HEADER HYDROLASE 21-OCT-98 7PCK
TITLE CRYSTAL STRUCTURE OF WILD TYPE HUMAN PROCATHEPSIN K
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (PROCATHEPSIN K);
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.4.22.38
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS HYDROLASE (THIOL PROTEASE), PROCATHEPSIN K, CYSTEINE PROTEASES,
KEYWDS 2 PROREGION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.SIVARAMAN,M.LALUMIERE,R.MENARD,M.CYGLER
REVDAT 4 20-SEP-23 7PCK 1 REMARK
REVDAT 3 29-JAN-20 7PCK 1 REMARK
REVDAT 2 24-FEB-09 7PCK 1 VERSN
REVDAT 1 25-OCT-99 7PCK 0
JRNL AUTH J.SIVARAMAN,M.LALUMIERE,R.MENARD,M.CYGLER
JRNL TITL CRYSTAL STRUCTURE OF WILD-TYPE HUMAN PROCATHEPSIN K.
JRNL REF PROTEIN SCI. V. 8 283 1999
JRNL REFN ISSN 0961-8368
JRNL PMID 10048321
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.843
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.0
REMARK 3 NUMBER OF REFLECTIONS : 20997
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1230
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 : 9305
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
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) : 0.00
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) : 0.041
REMARK 3 BOND ANGLES (DEGREES) : 2.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.75
REMARK 3 IMPROPER ANGLES (DEGREES) : 4.561
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 : RESTRAINTS
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : 1.5 ; 300
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7PCK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-99.
REMARK 100 THE DEPOSITION ID IS D_1000007322.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-AUG-97
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
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 : 21801
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 8.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.2
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 68.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.26000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1CJL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL, 5% 2-METHYL-2,4
REMARK 280 -PENTANEDIOL, 12 MM AMMONIUM SULPHATE AND 9% PEG, PH 7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
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 42.20000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 1560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
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 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 -0.81472
