HEADER DNA BINDING PROTEIN 17-JUL-18 6E49
TITLE PIF1 PEPTIDE BOUND TO PCNA TRIMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLIFERATING CELL NUCLEAR ANTIGEN;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: PCNA;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ATP-DEPENDENT DNA HELICASE PIF1;
COMPND 8 CHAIN: D, E, F;
COMPND 9 FRAGMENT: UNP RESIDUES 815-831;
COMPND 10 SYNONYM: DNA REPAIR AND RECOMBINATION HELICASE PIF1, PETITE
COMPND 11 INTEGRATION FREQUENCY PROTEIN 1, TELOMERE STABILITY PROTEIN 1;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 3 S288C);
SOURCE 4 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 5 ORGANISM_TAXID: 559292;
SOURCE 6 STRAIN: ATCC 204508 / S288C;
SOURCE 7 GENE: POL30, YBR088C, YBR0811;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 12 S288C);
SOURCE 13 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 14 ORGANISM_TAXID: 559292;
SOURCE 15 STRAIN: ATCC 204508 / S288C;
SOURCE 16 GENE: PIF1, TST1, YML061C, YM9958.01C;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 511693
KEYWDS COMPLEX, PCNA, PIF1 PEPTIDE, DNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR O.BUZOVETSKY,Y.KWON,N.T.PHAM,C.KIM,G.IRA,P.SUNG,Y.XIONG
REVDAT 2 13-MAR-24 6E49 1 REMARK
REVDAT 1 22-AUG-18 6E49 0
SPRSDE 22-AUG-18 6E49 6B8I
JRNL AUTH O.BUZOVETSKY,Y.KWON,N.T.PHAM,C.KIM,G.IRA,P.SUNG,Y.XIONG
JRNL TITL ROLE OF THE PIF1-PCNA COMPLEX IN POL DELTA-DEPENDENT STRAND
JRNL TITL 2 DISPLACEMENT DNA SYNTHESIS AND BREAK-INDUCED REPLICATION.
JRNL REF CELL REP V. 21 1707 2017
JRNL REFN ESSN 2211-1247
JRNL PMID 29141206
JRNL DOI 10.1016/J.CELREP.2017.10.079
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 18.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.6
REMARK 3 NUMBER OF REFLECTIONS : 20619
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) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1135
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1482
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.45
REMARK 3 BIN R VALUE (WORKING SET) : 0.3370
REMARK 3 BIN FREE R VALUE SET COUNT : 80
REMARK 3 BIN FREE R VALUE : 0.3880
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6258
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 8
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.89000
REMARK 3 B22 (A**2) : 3.47000
REMARK 3 B33 (A**2) : -0.52000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.73000
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): 0.422
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.361
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 42.000
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.919
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6347 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 6117 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8549 ; 1.989 ; 1.991
REMARK 3 BOND ANGLES OTHERS (DEGREES): 14235 ; 1.061 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 791 ; 8.168 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 278 ;38.355 ;25.360
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1211 ;21.883 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 29 ;19.478 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1008 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6920 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1205 ; 0.002 ; 0.020
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): 3182 ; 5.050 ; 7.186
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3181 ; 5.045 ; 7.183
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3967 ; 8.301 ;10.760
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3968 ; 8.302 ;10.764
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3165 ; 5.270 ; 7.777
