HEADER TRANSFERASE/DNA 24-SEP-07 2RDJ
TITLE SNAPSHOTS OF A Y-FAMILY DNA POLYMERASE IN REPLICATION: DPO4 IN APO AND
TITLE 2 BINARY/TERNARY COMPLEX FORMS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-
COMPND 3 D(*DGP*DGP*DGP*DAP*DCP*DCP*DCP*DTP*DTP*DCP*DGP*DAP*DAP*DT)-3');
COMPND 4 CHAIN: C, E;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: DNA PRIMER STRAND;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DNA (5'-
COMPND 9 D(P*DTP*DTP*DAP*DTP*DTP*DCP*DGP*DAP*DAP*DGP*DGP*DGP*DTP*DCP*DCP*DC)-
COMPND 10 3');
COMPND 11 CHAIN: D;
COMPND 12 ENGINEERED: YES;
COMPND 13 OTHER_DETAILS: DNA TEMPLATE STRAND FROM POLYPEPTIDE CHAIN A;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: DNA (5'-
COMPND 16 D(P*DTP*DAP*DTP*DTP*DCP*DGP*DAP*DAP*DGP*DGP*DGP*DTP*DCP*DCP*DC)-3');
COMPND 17 CHAIN: F;
COMPND 18 ENGINEERED: YES;
COMPND 19 OTHER_DETAILS: DNA TEMPLATE STRAND FROM POLYPEPTIDE CHAIN B;
COMPND 20 MOL_ID: 4;
COMPND 21 MOLECULE: DNA POLYMERASE IV;
COMPND 22 CHAIN: A, B;
COMPND 23 SYNONYM: POL IV;
COMPND 24 EC: 2.7.7.7;
COMPND 25 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 MOL_ID: 3;
SOURCE 6 SYNTHETIC: YES;
SOURCE 7 MOL_ID: 4;
SOURCE 8 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;
SOURCE 9 STRAIN: P2;
SOURCE 10 GENE: DBH, DPO4;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS DNA POLYMERASE, DNA-ENZYME COMPLEX, Y-FAMILY, DNA DAMAGE, DNA REPAIR,
KEYWDS 2 DNA REPLICATION, DNA-BINDING, DNA-DIRECTED DNA POLYMERASE,
KEYWDS 3 MAGNESIUM, METAL-BINDING, MUTATOR PROTEIN, NUCLEOTIDYLTRANSFERASE,
KEYWDS 4 TRANSFERASE, TRANSFERASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.H.Y.WONG,H.LING
REVDAT 6 30-AUG-23 2RDJ 1 REMARK DBREF LINK
REVDAT 5 11-OCT-17 2RDJ 1 REMARK
REVDAT 4 13-JUL-11 2RDJ 1 VERSN
REVDAT 3 24-FEB-09 2RDJ 1 VERSN
REVDAT 2 01-JUL-08 2RDJ 1 REMARK
REVDAT 1 24-JUN-08 2RDJ 0
JRNL AUTH J.H.WONG,K.A.FIALA,Z.SUO,H.LING
JRNL TITL SNAPSHOTS OF A Y-FAMILY DNA POLYMERASE IN REPLICATION:
JRNL TITL 2 SUBSTRATE-INDUCED CONFORMATIONAL TRANSITIONS AND
JRNL TITL 3 IMPLICATIONS FOR FIDELITY OF DPO4.
JRNL REF J.MOL.BIOL. V. 379 317 2008
JRNL REFN ISSN 0022-2836
JRNL PMID 18448122
JRNL DOI 10.1016/J.JMB.2008.03.038
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.11
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 51924
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) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2660
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) : 2.21
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2850
REMARK 3 BIN FREE R VALUE SET COUNT : 199
REMARK 3 BIN FREE R VALUE : 0.3520
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5486
REMARK 3 NUCLEIC ACID ATOMS : 1202
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 305
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.55000
REMARK 3 B22 (A**2) : -1.66000
REMARK 3 B33 (A**2) : -0.89000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.169
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.829
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6948 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9576 ; 1.502 ; 2.213
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 680 ; 5.554 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 242 ;31.202 ;23.636
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1126 ;15.631 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 48 ;16.448 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1093 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4637 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2872 ; 0.200 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4645 ; 0.303 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 460 ; 0.154 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 8 ; 0.152 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 48 ; 0.151 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.136 ; 0.200
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): 3553 ; 0.678 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5520 ; 1.115 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4237 ; 1.744 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4056 ; 2.756 ; 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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2RDJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-OCT-07.