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -42.20000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 155.59787
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 1650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 57.88528
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -42.20000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 155.59787
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 SER B 83P
REMARK 465 HIS B 84P
REMARK 465 SER B 85P
REMARK 465 SER C 83P
REMARK 465 HIS C 84P
REMARK 465 SER C 85P
REMARK 465 ARG C 86P
REMARK 465 SER C 87P
REMARK 465 PRO D 81P
REMARK 465 LEU D 82P
REMARK 465 SER D 83P
REMARK 465 HIS D 84P
REMARK 465 SER D 85P
REMARK 465 ARG D 86P
REMARK 465 SER D 87P
REMARK 465 ASN D 88P
REMARK 465 ASP D 89P
REMARK 465 THR D 90P
REMARK 465 PRO D 94P
REMARK 465 GLU D 95P
REMARK 465 TRP D 96P
REMARK 465 GLU D 97P
REMARK 465 GLY D 98P
REMARK 465 ARG D 99P
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 TYR A 2P CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 5P CG CD OE1 OE2
REMARK 470 LYS A 16P CG CD CE NZ
REMARK 470 ARG A 19P CG CD NE CZ NH1 NH2
REMARK 470 GLN A 21P CG CD OE1 NE2
REMARK 470 GLU A 69P CG CD OE1 OE2
REMARK 470 HIS A 84P CG ND1 CD2 CE1 NE2
REMARK 470 SER A 85P OG
REMARK 470 ARG A 86P CG CD NE CZ NH1 NH2
REMARK 470 SER A 87P OG
REMARK 470 ASP A 89P CG OD1 OD2
REMARK 470 THR A 90P OG1 CG2
REMARK 470 LEU A 91P CG CD1 CD2
REMARK 470 TYR A 92P CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TRP A 96P CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 96P CZ3 CH2
REMARK 470 GLU A 97P CG CD OE1 OE2
REMARK 470 LYS A 44 CG CD CE NZ
REMARK 470 TYR A 67 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 79 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 92 CG CD OE1 NE2
REMARK 470 LYS A 119 CG CD CE NZ
REMARK 470 ARG A 123 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 127 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 153 CG CD OE1 OE2
REMARK 470 LYS A 191 CG CD CE NZ
REMARK 470 ASN A 201 CG OD1 ND2
REMARK 470 TYR B 2P CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 4P CG CD OE1 OE2
REMARK 470 GLU B 5P CG CD OE1 OE2
REMARK 470 LYS B 16P CG CD CE NZ
REMARK 470 ARG B 19P CG CD NE CZ NH1 NH2
REMARK 470 GLN B 21P CG CD OE1 NE2
REMARK 470 GLU B 69P CG CD OE1 OE2
REMARK 470 LYS B 79P CG CD CE NZ
REMARK 470 LEU B 82P CG CD1 CD2
REMARK 470 SER B 87P OG
REMARK 470 ASP B 89P CG OD1 OD2
REMARK 470 TYR B 92P CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 95P CG CD OE1 OE2