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3166 ; 5.269 ; 7.779
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4583 ; 8.577 ;11.449
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 24606 ;15.349 ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 24607 ;15.348 ; 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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 3
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 1 255 B 1 255 15416 0.08 0.05
REMARK 3 2 A 1 253 C 1 253 15478 0.06 0.05
REMARK 3 3 B 1 253 C 1 253 15402 0.07 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 127
REMARK 3 ORIGIN FOR THE GROUP (A): 3.6704 -2.6939 21.2719
REMARK 3 T TENSOR
REMARK 3 T11: 0.4052 T22: 0.3912
REMARK 3 T33: 0.3897 T12: 0.0684
REMARK 3 T13: 0.0469 T23: -0.0430
REMARK 3 L TENSOR
REMARK 3 L11: 3.1627 L22: 0.0426
REMARK 3 L33: 2.5068 L12: -0.0776
REMARK 3 L13: 1.0157 L23: -0.0723
REMARK 3 S TENSOR
REMARK 3 S11: -0.0081 S12: -0.1978 S13: 0.3767
REMARK 3 S21: -0.0803 S22: -0.0657 S23: 0.0500
REMARK 3 S31: 0.3417 S32: 0.4009 S33: 0.0738
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 127
REMARK 3 ORIGIN FOR THE GROUP (A): -45.9912 2.6970 23.5772
REMARK 3 T TENSOR
REMARK 3 T11: 0.4652 T22: 0.2366
REMARK 3 T33: 0.4713 T12: -0.0245
REMARK 3 T13: 0.1198 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 1.1048 L22: 0.8606
REMARK 3 L33: 2.2310 L12: 0.2921
REMARK 3 L13: -1.2434 L23: -0.1326
REMARK 3 S TENSOR
REMARK 3 S11: -0.1147 S12: 0.1044 S13: 0.0263
REMARK 3 S21: 0.1460 S22: -0.0147 S23: 0.1167
REMARK 3 S31: -0.0936 S32: -0.2815 S33: 0.1294
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 127
REMARK 3 ORIGIN FOR THE GROUP (A): -19.3763 -4.0057 65.2756
REMARK 3 T TENSOR
REMARK 3 T11: 0.5061 T22: 0.7030
REMARK 3 T33: 0.0194 T12: 0.1344
REMARK 3 T13: 0.0777 T23: -0.0370
REMARK 3 L TENSOR
REMARK 3 L11: 2.8136 L22: 0.4968
REMARK 3 L33: 0.5821 L12: -0.1939
REMARK 3 L13: 0.7836 L23: -0.4720
REMARK 3 S TENSOR
REMARK 3 S11: 0.2321 S12: -0.6934 S13: 0.1594
REMARK 3 S21: -0.0644 S22: -0.2582 S23: 0.0110
REMARK 3 S31: 0.1311 S32: 0.0961 S33: 0.0262
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 128 A 255
REMARK 3 ORIGIN FOR THE GROUP (A): 5.4884 -7.1058 48.1443
REMARK 3 T TENSOR
REMARK 3 T11: 0.4722 T22: 0.8416
REMARK 3 T33: 0.0552 T12: 0.2691
REMARK 3 T13: -0.0713 T23: -0.1243
REMARK 3 L TENSOR
REMARK 3 L11: 1.9175 L22: 0.6960
REMARK 3 L33: 3.9957 L12: -0.9777
REMARK 3 L13: -1.2123 L23: 1.2545
REMARK 3 S TENSOR
REMARK 3 S11: -0.3934 S12: -0.7687 S13: 0.1680
REMARK 3 S21: 0.0779 S22: 0.3522 S23: -0.0200
REMARK 3 S31: 0.4423 S32: 0.8424 S33: 0.0412
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 128 B 255
REMARK 3 ORIGIN FOR THE GROUP (A): -23.6821 -1.0786 8.3192
REMARK 3 T TENSOR
REMARK 3 T11: 0.5819 T22: 0.1638
REMARK 3 T33: 0.4129 T12: -0.0459
REMARK 3 T13: 0.0722 T23: 0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 2.0096 L22: 1.2418
REMARK 3 L33: 0.5918 L12: 0.0608
REMARK 3 L13: -0.5352 L23: -0.1767
REMARK 3 S TENSOR
REMARK 3 S11: 0.1424 S12: 0.1904 S13: -0.0430
REMARK 3 S21: 0.0130 S22: -0.2235 S23: -0.0295
REMARK 3 S31: -0.0369 S32: -0.0484 S33: 0.0811
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 128 C 254
REMARK 3 ORIGIN FOR THE GROUP (A): -43.8544 -1.9224 53.3301
REMARK 3 T TENSOR
REMARK 3 T11: 0.5349 T22: 0.3558
REMARK 3 T33: 0.3242 T12: 0.0966
REMARK 3 T13: 0.2080 T23: -0.0309
REMARK 3 L TENSOR
REMARK 3 L11: 2.3270 L22: 0.4065
REMARK 3 L33: 2.9633 L12: -0.6544
REMARK 3 L13: 0.8429 L23: -0.8205
REMARK 3 S TENSOR
REMARK 3 S11: -0.1198 S12: -0.6053 S13: -0.0613
REMARK 3 S21: -0.1190 S22: 0.0561 S23: -0.0231
REMARK 3 S31: -0.0203 S32: -0.2940 S33: 0.0638
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 6E49 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUL-18.