REMARK 100 THE DEPOSITION ID IS D_1000044730.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRADED MULTILAYER (OSMIC)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51948
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1JX4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-15% PEG3350, 0.2M CALCIUM ACETATE,
REMARK 280 0.1M HEPES PH 7.0, 5% GLYCEROL, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 48.99650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.05450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.25500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.05450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.99650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.25500
REMARK 290 SMTRY3 4 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 300 REMARK: BIOLOGICAL UNIT IS CHAIN A ALONE OR CHAIN B ALONE.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, 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 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 GLU A 342
REMARK 465 ALA A 343
REMARK 465 ILE A 344
REMARK 465 GLY A 345
REMARK 465 LEU A 346
REMARK 465 ASP A 347
REMARK 465 LYS A 348
REMARK 465 PHE A 349
REMARK 465 PHE A 350
REMARK 465 ASP A 351
REMARK 465 THR A 352
REMARK 465 GLU B 342
REMARK 465 ALA B 343
REMARK 465 ILE B 344
REMARK 465 GLY B 345
REMARK 465 LEU B 346
REMARK 465 ASP B 347
REMARK 465 LYS B 348
REMARK 465 PHE B 349
REMARK 465 PHE B 350
REMARK 465 ASP B 351
REMARK 465 THR B 352
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 DC F 8 O3' DC F 8 C3' -0.040
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 DA C 4 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DA C 4 C3' - O3' - P ANGL. DEV. = 8.1 DEGREES
REMARK 500 DC C 5 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 DC C 10 N1 - C1' - C2' ANGL. DEV. = 8.7 DEGREES
REMARK 500 DA C 12 O4' - C1' - N9 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DA C 13 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DT D 3 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DT D 3 N3 - C2 - O2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 DA D 10 C3' - O3' - P ANGL. DEV. = 8.2 DEGREES
REMARK 500 DA D 11 O4' - C1' - N9 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DG D 12 O4' - C1' - N9 ANGL. DEV. = 9.9 DEGREES
REMARK 500 DG D 13 O4' - C1' - N9 ANGL. DEV. = 5.2 DEGREES
REMARK 500 DG D 14 O4' - C4' - C3' ANGL. DEV. = -3.2 DEGREES
REMARK 500 DC D 16 O4' - C1' - N1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DC D 16 C3' - O3' - P ANGL. DEV. = 7.8 DEGREES
REMARK 500 DC D 17 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DC D 18 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DG E 2 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DG E 3 C5 - C6 - O6 ANGL. DEV. = -3.8 DEGREES
REMARK 500 DC E 5 O4' - C1' - N1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 DC E 5 N1 - C2 - O2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 DC E 7 C2 - N3 - C4 ANGL. DEV. = 3.5 DEGREES