REMARK 470 TRP B 96P CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 96P CZ3 CH2
REMARK 470 LYS B 44 CG CD CE NZ
REMARK 470 TYR B 67 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG B 79 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 92 CG CD OE1 NE2
REMARK 470 LYS B 119 CG CD CE NZ
REMARK 470 ARG B 123 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 127 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 153 CG CD OE1 OE2
REMARK 470 LYS B 191 CG CD CE NZ
REMARK 470 ASN B 201 CG OD1 ND2
REMARK 470 LEU C 1P CG CD1 CD2
REMARK 470 TYR C 2P CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU C 4P CG CD OE1 OE2
REMARK 470 GLU C 5P CG CD OE1 OE2
REMARK 470 LYS C 16P CG CD CE NZ
REMARK 470 ARG C 19P CG CD NE CZ NH1 NH2
REMARK 470 GLN C 21P CG CD OE1 NE2
REMARK 470 ASN C 23P CG OD1 ND2
REMARK 470 ASN C 24P CG OD1 ND2
REMARK 470 LYS C 25P CG CD CE NZ
REMARK 470 GLU C 69P CG CD OE1 OE2
REMARK 470 LYS C 79P CG CD CE NZ
REMARK 470 GLU C 95P CG CD OE1 OE2
REMARK 470 GLU C 97P CG CD OE1 OE2
REMARK 470 ARG C 99P CG CD NE CZ NH1 NH2
REMARK 470 LYS C 44 CG CD CE NZ
REMARK 470 TYR C 67 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG C 79 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 92 CG CD OE1 NE2
REMARK 470 LYS C 119 CG CD CE NZ
REMARK 470 ARG C 123 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 127 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 153 CG CD OE1 OE2
REMARK 470 LYS C 191 CG CD CE NZ
REMARK 470 ASN C 201 CG OD1 ND2
REMARK 470 LEU D 1P CG CD1 CD2
REMARK 470 TYR D 2P CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU D 4P CG CD OE1 OE2
REMARK 470 LYS D 16P CG CD CE NZ
REMARK 470 ARG D 19P CG CD NE CZ NH1 NH2
REMARK 470 GLN D 21P CG CD OE1 NE2
REMARK 470 ASN D 23P CG OD1 ND2
REMARK 470 ASN D 24P CG OD1 ND2
REMARK 470 LYS D 25P CG CD CE NZ
REMARK 470 GLU D 69P CG CD OE1 OE2
REMARK 470 LEU D 91P CG CD1 CD2
REMARK 470 LYS D 44 CG CD CE NZ
REMARK 470 TYR D 67 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG D 79 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 92 CG CD OE1 NE2
REMARK 470 LYS D 119 CG CD CE NZ
REMARK 470 ARG D 123 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 127 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 153 CG CD OE1 OE2
REMARK 470 LYS D 191 CG CD CE NZ
REMARK 470 ASN D 201 CG OD1 ND2
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 MET A 60P CG - SD - CE ANGL. DEV. = 9.8 DEGREES
REMARK 500 MET B 60P CG - SD - CE ANGL. DEV. = 9.8 DEGREES