REMARK 100 THE DEPOSITION ID IS D_1000235691.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21636
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 18.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.9
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.96000
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MIB (QIAGEN), PH 9.0, 25%
REMARK 280 PEG1500, MICROBATCH, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
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 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 84.67300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 20.89750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 84.67300
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 20.89750
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 MET A -13
REMARK 465 GLY A -12
REMARK 465 SER A -11
REMARK 465 SER A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 SER A -3
REMARK 465 GLN A -2
REMARK 465 ASP A -1
REMARK 465 PRO A 0
REMARK 465 ASP A 256
REMARK 465 GLU A 257
REMARK 465 GLU A 258
REMARK 465 MET B -13
REMARK 465 GLY B -12
REMARK 465 SER B -11
REMARK 465 SER B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 SER B -3
REMARK 465 GLN B -2
REMARK 465 ASP B -1
REMARK 465 PRO B 0
REMARK 465 ASP B 256
REMARK 465 GLU B 257
REMARK 465 GLU B 258
REMARK 465 MET C -13
REMARK 465 GLY C -12
REMARK 465 SER C -11
REMARK 465 SER C -10
REMARK 465 HIS C -9
REMARK 465 HIS C -8
REMARK 465 HIS C -7
REMARK 465 HIS C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 SER C -3
REMARK 465 GLN C -2
REMARK 465 ASP C -1
REMARK 465 PRO C 0
REMARK 465 ASN C 255
REMARK 465 ASP C 256
REMARK 465 GLU C 257
REMARK 465 GLU C 258
REMARK 465 ASN E 815
REMARK 465 HIS E 824
REMARK 465 SER E 825
REMARK 465 ARG E 826
REMARK 465 LYS E 827
REMARK 465 ARG E 828
REMARK 465 PHE E 829
REMARK 465 GLN E 830
REMARK 465 LEU E 831
REMARK 465 ASN F 815
REMARK 465 HIS F 824
REMARK 465 SER F 825
REMARK 465 ARG F 826
REMARK 465 LYS F 827
REMARK 465 ARG F 828
REMARK 465 PHE F 829
REMARK 465 GLN F 830
REMARK 465 LEU F 831
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 GLU B 55 CG GLU B 55 CD 0.113
REMARK 500 GLU B 143 CD GLU B 143 OE1 0.066
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 PHE A 19 CB - CA - C ANGL. DEV. = -20.8 DEGREES
REMARK 500 PHE A 19 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 LYS A 20 CA - CB - CG ANGL. DEV. = 13.8 DEGREES
REMARK 500 ARG A 80 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP B 17 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 PHE B 19 CB - CA - C ANGL. DEV. = -20.9 DEGREES
REMARK 500 PHE B 19 CB - CG - CD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 LEU B 47 CA - CB - CG ANGL. DEV. = 15.4 DEGREES
REMARK 500 GLU B 189 OE1 - CD - OE2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 PHE C 19 CB - CA - C ANGL. DEV. = -21.0 DEGREES
REMARK 500 PHE C 19 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG D 826 NE - CZ - NH1 ANGL. DEV. = 3.1 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 CYS A 22 -13.57 66.21