REMARK 500 DC E 10 O4' - C1' - N1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 DG E 11 O4' - C1' - N9 ANGL. DEV. = 6.7 DEGREES
REMARK 500 DA E 12 O4' - C4' - C3' ANGL. DEV. = -2.7 DEGREES
REMARK 500 DA E 12 O4' - C1' - N9 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DT E 14 O4' - C1' - N1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 DT F 4 O4' - C1' - N1 ANGL. DEV. = 2.9 DEGREES
REMARK 500 DT F 6 C1' - O4' - C4' ANGL. DEV. = -6.1 DEGREES
REMARK 500 DC F 8 O4' - C1' - N1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 DA F 10 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DA F 11 C3' - O3' - P ANGL. DEV. = 7.2 DEGREES
REMARK 500 DG F 12 O4' - C1' - N9 ANGL. DEV. = 3.2 DEGREES
REMARK 500 DT F 15 O4' - C1' - N1 ANGL. DEV. = 2.8 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 10 58.63 26.53
REMARK 500 SER A 103 -171.75 -173.20
REMARK 500 SER A 145 -162.74 -168.39
REMARK 500 LYS A 196 0.47 -68.53
REMARK 500 ASN A 234 47.70 -157.84
REMARK 500 ASP A 277 -112.92 62.94
REMARK 500 TYR B 10 56.93 38.08
REMARK 500 ASN B 20 78.03 -152.14
REMARK 500 PHE B 37 -157.44 -163.90
REMARK 500 SER B 145 -160.90 -163.92
REMARK 500 ASN B 234 45.56 -154.24
REMARK 500 ASP B 277 -104.61 54.04
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 A 354 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 17 O
REMARK 620 2 ALA A 181 O 170.4
REMARK 620 3 ILE A 186 O 93.6 85.8
REMARK 620 4 HOH A 420 O 96.1 92.9 72.3
REMARK 620 5 HOH A 421 O 91.9 92.7 154.6 82.5
REMARK 620 6 HOH A 431 O 80.9 93.8 143.4 144.1 62.0
REMARK 620 7 HOH A 497 O 88.6 82.1 72.1 144.3 132.8 71.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 353 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 25 O
REMARK 620 2 ASP A 7 OD1 74.7
REMARK 620 3 PHE A 8 O 161.8 87.1
REMARK 620 4 ASP A 105 OD2 82.8 94.8 99.0
REMARK 620 5 TMP A 355 O1P 105.5 172.6 92.6 92.5
REMARK 620 6 HOH A 426 O 91.8 79.0 84.6 172.7 93.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 353 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DT E 14 OP1
REMARK 620 2 HOH E 26 O 93.8
REMARK 620 3 ASP B 7 OD1 77.0 170.8
REMARK 620 4 PHE B 8 O 147.2 111.5 77.0
REMARK 620 5 ASP B 105 OD2 79.0 96.1 82.0 77.9
REMARK 620 6 HOH B 368 O 76.3 107.9 70.5 112.9 146.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 354 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH E 15 O
REMARK 620 2 ALA B 181 O 178.4
REMARK 620 3 ILE B 186 O 90.1 89.5
REMARK 620 4 HOH B 402 O 88.8 92.4 148.4
REMARK 620 5 HOH B 406 O 87.4 91.1 70.6 140.8
REMARK 620 N 1 2 3 4
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 353
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 354
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 353
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 354
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP A 355
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 356
DBREF 2RDJ C 1 14 PDB 2RDJ 2RDJ 1 14