REMARK 500 MET C 60P CG - SD - CE ANGL. DEV. = 9.7 DEGREES
REMARK 500 MET D 60P CG - SD - CE ANGL. DEV. = 9.8 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 TYR A 2P 118.80 72.52
REMARK 500 GLU A 5P -16.82 -47.36
REMARK 500 ASN A 61P -168.16 -126.45
REMARK 500 THR A 76P -109.35 -115.00
REMARK 500 LEU A 82P -27.84 78.94
REMARK 500 SER A 83P 85.12 -151.96
REMARK 500 SER A 85P 159.51 79.52
REMARK 500 SER A 87P -176.96 94.62
REMARK 500 ASP A 89P 47.36 -163.16
REMARK 500 TYR A 92P 102.81 170.64
REMARK 500 PRO A 94P 75.71 -104.36
REMARK 500 GLU A 95P -161.74 24.72
REMARK 500 GLN A 19 -87.52 -78.11
REMARK 500 CYS A 22 120.16 -176.09
REMARK 500 LYS A 41 -62.81 -91.12
REMARK 500 ASP A 61 30.62 -90.49
REMARK 500 TYR A 87 70.96 -162.84
REMARK 500 TYR A 151 118.09 -161.50
REMARK 500 ASN A 159 51.76 -108.94
REMARK 500 TRP A 184 30.22 -98.81
REMARK 500 LYS A 200 69.65 -109.40
REMARK 500 LEU B 7P 0.74 -69.96
REMARK 500 ASN B 61P -167.95 -127.34
REMARK 500 THR B 76P -110.16 -115.16
REMARK 500 ASN B 88P 93.11 7.22
REMARK 500 ASP B 89P -140.10 40.88
REMARK 500 LEU B 91P 58.45 -108.78
REMARK 500 GLU B 95P -149.67 21.41
REMARK 500 TRP B 96P 92.08 179.06
REMARK 500 ARG B 99P -66.74 -128.56
REMARK 500 ALA B 1 134.85 83.75
REMARK 500 GLN B 19 -88.24 -78.98
REMARK 500 CYS B 22 121.15 -177.10
REMARK 500 LYS B 41 -63.27 -90.74
REMARK 500 ASP B 61 31.93 -90.84
REMARK 500 TYR B 87 70.38 -161.78
REMARK 500 TYR B 151 118.60 -161.14
REMARK 500 ASN B 159 51.95 -109.20
REMARK 500 LYS B 200 68.48 -107.65
REMARK 500 LEU C 7P 0.55 -69.42
REMARK 500 ASN C 61P -168.08 -126.47
REMARK 500 THR C 76P -108.57 -114.85
REMARK 500 TYR C 92P 56.88 -147.83
REMARK 500 GLU C 97P -58.33 164.86
REMARK 500 ALA C 1 56.06 -151.46
REMARK 500 GLN C 19 -87.15 -78.95
REMARK 500 CYS C 22 120.67 -175.73
REMARK 500 LYS C 41 -62.69 -91.19
REMARK 500 ASP C 61 30.88 -92.07
REMARK 500 TYR C 87 70.72 -162.07
REMARK 500
REMARK 500 THIS ENTRY HAS 67 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7PCK A 1P 215 UNP P43235 CATK_HUMAN 16 329
DBREF 7PCK B 1P 215 UNP P43235 CATK_HUMAN 16 329
DBREF 7PCK C 1P 215 UNP P43235 CATK_HUMAN 16 329
DBREF 7PCK D 1P 215 UNP P43235 CATK_HUMAN 16 329
SEQRES 1 A 314 LEU TYR PRO GLU GLU ILE LEU ASP THR HIS TRP GLU LEU
SEQRES 2 A 314 TRP LYS LYS THR HIS ARG LYS GLN TYR ASN ASN LYS VAL
SEQRES 3 A 314 ASP GLU ILE SER ARG ARG LEU ILE TRP GLU LYS ASN LEU
SEQRES 4 A 314 LYS TYR ILE SER ILE HIS ASN LEU GLU ALA SER LEU GLY
SEQRES 5 A 314 VAL HIS THR TYR GLU LEU ALA MET ASN HIS LEU GLY ASP
SEQRES 6 A 314 MET THR SER GLU GLU VAL VAL GLN LYS MET THR GLY LEU
