HEADER HYDROLASE 05-AUG-12 4B5L
TITLE THE 1.6 A HIGH ENERGY ROOM TEMPERATURE STRUCTURE OF PROTEINASE K AT
TITLE 2 38.4 KEV AND 0.04 MGY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEINASE K;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ENDOPEPTIDASE K, TRITIRACHIUM ALKALINE PROTEINASE;
COMPND 5 EC: 3.4.21.64
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENGYODONTIUM ALBUM;
SOURCE 3 ORGANISM_TAXID: 37998
KEYWDS HYDROLASE, LOW MOSAICITY
EXPDTA X-RAY DIFFRACTION
AUTHOR J.JAKONCIC
REVDAT 4 20-DEC-23 4B5L 1 REMARK LINK
REVDAT 3 06-FEB-19 4B5L 1 REMARK
REVDAT 2 30-JAN-19 4B5L 1 REMARK
REVDAT 1 15-AUG-12 4B5L 0
JRNL AUTH J.JAKONCIC,V.STOJANOFF,V.HONKIMAKI
JRNL TITL HIGH ENERGY MACROMOLECULAR CRYSTALLOGRAPHY ENABLES DATA
JRNL TITL 2 COLLECTION AT ROOM TEMPERATURE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 32791
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
REMARK 3 R VALUE (WORKING + TEST SET) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.184
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1741
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2148
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.69
REMARK 3 BIN R VALUE (WORKING SET) : 0.2260
REMARK 3 BIN FREE R VALUE SET COUNT : 107
REMARK 3 BIN FREE R VALUE : 0.2570
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2032
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 133
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.04000
REMARK 3 B22 (A**2) : -0.04000
REMARK 3 B33 (A**2) : 0.08000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.078
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.078
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.047
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.352
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.960
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2122 ; 0.013 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2899 ; 1.460 ; 1.938
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 296 ; 5.768 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 87 ;36.292 ;23.448
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 312 ;11.791 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;18.859 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 322 ; 0.108 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1656 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. U VALUES REFINED INDIVIDUALLY.
REMARK 4
REMARK 4 4B5L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-AUG-12.
REMARK 100 THE DEPOSITION ID IS D_1290053628.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-NOV-11
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID15C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.328
REMARK 200 MONOCHROMATOR : SINGLE BOUNCE LAUE SI(111)
REMARK 200 CYLINDRICALLY BENT CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34541
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 11.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.13000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.1000
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) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.82000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3Q5G
REMARK 200
REMARK 200 REMARK: DATA COLLECTED AT ROOM TEMPERATURE AT 0.328 A WAVELENGTH.
REMARK 200 THE SAMPLE RECEIVED 0.04 MGY DOSE AND DID NOT DECAY AS JUDGED BY
REMARK 200 SUBSEQUENT DATA COLLECTED.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 UL OF 40 MG/ML PROTEIN IN DH2O MIXED
REMARK 280 WITH 1 MUL OF THE MOTHER LIQUOR. MOTHER LIQUOR 400 MM AMMONIUM
REMARK 280 SO4, 25% GLYCEROL, 100 MM NA CACODYLATE PH 6.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
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 54.18750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 34.26900
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 34.26900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 81.28125
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 34.26900
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 34.26900
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 27.09375
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 34.26900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 34.26900
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 81.28125
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 34.26900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.26900
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 27.09375
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 54.18750
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 69 CG HIS A 69 CD2 0.059
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 -146.15 -169.01
REMARK 500 SER A 216 -168.68 -115.61
REMARK 500 SER A 216 -168.84 -115.43
REMARK 500 ASN A 270 78.38 -108.47
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 85.7
REMARK 620 3 ASP A 200 OD1 151.3 115.4
REMARK 620 4 ASP A 200 OD2 158.3 81.6 50.1
REMARK 620 5 HOH A2087 O 81.1 74.9 121.8 78.7