DBREF 2RDJ D 3 18 PDB 2RDJ 2RDJ 3 18
DBREF 2RDJ E 1 14 PDB 2RDJ 2RDJ 1 14
DBREF 2RDJ F 4 18 PDB 2RDJ 2RDJ 4 18
DBREF 2RDJ A 1 352 UNP Q97W02 DPO42_SULSO 1 352
DBREF 2RDJ B 1 352 UNP Q97W02 DPO42_SULSO 1 352
SEQRES 1 C 14 DG DG DG DA DC DC DC DT DT DC DG DA DA
SEQRES 2 C 14 DT
SEQRES 1 D 16 DT DT DA DT DT DC DG DA DA DG DG DG DT
SEQRES 2 D 16 DC DC DC
SEQRES 1 E 14 DG DG DG DA DC DC DC DT DT DC DG DA DA
SEQRES 2 E 14 DT
SEQRES 1 F 15 DT DA DT DT DC DG DA DA DG DG DG DT DC
SEQRES 2 F 15 DC DC
SEQRES 1 A 352 MET ILE VAL LEU PHE VAL ASP PHE ASP TYR PHE TYR ALA
SEQRES 2 A 352 GLN VAL GLU GLU VAL LEU ASN PRO SER LEU LYS GLY LYS
SEQRES 3 A 352 PRO VAL VAL VAL CYS VAL PHE SER GLY ARG PHE GLU ASP
SEQRES 4 A 352 SER GLY ALA VAL ALA THR ALA ASN TYR GLU ALA ARG LYS
SEQRES 5 A 352 PHE GLY VAL LYS ALA GLY ILE PRO ILE VAL GLU ALA LYS
SEQRES 6 A 352 LYS ILE LEU PRO ASN ALA VAL TYR LEU PRO MET ARG LYS
SEQRES 7 A 352 GLU VAL TYR GLN GLN VAL SER SER ARG ILE MET ASN LEU
SEQRES 8 A 352 LEU ARG GLU TYR SER GLU LYS ILE GLU ILE ALA SER ILE
SEQRES 9 A 352 ASP GLU ALA TYR LEU ASP ILE SER ASP LYS VAL ARG ASP
SEQRES 10 A 352 TYR ARG GLU ALA TYR ASN LEU GLY LEU GLU ILE LYS ASN
SEQRES 11 A 352 LYS ILE LEU GLU LYS GLU LYS ILE THR VAL THR VAL GLY
SEQRES 12 A 352 ILE SER LYS ASN LYS VAL PHE ALA LYS ILE ALA ALA ASP
SEQRES 13 A 352 MET ALA LYS PRO ASN GLY ILE LYS VAL ILE ASP ASP GLU
SEQRES 14 A 352 GLU VAL LYS ARG LEU ILE ARG GLU LEU ASP ILE ALA ASP
SEQRES 15 A 352 VAL PRO GLY ILE GLY ASN ILE THR ALA GLU LYS LEU LYS
SEQRES 16 A 352 LYS LEU GLY ILE ASN LYS LEU VAL ASP THR LEU SER ILE
SEQRES 17 A 352 GLU PHE ASP LYS LEU LYS GLY MET ILE GLY GLU ALA LYS
SEQRES 18 A 352 ALA LYS TYR LEU ILE SER LEU ALA ARG ASP GLU TYR ASN
SEQRES 19 A 352 GLU PRO ILE ARG THR ARG VAL ARG LYS SER ILE GLY ARG
SEQRES 20 A 352 ILE VAL THR MET LYS ARG ASN SER ARG ASN LEU GLU GLU
SEQRES 21 A 352 ILE LYS PRO TYR LEU PHE ARG ALA ILE GLU GLU SER TYR
SEQRES 22 A 352 TYR LYS LEU ASP LYS ARG ILE PRO LYS ALA ILE HIS VAL
SEQRES 23 A 352 VAL ALA VAL THR GLU ASP LEU ASP ILE VAL SER ARG GLY
SEQRES 24 A 352 ARG THR PHE PRO HIS GLY ILE SER LYS GLU THR ALA TYR
SEQRES 25 A 352 SER GLU SER VAL LYS LEU LEU GLN LYS ILE LEU GLU GLU
SEQRES 26 A 352 ASP GLU ARG LYS ILE ARG ARG ILE GLY VAL ARG PHE SER
SEQRES 27 A 352 LYS PHE ILE GLU ALA ILE GLY LEU ASP LYS PHE PHE ASP
SEQRES 28 A 352 THR
SEQRES 1 B 352 MET ILE VAL LEU PHE VAL ASP PHE ASP TYR PHE TYR ALA
SEQRES 2 B 352 GLN VAL GLU GLU VAL LEU ASN PRO SER LEU LYS GLY LYS
SEQRES 3 B 352 PRO VAL VAL VAL CYS VAL PHE SER GLY ARG PHE GLU ASP
SEQRES 4 B 352 SER GLY ALA VAL ALA THR ALA ASN TYR GLU ALA ARG LYS
SEQRES 5 B 352 PHE GLY VAL LYS ALA GLY ILE PRO ILE VAL GLU ALA LYS
SEQRES 6 B 352 LYS ILE LEU PRO ASN ALA VAL TYR LEU PRO MET ARG LYS
SEQRES 7 B 352 GLU VAL TYR GLN GLN VAL SER SER ARG ILE MET ASN LEU
SEQRES 8 B 352 LEU ARG GLU TYR SER GLU LYS ILE GLU ILE ALA SER ILE
SEQRES 9 B 352 ASP GLU ALA TYR LEU ASP ILE SER ASP LYS VAL ARG ASP