SEQRES 7 A 314 LYS VAL PRO LEU SER HIS SER ARG SER ASN ASP THR LEU
SEQRES 8 A 314 TYR ILE PRO GLU TRP GLU GLY ARG ALA PRO ASP SER VAL
SEQRES 9 A 314 ASP TYR ARG LYS LYS GLY TYR VAL THR PRO VAL LYS ASN
SEQRES 10 A 314 GLN GLY GLN CYS GLY SER CYS TRP ALA PHE SER SER VAL
SEQRES 11 A 314 GLY ALA LEU GLU GLY GLN LEU LYS LYS LYS THR GLY LYS
SEQRES 12 A 314 LEU LEU ASN LEU SER PRO GLN ASN LEU VAL ASP CYS VAL
SEQRES 13 A 314 SER GLU ASN ASP GLY CYS GLY GLY GLY TYR MET THR ASN
SEQRES 14 A 314 ALA PHE GLN TYR VAL GLN LYS ASN ARG GLY ILE ASP SER
SEQRES 15 A 314 GLU ASP ALA TYR PRO TYR VAL GLY GLN GLU GLU SER CYS
SEQRES 16 A 314 MET TYR ASN PRO THR GLY LYS ALA ALA LYS CYS ARG GLY
SEQRES 17 A 314 TYR ARG GLU ILE PRO GLU GLY ASN GLU LYS ALA LEU LYS
SEQRES 18 A 314 ARG ALA VAL ALA ARG VAL GLY PRO VAL SER VAL ALA ILE
SEQRES 19 A 314 ASP ALA SER LEU THR SER PHE GLN PHE TYR SER LYS GLY
SEQRES 20 A 314 VAL TYR TYR ASP GLU SER CYS ASN SER ASP ASN LEU ASN
SEQRES 21 A 314 HIS ALA VAL LEU ALA VAL GLY TYR GLY ILE GLN LYS GLY
SEQRES 22 A 314 ASN LYS HIS TRP ILE ILE LYS ASN SER TRP GLY GLU ASN
SEQRES 23 A 314 TRP GLY ASN LYS GLY TYR ILE LEU MET ALA ARG ASN LYS
SEQRES 24 A 314 ASN ASN ALA CYS GLY ILE ALA ASN LEU ALA SER PHE PRO
SEQRES 25 A 314 LYS MET
SEQRES 1 B 314 LEU TYR PRO GLU GLU ILE LEU ASP THR HIS TRP GLU LEU
SEQRES 2 B 314 TRP LYS LYS THR HIS ARG LYS GLN TYR ASN ASN LYS VAL
SEQRES 3 B 314 ASP GLU ILE SER ARG ARG LEU ILE TRP GLU LYS ASN LEU
SEQRES 4 B 314 LYS TYR ILE SER ILE HIS ASN LEU GLU ALA SER LEU GLY
SEQRES 5 B 314 VAL HIS THR TYR GLU LEU ALA MET ASN HIS LEU GLY ASP
SEQRES 6 B 314 MET THR SER GLU GLU VAL VAL GLN LYS MET THR GLY LEU
SEQRES 7 B 314 LYS VAL PRO LEU SER HIS SER ARG SER ASN ASP THR LEU
SEQRES 8 B 314 TYR ILE PRO GLU TRP GLU GLY ARG ALA PRO ASP SER VAL
SEQRES 9 B 314 ASP TYR ARG LYS LYS GLY TYR VAL THR PRO VAL LYS ASN
SEQRES 10 B 314 GLN GLY GLN CYS GLY SER CYS TRP ALA PHE SER SER VAL
SEQRES 11 B 314 GLY ALA LEU GLU GLY GLN LEU LYS LYS LYS THR GLY LYS
SEQRES 12 B 314 LEU LEU ASN LEU SER PRO GLN ASN LEU VAL ASP CYS VAL
SEQRES 13 B 314 SER GLU ASN ASP GLY CYS GLY GLY GLY TYR MET THR ASN
SEQRES 14 B 314 ALA PHE GLN TYR VAL GLN LYS ASN ARG GLY ILE ASP SER
SEQRES 15 B 314 GLU ASP ALA TYR PRO TYR VAL GLY GLN GLU GLU SER CYS
SEQRES 16 B 314 MET TYR ASN PRO THR GLY LYS ALA ALA LYS CYS ARG GLY
SEQRES 17 B 314 TYR ARG GLU ILE PRO GLU GLY ASN GLU LYS ALA LEU LYS
SEQRES 18 B 314 ARG ALA VAL ALA ARG VAL GLY PRO VAL SER VAL ALA ILE
SEQRES 19 B 314 ASP ALA SER LEU THR SER PHE GLN PHE TYR SER LYS GLY