REMARK 620 6 HOH A2089 O 90.3 72.2 79.0 102.4 146.5
REMARK 620 7 HOH A2090 O 76.1 139.4 75.3 124.5 135.2 72.0
REMARK 620 8 HOH A2091 O 92.8 148.4 79.1 89.0 73.7 139.4 69.5
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 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BJR RELATED DB: PDB
REMARK 900 COMPLEX FORMED BETWEEN PROTEOLYTICALLY GENERATEDLACTOFERRIN
REMARK 900 FRAGMENT AND PROTEINASE K
REMARK 900 RELATED ID: 1CNM RELATED DB: PDB
REMARK 900 ENHANCEMENT OF CATALYTIC EFFICIENCY OF PROTEINASE K THROUGHEXPOSURE
REMARK 900 TO ANHYDROUS ORGANIC SOLVENT AT 70 DEGREES CELSIUS
REMARK 900 RELATED ID: 1EGQ RELATED DB: PDB
REMARK 900 ENHANCEMENT OF ENZYME ACTIVITY THROUGH THREE- PHASEPARTITIONING:
REMARK 900 CRYSTAL STRUCTURE OF A MODIFIED SERINEPROTEINASE AT 1.5 A RESOLUTION
REMARK 900 RELATED ID: 1HT3 RELATED DB: PDB
REMARK 900 MERCURY INDUCED MODIFICATIONS IN THE STEREOCHEMISTRY OF THEACTIVE
REMARK 900 SITE THROUGH CYS-73 IN A SERINE PROTEASE: CRYSTALSTRUCTURE OF THE
REMARK 900 COMPLEX OF A PARTIALLY MODIFIEDPROTEINASE K WITH MERCURY AT 1.8 A
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1IC6 RELATED DB: PDB
REMARK 900 STRUCTURE OF A SERINE PROTEASE PROTEINASE K FROMTRITIRACHIUM ALBUM
REMARK 900 LIMBER AT 0.98 A RESOLUTION
REMARK 900 RELATED ID: 1OYO RELATED DB: PDB
REMARK 900 REGULATION OF PROTEASE ACTIVITY BY MELANIN: CRYSTALSTRUCTURE OF THE
REMARK 900 COMPLEX FORMED BETWEEN PROTEINASE K ANDMELANIN MONOMERS AT 2.0
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1P7V RELATED DB: PDB
REMARK 900 STRUCTURE OF A COMPLEX FORMED BETWEEN PROTEINASE K AND ADESIGNED
REMARK 900 HEPTAPEPTIDE INHIBITOR PRO-ALA-PRO-PHE-ALA- ALA-ALA AT ATOMIC
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1P7W RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF PROTEINASE K WITH ADESIGNED
REMARK 900 HEPTAPEPTIDE INHIBITOR PRO-ALA-PRO-PHE-ALA- SER-ALA AT ATOMIC
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1PEK RELATED DB: PDB
REMARK 900 RELATED ID: 1PFG RELATED DB: PDB
REMARK 900 STRATEGY TO DESIGN INHIBITORS: STRUCTURE OF A COMPLEX OFPROTEINASE
REMARK 900 K WITH A DESIGNED OCTAPEPTIDE INHIBITOR N- AC-PRO-ALA-PRO-PHE-DALA-
REMARK 900 ALA-ALA-ALA-NH2 AT 2. 5A RESOLUTION
REMARK 900 RELATED ID: 1PJ8 RELATED DB: PDB
REMARK 900 STRUCTURE OF A TERNARY COMPLEX OF PROTEINASE K, MERCURY ANDA
REMARK 900 SUBSTRATE-ANALOGUE HEXAPEPTIDE AT 2.2 A RESOLUTION
REMARK 900 RELATED ID: 1PTK RELATED DB: PDB
REMARK 900 RELATED ID: 2DP4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN PROTEINASEK AND A
REMARK 900 HUMAN LACTOFERRIN FRAGMENT AT 2.9 A RESOLUTION
REMARK 900 RELATED ID: 2DQK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF PROTEINASE K WITH ASPECIFIC
REMARK 900 LACTOFERRIN PEPTIDE VAL-LEU-LEU-HIS AT 1. 93 ARESOLUTION
REMARK 900 RELATED ID: 2HD4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROTEINASE K INHIBITED BY ALACTOFERRIN
REMARK 900 OCTAPEPTIDE GLY-ASP-GLU-GLN-GLY-GLU-ASN- LYS AT2.15 A RESOLUTION
REMARK 900 RELATED ID: 2PKC RELATED DB: PDB
REMARK 900 RELATED ID: 2PRK RELATED DB: PDB
REMARK 900 RELATED ID: 2V8B RELATED DB: PDB
REMARK 900 SAD STRUCTURE SOLUTION OF PROTEINASE K GROWN IN SELENATE SOLUTION
REMARK 900 RELATED ID: 3PRK RELATED DB: PDB
DBREF 4B5L A 1 279 UNP P06873 PRTK_TRIAL 106 384
SEQADV 4B5L ASP A 207 UNP P06873 SER 312 CONFLICT
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
HETNAM CA CALCIUM ION
FORMUL 2 CA CA 2+
FORMUL 3 HOH *133(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 GLY A 222 LEU A 240 1 19
HELIX 8 8 SER A 247 THR A 255 1 9
SHEET 1 AA 2 ALA A 2 GLN A 3 0
SHEET 2 AA 2 TYR A 23 TYR A 24 -1 O TYR A 23 N GLN A 3
SHEET 1 AB 7 ALA A 53 THR A 58 0
SHEET 2 AB 7 GLN A 89 LYS A 94 1 O LEU A 90 N GLN A 54
SHEET 3 AB 7 SER A 33 ASP A 39 1 O SER A 33 N GLN A 89
SHEET 4 AB 7 GLY A 126 LEU A 131 1 O GLY A 126 N CYS A 34
SHEET 5 AB 7 MET A 154 ALA A 158 1 O MET A 154 N ALA A 129
SHEET 6 AB 7 CYS A 178 SER A 183 1 O CYS A 178 N VAL A 157
SHEET 7 AB 7 ILE A 201 PRO A 204 1 O ILE A 201 N GLY A 181
SHEET 1 AC 2 GLY A 135 GLY A 136 0
SHEET 2 AC 2 TYR A 169 SER A 170 -1 O SER A 170 N GLY A 135
SHEET 1 AD 2 ILE A 208 TRP A 212 0
SHEET 2 AD 2 SER A 216 ILE A 220 -1 O SER A 216 N TRP A 212
SHEET 1 AE 2 ASN A 257 LYS A 258 0
SHEET 2 AE 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 2.02
LINK O PRO A 175 CA CA A1280 1555 1555 2.36
LINK O VAL A 177 CA CA A1280 1555 1555 2.42
LINK OD1 ASP A 200 CA CA A1280 1555 1555 2.72
LINK OD2 ASP A 200 CA CA A1280 1555 1555 2.41
LINK CA CA A1280 O HOH A2087 1555 1555 2.48
LINK CA CA A1280 O HOH A2089 1555 1555 2.47
LINK CA CA A1280 O HOH A2090 1555 1555 2.60
LINK CA CA A1280 O HOH A2091 1555 1555 2.50
CISPEP 1 SER A 170 PRO A 171 0 -0.38
SITE 1 AC1 7 PRO A 175 VAL A 177 ASP A 200 HOH A2087
SITE 2 AC1 7 HOH A2089 HOH A2090 HOH A2091
CRYST1 68.538 68.538 108.375 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 0.014590 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014590 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009227 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