SEQRES 10 B 352 TYR ARG GLU ALA TYR ASN LEU GLY LEU GLU ILE LYS ASN
SEQRES 11 B 352 LYS ILE LEU GLU LYS GLU LYS ILE THR VAL THR VAL GLY
SEQRES 12 B 352 ILE SER LYS ASN LYS VAL PHE ALA LYS ILE ALA ALA ASP
SEQRES 13 B 352 MET ALA LYS PRO ASN GLY ILE LYS VAL ILE ASP ASP GLU
SEQRES 14 B 352 GLU VAL LYS ARG LEU ILE ARG GLU LEU ASP ILE ALA ASP
SEQRES 15 B 352 VAL PRO GLY ILE GLY ASN ILE THR ALA GLU LYS LEU LYS
SEQRES 16 B 352 LYS LEU GLY ILE ASN LYS LEU VAL ASP THR LEU SER ILE
SEQRES 17 B 352 GLU PHE ASP LYS LEU LYS GLY MET ILE GLY GLU ALA LYS
SEQRES 18 B 352 ALA LYS TYR LEU ILE SER LEU ALA ARG ASP GLU TYR ASN
SEQRES 19 B 352 GLU PRO ILE ARG THR ARG VAL ARG LYS SER ILE GLY ARG
SEQRES 20 B 352 ILE VAL THR MET LYS ARG ASN SER ARG ASN LEU GLU GLU
SEQRES 21 B 352 ILE LYS PRO TYR LEU PHE ARG ALA ILE GLU GLU SER TYR
SEQRES 22 B 352 TYR LYS LEU ASP LYS ARG ILE PRO LYS ALA ILE HIS VAL
SEQRES 23 B 352 VAL ALA VAL THR GLU ASP LEU ASP ILE VAL SER ARG GLY
SEQRES 24 B 352 ARG THR PHE PRO HIS GLY ILE SER LYS GLU THR ALA TYR
SEQRES 25 B 352 SER GLU SER VAL LYS LEU LEU GLN LYS ILE LEU GLU GLU
SEQRES 26 B 352 ASP GLU ARG LYS ILE ARG ARG ILE GLY VAL ARG PHE SER
SEQRES 27 B 352 LYS PHE ILE GLU ALA ILE GLY LEU ASP LYS PHE PHE ASP
SEQRES 28 B 352 THR
HET CA A 353 1
HET CA A 354 1
HET TMP A 355 21
HET GOL A 356 6
HET CA B 353 1
HET CA B 354 1
HETNAM CA CALCIUM ION
HETNAM TMP THYMIDINE-5'-PHOSPHATE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 7 CA 4(CA 2+)
FORMUL 9 TMP C10 H15 N2 O8 P
FORMUL 10 GOL C3 H8 O3
FORMUL 13 HOH *305(H2 O)
HELIX 1 1 TYR A 10 ASN A 20 1 11
HELIX 2 2 PRO A 21 LYS A 24 5 4
HELIX 3 3 ASN A 47 LYS A 52 1 6
HELIX 4 4 PRO A 60 LEU A 68 1 9
HELIX 5 5 ARG A 77 ARG A 93 1 17
HELIX 6 6 GLU A 94 SER A 96 5 3
HELIX 7 7 ASP A 117 LYS A 137 1 21
HELIX 8 8 ASN A 147 LYS A 159 1 13
HELIX 9 9 ASP A 167 LEU A 178 1 12
HELIX 10 10 ASP A 179 VAL A 183 5 5
HELIX 11 11 GLY A 187 LYS A 196 1 10
HELIX 12 12 LYS A 201 SER A 207 5 7
HELIX 13 13 GLU A 209 GLY A 218 1 10
HELIX 14 14 GLY A 218 ARG A 230 1 13
HELIX 15 15 ASN A 257 ASP A 277 1 21
HELIX 16 16 SER A 307 ASP A 326 1 20
HELIX 17 17 TYR B 10 ASN B 20 1 11
HELIX 18 18 PRO B 21 LYS B 24 5 4
HELIX 19 19 ASN B 47 PHE B 53 1 7
HELIX 20 20 PRO B 60 LEU B 68 1 9
HELIX 21 21 ARG B 77 ARG B 93 1 17
HELIX 22 22 ASP B 117 LYS B 137 1 21
HELIX 23 23 ASN B 147 LYS B 159 1 13
HELIX 24 24 ASP B 167 LEU B 178 1 12
HELIX 25 25 ASP B 179 VAL B 183 5 5
HELIX 26 26 GLY B 187 LEU B 197 1 11
HELIX 27 27 LYS B 201 SER B 207 5 7
HELIX 28 28 GLU B 209 GLY B 218 1 10
HELIX 29 29 GLY B 218 ARG B 230 1 13
HELIX 30 30 ASN B 257 ASP B 277 1 21
HELIX 31 31 SER B 307 ASP B 326 1 20
SHEET 1 A 5 ILE A 99 SER A 103 0
SHEET 2 A 5 GLU A 106 ASP A 110 -1 O TYR A 108 N GLU A 100
SHEET 3 A 5 VAL A 3 PHE A 8 -1 N LEU A 4 O LEU A 109
SHEET 4 A 5 VAL A 140 SER A 145 -1 O GLY A 143 N PHE A 5
SHEET 5 A 5 ILE A 163 VAL A 165 1 O LYS A 164 N ILE A 144
SHEET 1 B 3 GLY A 41 ALA A 46 0
SHEET 2 B 3 VAL A 28 PHE A 33 -1 N VAL A 32 O ALA A 42