SEQRES 20 B 314 VAL TYR TYR ASP GLU SER CYS ASN SER ASP ASN LEU ASN
SEQRES 21 B 314 HIS ALA VAL LEU ALA VAL GLY TYR GLY ILE GLN LYS GLY
SEQRES 22 B 314 ASN LYS HIS TRP ILE ILE LYS ASN SER TRP GLY GLU ASN
SEQRES 23 B 314 TRP GLY ASN LYS GLY TYR ILE LEU MET ALA ARG ASN LYS
SEQRES 24 B 314 ASN ASN ALA CYS GLY ILE ALA ASN LEU ALA SER PHE PRO
SEQRES 25 B 314 LYS MET
SEQRES 1 C 314 LEU TYR PRO GLU GLU ILE LEU ASP THR HIS TRP GLU LEU
SEQRES 2 C 314 TRP LYS LYS THR HIS ARG LYS GLN TYR ASN ASN LYS VAL
SEQRES 3 C 314 ASP GLU ILE SER ARG ARG LEU ILE TRP GLU LYS ASN LEU
SEQRES 4 C 314 LYS TYR ILE SER ILE HIS ASN LEU GLU ALA SER LEU GLY
SEQRES 5 C 314 VAL HIS THR TYR GLU LEU ALA MET ASN HIS LEU GLY ASP
SEQRES 6 C 314 MET THR SER GLU GLU VAL VAL GLN LYS MET THR GLY LEU
SEQRES 7 C 314 LYS VAL PRO LEU SER HIS SER ARG SER ASN ASP THR LEU
SEQRES 8 C 314 TYR ILE PRO GLU TRP GLU GLY ARG ALA PRO ASP SER VAL
SEQRES 9 C 314 ASP TYR ARG LYS LYS GLY TYR VAL THR PRO VAL LYS ASN
SEQRES 10 C 314 GLN GLY GLN CYS GLY SER CYS TRP ALA PHE SER SER VAL
SEQRES 11 C 314 GLY ALA LEU GLU GLY GLN LEU LYS LYS LYS THR GLY LYS
SEQRES 12 C 314 LEU LEU ASN LEU SER PRO GLN ASN LEU VAL ASP CYS VAL
SEQRES 13 C 314 SER GLU ASN ASP GLY CYS GLY GLY GLY TYR MET THR ASN
SEQRES 14 C 314 ALA PHE GLN TYR VAL GLN LYS ASN ARG GLY ILE ASP SER
SEQRES 15 C 314 GLU ASP ALA TYR PRO TYR VAL GLY GLN GLU GLU SER CYS
SEQRES 16 C 314 MET TYR ASN PRO THR GLY LYS ALA ALA LYS CYS ARG GLY
SEQRES 17 C 314 TYR ARG GLU ILE PRO GLU GLY ASN GLU LYS ALA LEU LYS
SEQRES 18 C 314 ARG ALA VAL ALA ARG VAL GLY PRO VAL SER VAL ALA ILE
SEQRES 19 C 314 ASP ALA SER LEU THR SER PHE GLN PHE TYR SER LYS GLY
SEQRES 20 C 314 VAL TYR TYR ASP GLU SER CYS ASN SER ASP ASN LEU ASN
SEQRES 21 C 314 HIS ALA VAL LEU ALA VAL GLY TYR GLY ILE GLN LYS GLY
SEQRES 22 C 314 ASN LYS HIS TRP ILE ILE LYS ASN SER TRP GLY GLU ASN
SEQRES 23 C 314 TRP GLY ASN LYS GLY TYR ILE LEU MET ALA ARG ASN LYS
SEQRES 24 C 314 ASN ASN ALA CYS GLY ILE ALA ASN LEU ALA SER PHE PRO
SEQRES 25 C 314 LYS MET
SEQRES 1 D 314 LEU TYR PRO GLU GLU ILE LEU ASP THR HIS TRP GLU LEU
SEQRES 2 D 314 TRP LYS LYS THR HIS ARG LYS GLN TYR ASN ASN LYS VAL
SEQRES 3 D 314 ASP GLU ILE SER ARG ARG LEU ILE TRP GLU LYS ASN LEU
SEQRES 4 D 314 LYS TYR ILE SER ILE HIS ASN LEU GLU ALA SER LEU GLY
SEQRES 5 D 314 VAL HIS THR TYR GLU LEU ALA MET ASN HIS LEU GLY ASP
SEQRES 6 D 314 MET THR SER GLU GLU VAL VAL GLN LYS MET THR GLY LEU
SEQRES 7 D 314 LYS VAL PRO LEU SER HIS SER ARG SER ASN ASP THR LEU
SEQRES 8 D 314 TYR ILE PRO GLU TRP GLU GLY ARG ALA PRO ASP SER VAL
