HEADER TRANSCRIPTION 08-AUG-03 1OLO
TITLE HEXAMERIC REPLICATIVE DNA HELICASE REPA FROM PLASMID RSF1010 - CUBIC
TITLE 2 CRYSTAL STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: REGULATORY PROTEIN REPA;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: XL1-BLUE;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PTACREP-A;
SOURCE 8 OTHER_DETAILS: BROAD HOST RANGE PLASMID RSF1010
KEYWDS DNA HELICASE, ATPASE, MOTOR PROTEIN, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR T.NIEDENZU,W.SAENGER
REVDAT 8 13-DEC-23 1OLO 1 REMARK
REVDAT 7 22-MAY-19 1OLO 1 REMARK
REVDAT 6 08-MAY-19 1OLO 1 REMARK
REVDAT 5 28-JUN-17 1OLO 1 REMARK
REVDAT 4 13-JUL-11 1OLO 1 VERSN
REVDAT 3 24-FEB-09 1OLO 1 VERSN
REVDAT 2 09-OCT-03 1OLO 1 JRNL
REVDAT 1 19-SEP-03 1OLO 0
JRNL AUTH G.ZIEGELIN,T.NIEDENZU,R.LURZ,W.SAENGER,E.LANKA
JRNL TITL HEXAMERIC RSF1010 HELICASE REPA: THE STRUCTURAL AND
JRNL TITL 2 FUNCTIONAL IMPORTANCE OF SINGLE AMINO ACID RESIDUES
JRNL REF NUCLEIC ACIDS RES. V. 31 5917 2003
JRNL REFN ISSN 0305-1048
JRNL PMID 14530440
JRNL DOI 10.1093/NAR/GKG790
REMARK 2
REMARK 2 RESOLUTION. 2.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 37753
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.600
REMARK 3 FREE R VALUE TEST SET COUNT : 991
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) : 2.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.62
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2726
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2300
REMARK 3 BIN FREE R VALUE SET COUNT : 69
REMARK 3 BIN FREE R VALUE : 0.3020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3810
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 421
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.09
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.207
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.183
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.123
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.671
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
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): 2490 ; 0.829 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3987 ; 1.564 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1475 ; 2.633 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1402 ; 4.223 ; 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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 270
REMARK 3 RESIDUE RANGE : A 300 A 300
REMARK 3 ORIGIN FOR THE GROUP (A): 16.0114 46.1237 61.3307
REMARK 3 T TENSOR
REMARK 3 T11: 0.0858 T22: 0.0722
REMARK 3 T33: 0.0901 T12: 0.0558
REMARK 3 T13: -0.0229 T23: -0.0698
REMARK 3 L TENSOR
REMARK 3 L11: 2.8844 L22: 2.2839
REMARK 3 L33: 1.2197 L12: -1.4067
REMARK 3 L13: -0.2438 L23: -0.4871
REMARK 3 S TENSOR
REMARK 3 S11: 0.1370 S12: 0.1890 S13: -0.4850
REMARK 3 S21: -0.2166 S22: -0.1627 S23: 0.3090
REMARK 3 S31: 0.1982 S32: -0.0354 S33: 0.0257
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 271
REMARK 3 RESIDUE RANGE : B 300 B 300
REMARK 3 ORIGIN FOR THE GROUP (A): 36.2717 21.4605 65.9339
REMARK 3 T TENSOR
REMARK 3 T11: 0.0668 T22: 0.2094
REMARK 3 T33: 0.0874 T12: -0.0144
REMARK 3 T13: -0.0741 T23: 0.0263
REMARK 3 L TENSOR
REMARK 3 L11: 2.3847 L22: 1.8448
REMARK 3 L33: 1.6691 L12: -1.2559
REMARK 3 L13: -0.4701 L23: -0.1718
REMARK 3 S TENSOR
REMARK 3 S11: 0.0311 S12: 0.2764 S13: -0.2422
REMARK 3 S21: -0.1380 S22: 0.0249 S23: 0.2764
REMARK 3 S31: 0.1909 S32: -0.4859 S33: -0.0560
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL PLUS 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: NULL
REMARK 4
REMARK 4 1OLO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-AUG-03.
