HEADER HYDROLASE 29-MAY-07 2Z2Z
TITLE CRYSTAL STRUCTURE OF UNAUTOPROCESSED FORM OF TK-SUBTILISIN SOAKED BY
TITLE 2 10MM CACL2
CAVEAT 2Z2Z CHIRALITY ERROR AT THE CB CENTER OF THR A 361
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TK-SUBTILISIN PRECURSOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 28-422;
COMPND 5 EC: 3.4.21.62;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOCOCCUS KODAKARENSIS;
SOURCE 3 ORGANISM_TAXID: 69014;
SOURCE 4 STRAIN: KOD1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET25B
KEYWDS SUBTILISIN, THERMOCOCCUS KODAKARAENSIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.TANAKA,H.MATSUMURA,Y.KOGA,K.TAKANO,S.KANAYA
REVDAT 6 01-NOV-23 2Z2Z 1 REMARK
REVDAT 5 10-NOV-21 2Z2Z 1 REMARK SEQADV
REVDAT 4 13-JUL-11 2Z2Z 1 VERSN
REVDAT 3 08-SEP-09 2Z2Z 1 CAVEAT
REVDAT 2 24-FEB-09 2Z2Z 1 VERSN
REVDAT 1 04-DEC-07 2Z2Z 0
JRNL AUTH S.TANAKA,H.MATSUMURA,Y.KOGA,K.TAKANO,S.KANAYA
JRNL TITL FOUR NEW CRYSTAL STRUCTURES OF TK-SUBTILISIN IN
JRNL TITL 2 UNAUTOPROCESSED, AUTOPROCESSED AND MATURE FORMS: INSIGHT
JRNL TITL 3 INTO STRUCTURAL CHANGES DURING MATURATION
JRNL REF J.MOL.BIOL. V. 372 1055 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17706669
JRNL DOI 10.1016/J.JMB.2007.07.027
REMARK 2
REMARK 2 RESOLUTION. 1.87 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
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) : 1.87
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.33
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 33178
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) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1752
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) : 1.87
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2309
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1900
REMARK 3 BIN FREE R VALUE SET COUNT : 106
REMARK 3 BIN FREE R VALUE : 0.2480
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2861
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 7
REMARK 3 SOLVENT ATOMS : 410
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.130
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.127
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.118
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.821
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2922 ; 0.029 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2654 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3998 ; 2.279 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6174 ; 1.057 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 387 ; 5.351 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 472 ;17.847 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 465 ; 0.241 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3326 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 530 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 755 ; 0.247 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2853 ; 0.227 ; 0.300
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): 374 ; 0.219 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.002 ; 0.500
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 35 ; 0.213 ; 0.500
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 18 ; 0.250 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 46 ; 0.332 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 27 ; 0.477 ; 0.500
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): 1926 ; 1.429 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3102 ; 2.366 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 996 ; 3.585 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 896 ; 5.437 ; 4.500
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 : 1.40
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
REMARK 4
REMARK 4 2Z2Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-MAY-07.