SHEET 3 B 3 VAL A 72 PRO A 75 1 O VAL A 72 N VAL A 29
SHEET 1 C 4 SER A 244 SER A 255 0
SHEET 2 C 4 ILE A 330 PHE A 340 -1 O ILE A 333 N VAL A 249
SHEET 3 C 4 PRO A 281 THR A 290 -1 N VAL A 289 O ARG A 331
SHEET 4 C 4 ILE A 295 THR A 301 -1 O VAL A 296 N ALA A 288
SHEET 1 D 5 ILE B 99 SER B 103 0
SHEET 2 D 5 GLU B 106 ASP B 110 -1 O TYR B 108 N GLU B 100
SHEET 3 D 5 VAL B 3 PHE B 8 -1 N LEU B 4 O LEU B 109
SHEET 4 D 5 VAL B 140 SER B 145 -1 O GLY B 143 N PHE B 5
SHEET 5 D 5 ILE B 163 VAL B 165 1 O LYS B 164 N ILE B 144
SHEET 1 E 3 GLY B 41 ALA B 46 0
SHEET 2 E 3 VAL B 28 PHE B 33 -1 N VAL B 30 O ALA B 44
SHEET 3 E 3 VAL B 72 PRO B 75 1 O VAL B 72 N VAL B 29
SHEET 1 F 4 SER B 244 SER B 255 0
SHEET 2 F 4 ILE B 330 PHE B 340 -1 O PHE B 337 N ILE B 245
SHEET 3 F 4 PRO B 281 THR B 290 -1 N VAL B 289 O ARG B 331
SHEET 4 F 4 ILE B 295 THR B 301 -1 O VAL B 296 N ALA B 288
LINK O HOH C 17 CA CA A 354 1555 1555 2.38
LINK O HOH C 25 CA CA A 353 1555 1555 2.30
LINK OP1 DT E 14 CA CA B 353 1555 1555 2.46
LINK O HOH E 15 CA CA B 354 1555 1555 2.36
LINK O HOH E 26 CA CA B 353 1555 1555 2.46
LINK OD1 ASP A 7 CA CA A 353 1555 1555 2.30
LINK O PHE A 8 CA CA A 353 1555 1555 2.31
LINK OD2 ASP A 105 CA CA A 353 1555 1555 2.30
LINK O ALA A 181 CA CA A 354 1555 1555 2.34
LINK O ILE A 186 CA CA A 354 1555 1555 2.33
LINK CA CA A 353 O1P TMP A 355 1555 1555 2.29
LINK CA CA A 353 O HOH A 426 1555 1555 2.35
LINK CA CA A 354 O HOH A 420 1555 1555 2.27
LINK CA CA A 354 O HOH A 421 1555 1555 2.21
LINK CA CA A 354 O HOH A 431 1555 1555 2.30
LINK CA CA A 354 O HOH A 497 1555 1555 2.34
LINK OD1 ASP B 7 CA CA B 353 1555 1555 2.58
LINK O PHE B 8 CA CA B 353 1555 1555 2.24
LINK OD2 ASP B 105 CA CA B 353 1555 1555 2.30
LINK O ALA B 181 CA CA B 354 1555 1555 2.32
LINK O ILE B 186 CA CA B 354 1555 1555 2.36
LINK CA CA B 353 O HOH B 368 1555 1555 2.31
LINK CA CA B 354 O HOH B 402 1555 1555 2.21
LINK CA CA B 354 O HOH B 406 1555 1555 2.27
CISPEP 1 LYS A 159 PRO A 160 0 0.05
CISPEP 2 LYS B 159 PRO B 160 0 0.77
SITE 1 AC1 6 ASP A 7 PHE A 8 ASP A 105 TMP A 355
SITE 2 AC1 6 HOH A 426 HOH C 25
SITE 1 AC2 7 ALA A 181 ILE A 186 HOH A 420 HOH A 421
SITE 2 AC2 7 HOH A 431 HOH A 497 HOH C 17
SITE 1 AC3 6 ASP B 7 PHE B 8 ASP B 105 HOH B 368
SITE 2 AC3 6 DT E 14 HOH E 26
SITE 1 AC4 5 ALA B 181 ILE B 186 HOH B 402 HOH B 406
SITE 2 AC4 5 HOH E 15
SITE 1 AC5 18 PHE A 8 TYR A 10 PHE A 11 TYR A 12
SITE 2 AC5 18 ALA A 44 THR A 45 ARG A 51 ASP A 105
SITE 3 AC5 18 CA A 353 GOL A 356 HOH A 375 HOH A 427
SITE 4 AC5 18 HOH A 445 HOH A 499 DT C 14 HOH C 25
SITE 5 AC5 18 DT D 4 DA D 5
SITE 1 AC6 5 LYS A 56 ALA A 57 TMP A 355 HOH A 479
SITE 2 AC6 5 HOH A 495
CRYST1 97.993 102.510 106.109 90.00 90.00 90.00 P 21 21 21 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 0.010205 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009755 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009424 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