REMARK 100 THE DEPOSITION ID IS D_1290013293.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-00
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
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 : ENRAF-NONIUS FR571
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
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 : 40046
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.520
REMARK 200 RESOLUTION RANGE LOW (A) : 150.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 7.640
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.52
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.60000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1G8Y
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SITTING DROP VAPOR DIFFUSION AT 291K.
REMARK 280 PROTEIN STOCK: 26MG/ML REPA, 10MM TRIS-HCL PH8.0, 150MM NACL,
REMARK 280 0.1MM EDTA. PRECIPITANT: 100MM TRIS-HCL PH 7.5, 26% PEG400,
REMARK 280 100MM MGSO4, PH 7.50, VAPOR DIFFUSION, SITTING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 3 2
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 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
REMARK 290 13555 Y+1/4,X+3/4,-Z+3/4
REMARK 290 14555 -Y+1/4,-X+1/4,-Z+1/4
REMARK 290 15555 Y+3/4,-X+3/4,Z+1/4
REMARK 290 16555 -Y+3/4,X+1/4,Z+3/4
REMARK 290 17555 X+1/4,Z+3/4,-Y+3/4
REMARK 290 18555 -X+3/4,Z+1/4,Y+3/4
REMARK 290 19555 -X+1/4,-Z+1/4,-Y+1/4
REMARK 290 20555 X+3/4,-Z+3/4,Y+1/4
REMARK 290 21555 Z+1/4,Y+3/4,-X+3/4
REMARK 290 22555 Z+3/4,-Y+3/4,X+1/4
REMARK 290 23555 -Z+3/4,Y+1/4,X+3/4
REMARK 290 24555 -Z+1/4,-Y+1/4,-X+1/4
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 95.14650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 95.14650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 95.14650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 95.14650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 95.14650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 95.14650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 95.14650
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 95.14650
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 95.14650
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 95.14650
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 95.14650
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 95.14650
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 95.14650
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 95.14650
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 95.14650
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 95.14650
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 95.14650
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 95.14650
REMARK 290 SMTRY1 13 0.000000 1.000000 0.000000 47.57325
REMARK 290 SMTRY2 13 1.000000 0.000000 0.000000 142.71975
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 142.71975