SEQRES 9 D 314 ASP TYR ARG LYS LYS GLY TYR VAL THR PRO VAL LYS ASN
SEQRES 10 D 314 GLN GLY GLN CYS GLY SER CYS TRP ALA PHE SER SER VAL
SEQRES 11 D 314 GLY ALA LEU GLU GLY GLN LEU LYS LYS LYS THR GLY LYS
SEQRES 12 D 314 LEU LEU ASN LEU SER PRO GLN ASN LEU VAL ASP CYS VAL
SEQRES 13 D 314 SER GLU ASN ASP GLY CYS GLY GLY GLY TYR MET THR ASN
SEQRES 14 D 314 ALA PHE GLN TYR VAL GLN LYS ASN ARG GLY ILE ASP SER
SEQRES 15 D 314 GLU ASP ALA TYR PRO TYR VAL GLY GLN GLU GLU SER CYS
SEQRES 16 D 314 MET TYR ASN PRO THR GLY LYS ALA ALA LYS CYS ARG GLY
SEQRES 17 D 314 TYR ARG GLU ILE PRO GLU GLY ASN GLU LYS ALA LEU LYS
SEQRES 18 D 314 ARG ALA VAL ALA ARG VAL GLY PRO VAL SER VAL ALA ILE
SEQRES 19 D 314 ASP ALA SER LEU THR SER PHE GLN PHE TYR SER LYS GLY
SEQRES 20 D 314 VAL TYR TYR ASP GLU SER CYS ASN SER ASP ASN LEU ASN
SEQRES 21 D 314 HIS ALA VAL LEU ALA VAL GLY TYR GLY ILE GLN LYS GLY
SEQRES 22 D 314 ASN LYS HIS TRP ILE ILE LYS ASN SER TRP GLY GLU ASN
SEQRES 23 D 314 TRP GLY ASN LYS GLY TYR ILE LEU MET ALA ARG ASN LYS
SEQRES 24 D 314 ASN ASN ALA CYS GLY ILE ALA ASN LEU ALA SER PHE PRO
SEQRES 25 D 314 LYS MET
HELIX 1 1 GLU A 5P THR A 17P 5 13
HELIX 2 2 LYS A 25P SER A 50P 1 26
HELIX 3 3 SER A 68P MET A 75P 1 8
HELIX 4 4 CYS A 25 THR A 42 1 18
HELIX 5 5 PRO A 50 CYS A 56 1 7
HELIX 6 6 GLY A 62 GLY A 64 5 3
HELIX 7 7 MET A 68 ASN A 78 1 11
HELIX 8 8 GLU A 84 ALA A 86 5 3
HELIX 9 9 PRO A 100 GLY A 102 5 3
HELIX 10 10 GLU A 118 ARG A 127 1 10
HELIX 11 11 THR A 140 GLN A 143 1 4
HELIX 12 12 ALA A 203 GLY A 205 5 3
HELIX 13 13 GLU B 5P THR B 17P 5 13
HELIX 14 14 LYS B 25P SER B 50P 1 26
HELIX 15 15 SER B 68P MET B 75P 1 8
HELIX 16 16 CYS B 25 THR B 42 1 18
HELIX 17 17 PRO B 50 CYS B 56 1 7
HELIX 18 18 GLY B 62 GLY B 64 5 3
HELIX 19 19 MET B 68 ASN B 78 1 11
HELIX 20 20 GLU B 118 ARG B 127 1 10
HELIX 21 21 THR B 140 GLN B 143 1 4
HELIX 22 22 ALA B 203 GLY B 205 5 3
HELIX 23 23 GLU C 5P THR C 17P 5 13
HELIX 24 24 LYS C 25P SER C 50P 1 26
HELIX 25 25 SER C 68P MET C 75P 1 8
HELIX 26 26 CYS C 25 THR C 42 1 18
HELIX 27 27 PRO C 50 CYS C 56 1 7
HELIX 28 28 GLY C 62 GLY C 64 5 3
HELIX 29 29 MET C 68 ASN C 78 1 11
HELIX 30 30 GLU C 84 ALA C 86 5 3
HELIX 31 31 GLU C 118 ARG C 127 1 10
HELIX 32 32 THR C 140 GLN C 143 1 4
HELIX 33 33 ALA C 203 GLY C 205 5 3
HELIX 34 34 GLU D 5P THR D 17P 5 13
HELIX 35 35 LYS D 25P SER D 50P 1 26
HELIX 36 36 SER D 68P MET D 75P 1 8
HELIX 37 37 CYS D 25 THR D 42 1 18
HELIX 38 38 PRO D 50 CYS D 56 1 7
HELIX 39 39 GLY D 62 GLY D 64 5 3
HELIX 40 40 MET D 68 ASN D 78 1 11
HELIX 41 41 GLU D 84 ALA D 86 5 3