REMARK 100 THE DEPOSITION ID IS D_1000027455.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-OCT-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL38B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU JUPITER 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34961
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.870
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 45.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.87
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.18800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.400
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 2E1P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 4.0M SODIUM FORMATE, PH 8.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 46.32900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 62.08650
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 36.15700
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 46.32900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 62.08650
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 36.15700
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 46.32900
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 62.08650
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 36.15700
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 46.32900
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 62.08650
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 36.15700
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 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 LEU A 75
REMARK 465 GLY A 76
REMARK 465 GLY A 77
REMARK 465 GLY A 78
REMARK 465 SER A 79
REMARK 465 THR A 80
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 CB CYS A 147 O HOH A 1409 1.62
REMARK 500 NE2 GLN A 81 O HOH A 1413 1.63
REMARK 500 O HOH A 1209 O HOH A 1308 2.05
REMARK 500 O HOH A 1265 O HOH A 1321 2.09
REMARK 500 O HOH A 1230 O HOH A 1311 2.10
REMARK 500 O HOH A 1387 O HOH A 1400 2.11
REMARK 500 O HOH A 1206 O HOH A 1319 2.11
REMARK 500 O HOH A 1273 O HOH A 1338 2.14
REMARK 500 OD2 ASP A 381 O HOH A 1376 2.16
REMARK 500 O HOH A 1287 O HOH A 1315 2.17
REMARK 500 OD2 ASP A 167 O HOH A 1341 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 1407 O HOH A 1407 3656 0.78
REMARK 500 O HOH A 1173 O HOH A 1173 4556 1.67
REMARK 500 O HOH A 1321 O HOH A 1347 8555 2.12
REMARK 500
REMARK 500 REMARK: NULL
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 VAL A 8 CB VAL A 8 CG1 -0.148
REMARK 500 VAL A 22 CB VAL A 22 CG2 -0.150
REMARK 500 VAL A 39 CB VAL A 39 CG2 -0.181
REMARK 500 VAL A 41 CB VAL A 41 CG2 -0.156
REMARK 500 GLU A 91 CD GLU A 91 OE2 0.137
REMARK 500 VAL A 93 CB VAL A 93 CG2 -0.161
REMARK 500 TRP A 131 CE3 TRP A 131 CZ3 -0.104
REMARK 500 ARG A 183 NE ARG A 183 CZ 0.080
REMARK 500 THR A 361 CB THR A 361 CG2 -0.225
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 ASP A 115 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 121 CB - CG - OD1 ANGL. DEV. = 16.5 DEGREES
REMARK 500 ASP A 121 CB - CG - OD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 CYS A 132 CB - CA - C ANGL. DEV. = 15.5 DEGREES