REMARK 290 SMTRY1 14 0.000000 -1.000000 0.000000 47.57325
REMARK 290 SMTRY2 14 -1.000000 0.000000 0.000000 47.57325
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 47.57325
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 142.71975
REMARK 290 SMTRY2 15 -1.000000 0.000000 0.000000 142.71975
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 47.57325
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 142.71975
REMARK 290 SMTRY2 16 1.000000 0.000000 0.000000 47.57325
REMARK 290 SMTRY3 16 0.000000 0.000000 1.000000 142.71975
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 47.57325
REMARK 290 SMTRY2 17 0.000000 0.000000 1.000000 142.71975
REMARK 290 SMTRY3 17 0.000000 -1.000000 0.000000 142.71975
REMARK 290 SMTRY1 18 -1.000000 0.000000 0.000000 142.71975
REMARK 290 SMTRY2 18 0.000000 0.000000 1.000000 47.57325
REMARK 290 SMTRY3 18 0.000000 1.000000 0.000000 142.71975
REMARK 290 SMTRY1 19 -1.000000 0.000000 0.000000 47.57325
REMARK 290 SMTRY2 19 0.000000 0.000000 -1.000000 47.57325
REMARK 290 SMTRY3 19 0.000000 -1.000000 0.000000 47.57325
REMARK 290 SMTRY1 20 1.000000 0.000000 0.000000 142.71975
REMARK 290 SMTRY2 20 0.000000 0.000000 -1.000000 142.71975
REMARK 290 SMTRY3 20 0.000000 1.000000 0.000000 47.57325
REMARK 290 SMTRY1 21 0.000000 0.000000 1.000000 47.57325
REMARK 290 SMTRY2 21 0.000000 1.000000 0.000000 142.71975
REMARK 290 SMTRY3 21 -1.000000 0.000000 0.000000 142.71975
REMARK 290 SMTRY1 22 0.000000 0.000000 1.000000 142.71975
REMARK 290 SMTRY2 22 0.000000 -1.000000 0.000000 142.71975
REMARK 290 SMTRY3 22 1.000000 0.000000 0.000000 47.57325
REMARK 290 SMTRY1 23 0.000000 0.000000 -1.000000 142.71975
REMARK 290 SMTRY2 23 0.000000 1.000000 0.000000 47.57325
REMARK 290 SMTRY3 23 1.000000 0.000000 0.000000 142.71975
REMARK 290 SMTRY1 24 0.000000 0.000000 -1.000000 47.57325
REMARK 290 SMTRY2 24 0.000000 -1.000000 0.000000 47.57325
REMARK 290 SMTRY3 24 -1.000000 0.000000 0.000000 47.57325
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 300 REMARK: THE ASSEMBLY DESCRIBED BELOW IS A HOMOHEXAMERIC ASSEMBLY.
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 21590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -228.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 1.000000 0.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2016 LIES ON A SPECIAL POSITION.
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 MET A 1
REMARK 465 SER A 181
REMARK 465 LYS A 182
REMARK 465 GLY A 183
REMARK 465 ALA A 184
REMARK 465 ALA A 185
REMARK 465 MET A 186
REMARK 465 MET A 187
REMARK 465 GLY A 188
REMARK 465 ALA A 189
REMARK 465 GLY A 190
REMARK 465 ASP A 191
REMARK 465 GLN A 192
REMARK 465 GLN A 193
REMARK 465 GLN A 194
REMARK 465 ALA A 195
REMARK 465 SER A 196
REMARK 465 ARG A 197
REMARK 465 GLY A 198
REMARK 465 SER A 199
REMARK 465 SER A 200
REMARK 465 SER A 271
REMARK 465 LYS A 272
REMARK 465 GLY A 273
REMARK 465 VAL A 274