HELIX 42 42 PRO D 100 GLY D 102 5 3
HELIX 43 43 GLU D 118 ARG D 127 1 10
HELIX 44 44 THR D 140 GLN D 143 1 4
HELIX 45 45 ALA D 203 GLY D 205 5 3
SHEET 1 A 2 TYR A 110 GLU A 112 0
SHEET 2 A 2 SER A 211 PRO A 213 -1 N PHE A 212 O ARG A 111
SHEET 1 B 4 VAL A 131 ILE A 135 0
SHEET 2 B 4 HIS A 162 GLN A 172 -1 N ALA A 166 O VAL A 131
SHEET 3 B 4 ASN A 175 LYS A 181 -1 N LYS A 181 O LEU A 165
SHEET 4 B 4 TYR A 193 ALA A 197 -1 N MET A 196 O TRP A 178
SHEET 1 C 2 TYR A 56P LEU A 58P 0
SHEET 2 C 2 TYR A 145 GLY A 148 -1 N LYS A 147 O GLU A 57P
SHEET 1 D 2 TYR B 110 GLU B 112 0
SHEET 2 D 2 SER B 211 PRO B 213 -1 N PHE B 212 O ARG B 111
SHEET 1 E 4 VAL B 131 ILE B 135 0
SHEET 2 E 4 HIS B 162 GLN B 172 -1 N ALA B 166 O VAL B 131
SHEET 3 E 4 ASN B 175 LYS B 181 -1 N LYS B 181 O LEU B 165
SHEET 4 E 4 TYR B 193 ALA B 197 -1 N MET B 196 O TRP B 178
SHEET 1 F 2 TYR B 56P LEU B 58P 0
SHEET 2 F 2 TYR B 145 GLY B 148 -1 N LYS B 147 O GLU B 57P
SHEET 1 G 2 TYR C 110 GLU C 112 0
SHEET 2 G 2 SER C 211 PRO C 213 -1 N PHE C 212 O ARG C 111
SHEET 1 H 4 VAL C 131 ILE C 135 0
SHEET 2 H 4 HIS C 162 GLN C 172 -1 N ALA C 166 O VAL C 131
SHEET 3 H 4 ASN C 175 LYS C 181 -1 N LYS C 181 O LEU C 165
SHEET 4 H 4 TYR C 193 ALA C 197 -1 N MET C 196 O TRP C 178
SHEET 1 I 2 TYR C 56P LEU C 58P 0
SHEET 2 I 2 TYR C 145 GLY C 148 -1 N LYS C 147 O GLU C 57P
SHEET 1 J 2 TYR D 110 GLU D 112 0
SHEET 2 J 2 SER D 211 PRO D 213 -1 N PHE D 212 O ARG D 111
SHEET 1 K 4 VAL D 131 ILE D 135 0
SHEET 2 K 4 HIS D 162 GLN D 172 -1 N ALA D 166 O VAL D 131
SHEET 3 K 4 ASN D 175 LYS D 181 -1 N LYS D 181 O LEU D 165
SHEET 4 K 4 TYR D 193 ALA D 197 -1 N MET D 196 O TRP D 178
SHEET 1 L 2 TYR D 56P LEU D 58P 0
SHEET 2 L 2 TYR D 145 GLY D 148 -1 N LYS D 147 O GLU D 57P
SSBOND 1 CYS A 22 CYS A 63 1555 1555 2.03
SSBOND 2 CYS A 56 CYS A 96 1555 1555 2.03
SSBOND 3 CYS A 155 CYS A 204 1555 1555 2.02
SSBOND 4 CYS B 22 CYS B 63 1555 1555 2.04
SSBOND 5 CYS B 56 CYS B 96 1555 1555 2.03
SSBOND 6 CYS B 155 CYS B 204 1555 1555 2.02
SSBOND 7 CYS C 22 CYS C 63 1555 1555 2.03
SSBOND 8 CYS C 56 CYS C 96 1555 1555 2.02
SSBOND 9 CYS C 155 CYS C 204 1555 1555 2.03
SSBOND 10 CYS D 22 CYS D 63 1555 1555 2.04
SSBOND 11 CYS D 56 CYS D 96 1555 1555 2.03
SSBOND 12 CYS D 155 CYS D 204 1555 1555 2.03
CRYST1 58.700 84.400 155.600 90.00 90.30 90.00 P 1 21 1 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 0.017036 0.000000 0.000089 0.00000
SCALE2 0.000000 0.011848 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006427 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