REMARK 500 LEU A 144 CB - CG - CD2 ANGL. DEV. = 10.9 DEGREES
REMARK 500 ASP A 149 CB - CG - OD2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 ASP A 167 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 183 CD - NE - CZ ANGL. DEV. = 15.5 DEGREES
REMARK 500 ARG A 183 NE - CZ - NH1 ANGL. DEV. = 15.5 DEGREES
REMARK 500 ARG A 183 NE - CZ - NH2 ANGL. DEV. = -10.5 DEGREES
REMARK 500 ASP A 186 CB - CG - OD1 ANGL. DEV. = 8.8 DEGREES
REMARK 500 ASP A 214 CB - CG - OD2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 ASP A 225 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP A 289 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 297 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 297 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ASP A 372 CB - CG - OD1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ASP A 379 CB - CG - OD2 ANGL. DEV. = -5.9 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 SER A 105 36.21 -77.21
REMARK 500 ASP A 115 -149.28 -160.23
REMARK 500 ASN A 166 -145.17 -154.67
REMARK 500 VAL A 170 -162.49 -127.65
REMARK 500 ILE A 219 -76.24 -122.92
REMARK 500 SER A 316 -166.59 -126.79
REMARK 500
REMARK 500 REMARK: NULL
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 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1007
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2Z2X RELATED DB: PDB
REMARK 900 MATURE TK-SUBTILISIN
REMARK 900 RELATED ID: 2Z2Y RELATED DB: PDB
REMARK 900 AUTOPROCESSED FORM OF TK-SUBTILISIN
REMARK 900 RELATED ID: 2Z30 RELATED DB: PDB
REMARK 900 COMPLEX FORM BETWEEN MAT-TK-SUBTILISIN AND TK-PROPEPTIDE
DBREF 2Z2Z A 4 398 UNP P58502 TKSU_PYRKO 28 422
SEQADV 2Z2Z ALA A 324 UNP P58502 SER 348 ENGINEERED MUTATION
SEQRES 1 A 395 ASN THR ILE ARG VAL ILE VAL SER VAL ASP LYS ALA LYS
SEQRES 2 A 395 PHE ASN PRO HIS GLU VAL LEU GLY ILE GLY GLY HIS ILE
SEQRES 3 A 395 VAL TYR GLN PHE LYS LEU ILE PRO ALA VAL VAL VAL ASP
SEQRES 4 A 395 VAL PRO ALA ASN ALA VAL GLY LYS LEU LYS LYS MET PRO
SEQRES 5 A 395 GLY VAL GLU LYS VAL GLU PHE ASP HIS GLN ALA VAL LEU
SEQRES 6 A 395 LEU GLY LYS PRO SER TRP LEU GLY GLY GLY SER THR GLN
SEQRES 7 A 395 PRO ALA GLN THR ILE PRO TRP GLY ILE GLU ARG VAL LYS
SEQRES 8 A 395 ALA PRO SER VAL TRP SER ILE THR ASP GLY SER VAL SER
SEQRES 9 A 395 VAL ILE GLN VAL ALA VAL LEU ASP THR GLY VAL ASP TYR
SEQRES 10 A 395 ASP HIS PRO ASP LEU ALA ALA ASN ILE ALA TRP CYS VAL
SEQRES 11 A 395 SER THR LEU ARG GLY LYS VAL SER THR LYS LEU ARG ASP
SEQRES 12 A 395 CYS ALA ASP GLN ASN GLY HIS GLY THR HIS VAL ILE GLY
SEQRES 13 A 395 THR ILE ALA ALA LEU ASN ASN ASP ILE GLY VAL VAL GLY
SEQRES 14 A 395 VAL ALA PRO GLY VAL GLN ILE TYR SER VAL ARG VAL LEU
SEQRES 15 A 395 ASP ALA ARG GLY SER GLY SER TYR SER ASP ILE ALA ILE
SEQRES 16 A 395 GLY ILE GLU GLN ALA ILE LEU GLY PRO ASP GLY VAL ALA
SEQRES 17 A 395 ASP LYS ASP GLY ASP GLY ILE ILE ALA GLY ASP PRO ASP
SEQRES 18 A 395 ASP ASP ALA ALA GLU VAL ILE SER MET SER LEU GLY GLY
SEQRES 19 A 395 PRO ALA ASP ASP SER TYR LEU TYR ASP MET ILE ILE GLN
SEQRES 20 A 395 ALA TYR ASN ALA GLY ILE VAL ILE VAL ALA ALA SER GLY
SEQRES 21 A 395 ASN GLU GLY ALA PRO SER PRO SER TYR PRO ALA ALA TYR