REMARK 465 PRO A 275
REMARK 465 ARG A 276
REMARK 465 GLY A 277
REMARK 465 GLU A 278
REMARK 465 ALA A 279
REMARK 465 MET B 1
REMARK 465 SER B 181
REMARK 465 LYS B 182
REMARK 465 GLY B 183
REMARK 465 ALA B 184
REMARK 465 ALA B 185
REMARK 465 MET B 186
REMARK 465 MET B 187
REMARK 465 GLY B 188
REMARK 465 ALA B 189
REMARK 465 GLY B 190
REMARK 465 ASP B 191
REMARK 465 GLN B 192
REMARK 465 GLN B 193
REMARK 465 GLN B 194
REMARK 465 ALA B 195
REMARK 465 SER B 196
REMARK 465 ARG B 197
REMARK 465 GLY B 198
REMARK 465 SER B 199
REMARK 465 SER B 200
REMARK 465 LYS B 272
REMARK 465 GLY B 273
REMARK 465 VAL B 274
REMARK 465 PRO B 275
REMARK 465 ARG B 276
REMARK 465 GLY B 277
REMARK 465 GLU B 278
REMARK 465 ALA B 279
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 O HOH A 2198 O HOH A 2201 1.67
REMARK 500 O HOH B 2040 O HOH B 2041 1.74
REMARK 500 O HOH B 2041 O HOH B 2136 2.00
REMARK 500 O ALA B 16 O HOH B 2032 2.05
REMARK 500 OE2 GLU A 221 O HOH A 2173 2.09
REMARK 500 CA GLY A 244 O HOH A 2025 2.10
REMARK 500 O HOH B 2065 O HOH B 2194 2.14
REMARK 500 O HOH A 2152 O HOH A 2153 2.17
REMARK 500 CE1 TYR B 73 O HOH B 2097 2.18
REMARK 500 NH1 ARG A 86 O HOH A 2090 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 NE2 HIS A 85 O PRO B 18 9555 1.92
REMARK 500 CB PRO B 18 O HOH B 2018 13545 2.06
REMARK 500 O HOH B 2018 O HOH B 2018 13545 2.13
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 ARG B 129 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG B 134 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG B 134 NE - CZ - NH2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 ARG B 162 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP B 204 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG B 207 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG B 207 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP B 228 CB - CG - OD2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 VAL B 234 CB - CA - C ANGL. DEV. = -13.8 DEGREES
REMARK 500 ASP B 249 CB - CG - OD2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 ASP B 256 CB - CG - OD2 ANGL. DEV. = 6.8 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 243 144.15 -34.04
REMARK 500 PRO B 17 97.71 -60.41
REMARK 500 GLU B 221 43.06 -76.21
REMARK 500 GLU B 222 -22.98 -167.29
REMARK 500 ARG B 267 135.27 85.11
REMARK 500 ARG B 269 88.73 -61.03
REMARK 500 LYS B 270 98.01 -57.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2016 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH A2022 DISTANCE = 6.89 ANGSTROMS
REMARK 525 HOH B2045 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH B2081 DISTANCE = 6.62 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 300
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1G8Y RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HEXAMERIC REPLICATIVE HELICASE REPA OF
REMARK 900 PLASMID RSF1010
