH A5143 HOH A5285
SITE 3 BC2 12 HOH A5297 HOH A5309 HOH A5407 HOH A5511
SITE 1 BC3 10 LEU A 133 GLY A 134 ALA A 158 GLY A 160
SITE 2 BC3 10 ASN A 161 THR A 223 SER A 224 B2A A2002
SITE 3 BC3 10 HOH A5028 HOH A5458
SITE 1 BC4 9 HIS A 69 ASN A 161 ILE A 220 SER A 221
SITE 2 BC4 9 GLY A 222 SER A 224 MET A 225 B2A A2001
SITE 3 BC4 9 HOH A5349
CRYST1 67.302 67.302 106.506 90.00 90.00 90.00 P 43 21 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 0.014858 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014858 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009389 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