SEQRES 22 A 395 PRO GLU VAL ILE ALA VAL GLY ALA ILE ASP SER ASN ASP
SEQRES 23 A 395 ASN ILE ALA SER PHE SER ASN ARG GLN PRO GLU VAL SER
SEQRES 24 A 395 ALA PRO GLY VAL ASP ILE LEU SER THR TYR PRO ASP ASP
SEQRES 25 A 395 SER TYR GLU THR LEU MET GLY THR ALA MET ALA THR PRO
SEQRES 26 A 395 HIS VAL SER GLY VAL VAL ALA LEU ILE GLN ALA ALA TYR
SEQRES 27 A 395 TYR GLN LYS TYR GLY LYS ILE LEU PRO VAL GLY THR PHE
SEQRES 28 A 395 ASP ASP ILE SER LYS ASN THR VAL ARG GLY ILE LEU HIS
SEQRES 29 A 395 ILE THR ALA ASP ASP LEU GLY PRO THR GLY TRP ASP ALA
SEQRES 30 A 395 ASP TYR GLY TYR GLY VAL VAL ARG ALA ALA LEU ALA VAL
SEQRES 31 A 395 GLN ALA ALA LEU GLY
HET CA A1001 1
HET CA A1002 1
HET CA A1003 1
HET CA A1004 1
HET CA A1005 1
HET CA A1006 1
HET CA A1007 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 7(CA 2+)
FORMUL 9 HOH *410(H2 O)
HELIX 1 1 ASN A 18 ILE A 25 1 8
HELIX 2 2 ALA A 47 LYS A 53 1 7
HELIX 3 3 PRO A 87 VAL A 93 1 7
HELIX 4 4 ALA A 95 ILE A 101 5 7
HELIX 5 5 LEU A 125 ALA A 127 5 3
HELIX 6 6 LEU A 136 LYS A 139 5 4
HELIX 7 7 LYS A 143 ALA A 148 1 6
HELIX 8 8 GLY A 152 ALA A 163 1 12
HELIX 9 9 TYR A 193 GLY A 206 1 14
HELIX 10 10 ASP A 241 ALA A 254 1 14
HELIX 11 11 GLY A 322 GLY A 346 1 25
HELIX 12 12 THR A 361 ALA A 370 1 10
HELIX 13 13 ARG A 388 GLY A 398 1 11
SHEET 1 A 4 HIS A 28 GLN A 32 0
SHEET 2 A 4 ALA A 38 PRO A 44 -1 O VAL A 40 N VAL A 30
SHEET 3 A 4 THR A 5 VAL A 12 -1 N VAL A 10 O VAL A 39
SHEET 4 A 4 VAL A 57 PHE A 62 -1 O GLU A 61 N ILE A 9
SHEET 1 B 3 SER A 190 SER A 192 0
SHEET 2 B 3 GLN A 65 LEU A 68 -1 N ALA A 66 O GLY A 191
SHEET 3 B 3 LEU A 235 GLY A 236 -1 O GLY A 236 N VAL A 67
SHEET 1 C 3 LYS A 71 PRO A 72 0
SHEET 2 C 3 SER A 316 MET A 321 -1 O MET A 321 N LYS A 71
SHEET 3 C 3 ILE A 308 TYR A 312 -1 N TYR A 312 O SER A 316
SHEET 1 D 7 ILE A 129 SER A 134 0
SHEET 2 D 7 GLN A 178 ARG A 183 1 O ARG A 183 N VAL A 133
SHEET 3 D 7 GLN A 110 ASP A 115 1 N VAL A 113 O VAL A 182
SHEET 4 D 7 VAL A 230 MET A 233 1 O VAL A 230 N ALA A 112
SHEET 5 D 7 VAL A 257 ALA A 261 1 O VAL A 259 N ILE A 231
SHEET 6 D 7 VAL A 279 ILE A 285 1 O ILE A 280 N ALA A 260
SHEET 7 D 7 VAL A 301 PRO A 304 1 O VAL A 301 N GLY A 283
SSBOND 1 CYS A 132 CYS A 147 1555 1555 2.09
CISPEP 1 TYR A 272 PRO A 273 0 -0.16
CISPEP 2 PRO A 313 ASP A 314 0 -4.85
SITE 1 AC1 6 VAL A 108 GLN A 110 ALA A 227 GLU A 229
SITE 2 AC1 6 HOH A1405 HOH A1408
SITE 1 AC2 6 ASP A 119 ASP A 121 ASP A 314 ASP A 315
SITE 2 AC2 6 HOH A1086 HOH A1350
SITE 1 AC3 6 LEU A 205 ASP A 208 VAL A 210 ASP A 226
SITE 2 AC3 6 HOH A1008 HOH A1010
SITE 1 AC4 6 ASP A 212 ASP A 214 ASP A 216 ILE A 218
SITE 2 AC4 6 ASP A 222 ASP A 225
SITE 1 AC5 6 ASP A 214 ASP A 216 ASP A 222 ASP A 224
SITE 2 AC5 6 HOH A1385 HOH A1406
SITE 1 AC6 6 ASP A 372 LEU A 373 PRO A 375 GLY A 377
SITE 2 AC6 6 ASP A 379 HOH A1066
SITE 1 AC7 6 GLN A 84 ASP A 124 LEU A 164 ASN A 166
SITE 2 AC7 6 ILE A 168 VAL A 170
CRYST1 92.658 124.173 72.314 90.00 90.00 90.00 I 2 2 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 0.010792 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008053 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013829 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