REMARK 900 RELATED ID: 1NLF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DNA HELICASE REPA IN COMPLEX WITH SULFATE AT
REMARK 900 1.95 A RESOLUTION
DBREF 1OLO A 1 279 UNP P20356 REPJ_ECOLI 1 279
DBREF 1OLO B 1 279 UNP P20356 REPJ_ECOLI 1 279
SEQRES 1 A 279 MET ALA THR HIS LYS PRO ILE ASN ILE LEU GLU ALA PHE
SEQRES 2 A 279 ALA ALA ALA PRO PRO PRO LEU ASP TYR VAL LEU PRO ASN
SEQRES 3 A 279 MET VAL ALA GLY THR VAL GLY ALA LEU VAL SER PRO GLY
SEQRES 4 A 279 GLY ALA GLY LYS SER MET LEU ALA LEU GLN LEU ALA ALA
SEQRES 5 A 279 GLN ILE ALA GLY GLY PRO ASP LEU LEU GLU VAL GLY GLU
SEQRES 6 A 279 LEU PRO THR GLY PRO VAL ILE TYR LEU PRO ALA GLU ASP
SEQRES 7 A 279 PRO PRO THR ALA ILE HIS HIS ARG LEU HIS ALA LEU GLY
SEQRES 8 A 279 ALA HIS LEU SER ALA GLU GLU ARG GLN ALA VAL ALA ASP
SEQRES 9 A 279 GLY LEU LEU ILE GLN PRO LEU ILE GLY SER LEU PRO ASN
SEQRES 10 A 279 ILE MET ALA PRO GLU TRP PHE ASP GLY LEU LYS ARG ALA
SEQRES 11 A 279 ALA GLU GLY ARG ARG LEU MET VAL LEU ASP THR LEU ARG
SEQRES 12 A 279 ARG PHE HIS ILE GLU GLU GLU ASN ALA SER GLY PRO MET
SEQRES 13 A 279 ALA GLN VAL ILE GLY ARG MET GLU ALA ILE ALA ALA ASP
SEQRES 14 A 279 THR GLY CYS SER ILE VAL PHE LEU HIS HIS ALA SER LYS
SEQRES 15 A 279 GLY ALA ALA MET MET GLY ALA GLY ASP GLN GLN GLN ALA
SEQRES 16 A 279 SER ARG GLY SER SER VAL LEU VAL ASP ASN ILE ARG TRP
SEQRES 17 A 279 GLN SER TYR LEU SER SER MET THR SER ALA GLU ALA GLU
SEQRES 18 A 279 GLU TRP GLY VAL ASP ASP ASP GLN ARG ARG PHE PHE VAL
SEQRES 19 A 279 ARG PHE GLY VAL SER LYS ALA ASN TYR GLY ALA PRO PHE
SEQRES 20 A 279 ALA ASP ARG TRP PHE ARG ARG HIS ASP GLY GLY VAL LEU
SEQRES 21 A 279 LYS PRO ALA VAL LEU GLU ARG GLN ARG LYS SER LYS GLY
SEQRES 22 A 279 VAL PRO ARG GLY GLU ALA
SEQRES 1 B 279 MET ALA THR HIS LYS PRO ILE ASN ILE LEU GLU ALA PHE
SEQRES 2 B 279 ALA ALA ALA PRO PRO PRO LEU ASP TYR VAL LEU PRO ASN
SEQRES 3 B 279 MET VAL ALA GLY THR VAL GLY ALA LEU VAL SER PRO GLY
SEQRES 4 B 279 GLY ALA GLY LYS SER MET LEU ALA LEU GLN LEU ALA ALA
SEQRES 5 B 279 GLN ILE ALA GLY GLY PRO ASP LEU LEU GLU VAL GLY GLU
SEQRES 6 B 279 LEU PRO THR GLY PRO VAL ILE TYR LEU PRO ALA GLU ASP
SEQRES 7 B 279 PRO PRO THR ALA ILE HIS HIS ARG LEU HIS ALA LEU GLY
SEQRES 8 B 279 ALA HIS LEU SER ALA GLU GLU ARG GLN ALA VAL ALA ASP
SEQRES 9 B 279 GLY LEU LEU ILE GLN PRO LEU ILE GLY SER LEU PRO ASN
SEQRES 10 B 279 ILE MET ALA PRO GLU TRP PHE ASP GLY LEU LYS ARG ALA
SEQRES 11 B 279 ALA GLU GLY ARG ARG LEU MET VAL LEU ASP THR LEU ARG
SEQRES 12 B 279 ARG PHE HIS ILE GLU GLU GLU ASN ALA SER GLY PRO MET
SEQRES 13 B 279 ALA GLN VAL ILE GLY ARG MET GLU ALA ILE ALA ALA ASP
SEQRES 14 B 279 THR GLY CYS SER ILE VAL PHE LEU HIS HIS ALA SER LYS
SEQRES 15 B 279 GLY ALA ALA MET MET GLY ALA GLY ASP GLN GLN GLN ALA
SEQRES 16 B 279 SER ARG GLY SER SER VAL LEU VAL ASP ASN ILE ARG TRP
SEQRES 17 B 279 GLN SER TYR LEU SER SER MET THR SER ALA GLU ALA GLU
SEQRES 18 B 279 GLU TRP GLY VAL ASP ASP ASP GLN ARG ARG PHE PHE VAL
SEQRES 19 B 279 ARG PHE GLY VAL SER LYS ALA ASN TYR GLY ALA PRO PHE
SEQRES 20 B 279 ALA ASP ARG TRP PHE ARG ARG HIS ASP GLY GLY VAL LEU
SEQRES 21 B 279 LYS PRO ALA VAL LEU GLU ARG GLN ARG LYS SER LYS GLY
SEQRES 22 B 279 VAL PRO ARG GLY GLU ALA
HET SO4 A 300 5
HET SO4 B 300 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 HOH *421(H2 O)
HELIX 1 1 ASN A 8 ALA A 15 1 8
HELIX 2 2 GLY A 42 GLY A 56 1 15
HELIX 3 3 PRO A 79 ALA A 92 1 14
HELIX 4 4 SER A 95 GLY A 105 1 11
HELIX 5 5 ALA A 120 GLU A 132 1 13
HELIX 6 6 THR A 141 HIS A 146 5 6
HELIX 7 7 ALA A 152 GLY A 171 1 20
HELIX 8 8 THR A 216 TRP A 223 1 8
HELIX 9 9 ASP A 226 ARG A 231 5 6
HELIX 10 10 ASP A 256 GLY A 258 5 3
HELIX 11 11 ASN B 8 ALA B 15 1 8
HELIX 12 12 GLY B 42 ALA B 55 1 14
HELIX 13 13 PRO B 79 ALA B 92 1 14
HELIX 14 14 SER B 95 GLY B 105 1 11
HELIX 15 15 ALA B 120 GLU B 132 1 13
HELIX 16 16 THR B 141 HIS B 146 5 6
HELIX 17 17 ALA B 152 GLY B 171 1 20
HELIX 18 18 VAL B 201 ILE B 206 1 6
HELIX 19 19 THR B 216 GLU B 221 1 6
HELIX 20 20 ASP B 226 ARG B 231 5 6
HELIX 21 21 ASP B 256 GLY B 258 5 3
SHEET 1 AA 2 TYR A 22 LEU A 24 0
SHEET 2 AA 2 MET A 27 VAL A 28 -1 O MET A 27 N VAL A 23
SHEET 1 AB 9 LEU A 106 ILE A 108 0
SHEET 2 AB 9 VAL A 71 PRO A 75 1 O VAL A 71 N LEU A 107
SHEET 3 AB 9 LEU A 136 ASP A 140 1 O LEU A 136 N ILE A 72
SHEET 4 AB 9 SER A 173 HIS A 179 1 O SER A 173 N MET A 137
SHEET 5 AB 9 VAL A 32 SER A 37 1 O GLY A 33 N PHE A 176
SHEET 6 AB 9 TRP A 208 SER A 214 1 O TRP A 208 N ALA A 34
SHEET 7 AB 9 PHE A 233 LYS A 240 -1 O ARG A 235 N SER A 213
SHEET 8 AB 9 ARG A 250 ARG A 254 -1 O ARG A 250 N PHE A 236
SHEET 9 AB 9 LEU A 260 PRO A 262 -1 O LYS A 261 N ARG A 253
SHEET 1 BA 2 TYR B 22 LEU B 24 0
SHEET 2 BA 2 MET B 27 VAL B 28 -1 O MET B 27 N VAL B 23
SHEET 1 BB 9 LEU B 106 ILE B 108 0
SHEET 2 BB 9 VAL B 71 PRO B 75 1 O VAL B 71 N LEU B 107
SHEET 3 BB 9 LEU B 136 ASP B 140 1 O LEU B 136 N ILE B 72
SHEET 4 BB 9 SER B 173 HIS B 179 1 O SER B 173 N MET B 137
SHEET 5 BB 9 VAL B 32 SER B 37 1 O GLY B 33 N PHE B 176
SHEET 6 BB 9 TRP B 208 SER B 214 1 O TRP B 208 N ALA B 34
SHEET 7 BB 9 PHE B 233 LYS B 240 -1 O ARG B 235 N SER B 213
SHEET 8 BB 9 ARG B 250 ARG B 254 -1 O ARG B 250 N PHE B 236
SHEET 9 BB 9 LEU B 260 PRO B 262 -1 O LYS B 261 N ARG B 253
CISPEP 1 ASP A 140 THR A 141 0 -9.29
CISPEP 2 ASP B 140 THR B 141 0 -8.28
SITE 1 AC1 10 SER A 37 GLY A 39 GLY A 40 ALA A 41
SITE 2 AC1 10 GLY A 42 LYS A 43 SER A 44 HIS A 179
SITE 3 AC1 10 HOH A2136 HOH B2193
SITE 1 AC2 9 ARG A 207 GLY B 40 ALA B 41 GLY B 42
SITE 2 AC2 9 LYS B 43 SER B 44 HIS B 179 HOH B2208
SITE 3 AC2 9 HOH B2209
CRYST1 190.293 190.293 190.293 90.00 90.00 90.00 P 43 3 2 48
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 0.005255 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005255 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005255 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