REMARK 500 VAL A 23 121.11 -172.33
REMARK 500 LYS A 108 76.84 -54.89
REMARK 500 ARG A 110 83.03 51.71
REMARK 500 LYS A 242 104.64 -58.77
REMARK 500 CYS B 22 -15.08 66.05
REMARK 500 VAL B 23 122.10 -171.59
REMARK 500 LEU B 79 40.16 -100.71
REMARK 500 THR B 95 66.73 39.76
REMARK 500 LYS B 108 73.20 -49.65
REMARK 500 ARG B 110 82.18 53.00
REMARK 500 CYS C 22 -13.81 67.36
REMARK 500 VAL C 23 122.04 -171.79
REMARK 500 LYS C 108 77.28 -55.91
REMARK 500 ARG C 110 83.66 48.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PHE A 19 LYS A 20 -147.97
REMARK 500 LEU A 79 ARG A 80 147.09
REMARK 500 GLU A 232 ALA A 233 -143.37
REMARK 500 PHE B 19 LYS B 20 -146.23
REMARK 500 LEU B 79 ARG B 80 143.95
REMARK 500 GLU B 232 ALA B 233 -143.98
REMARK 500 PHE C 19 LYS C 20 -149.70
REMARK 500 LEU C 79 ARG C 80 146.71
REMARK 500 GLU C 232 ALA C 233 -145.07
REMARK 500 GLN D 830 LEU D 831 -144.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 PHE B 19 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 PHE B 19 10.44
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6E49 A 1 258 UNP P15873 PCNA_YEAST 1 258
DBREF 6E49 B 1 258 UNP P15873 PCNA_YEAST 1 258
DBREF 6E49 C 1 258 UNP P15873 PCNA_YEAST 1 258
DBREF 6E49 D 815 831 UNP P07271 PIF1_YEAST 815 831
DBREF 6E49 E 815 831 UNP P07271 PIF1_YEAST 815 831
DBREF 6E49 F 815 831 UNP P07271 PIF1_YEAST 815 831
SEQADV 6E49 MET A -13 UNP P15873 EXPRESSION TAG
SEQADV 6E49 GLY A -12 UNP P15873 EXPRESSION TAG
SEQADV 6E49 SER A -11 UNP P15873 EXPRESSION TAG
SEQADV 6E49 SER A -10 UNP P15873 EXPRESSION TAG
SEQADV 6E49 HIS A -9 UNP P15873 EXPRESSION TAG
SEQADV 6E49 HIS A -8 UNP P15873 EXPRESSION TAG
SEQADV 6E49 HIS A -7 UNP P15873 EXPRESSION TAG
SEQADV 6E49 HIS A -6 UNP P15873 EXPRESSION TAG
SEQADV 6E49 HIS A -5 UNP P15873 EXPRESSION TAG
SEQADV 6E49 HIS A -4 UNP P15873 EXPRESSION TAG
SEQADV 6E49 SER A -3 UNP P15873 EXPRESSION TAG
SEQADV 6E49 GLN A -2 UNP P15873 EXPRESSION TAG
SEQADV 6E49 ASP A -1 UNP P15873 EXPRESSION TAG
SEQADV 6E49 PRO A 0 UNP P15873 EXPRESSION TAG
SEQADV 6E49 MET B -13 UNP P15873 EXPRESSION TAG
SEQADV 6E49 GLY B -12 UNP P15873 EXPRESSION TAG
SEQADV 6E49 SER B -11 UNP P15873 EXPRESSION TAG
SEQADV 6E49 SER B -10 UNP P15873 EXPRESSION TAG
SEQADV 6E49 HIS B -9 UNP P15873 EXPRESSION TAG
SEQADV 6E49 HIS B -8 UNP P15873 EXPRESSION TAG
SEQADV 6E49 HIS B -7 UNP P15873 EXPRESSION TAG
SEQADV 6E49 HIS B -6 UNP P15873 EXPRESSION TAG
SEQADV 6E49 HIS B -5 UNP P15873 EXPRESSION TAG
SEQADV 6E49 HIS B -4 UNP P15873 EXPRESSION TAG
SEQADV 6E49 SER B -3 UNP P15873 EXPRESSION TAG
SEQADV 6E49 GLN B -2 UNP P15873 EXPRESSION TAG
SEQADV 6E49 ASP B -1 UNP P15873 EXPRESSION TAG
SEQADV 6E49 PRO B 0 UNP P15873 EXPRESSION TAG
SEQADV 6E49 MET C -13 UNP P15873 EXPRESSION TAG
SEQADV 6E49 GLY C -12 UNP P15873 EXPRESSION TAG
SEQADV 6E49 SER C -11 UNP P15873 EXPRESSION TAG
SEQADV 6E49 SER C -10 UNP P15873 EXPRESSION TAG
SEQADV 6E49 HIS C -9 UNP P15873 EXPRESSION TAG
SEQADV 6E49 HIS C -8 UNP P15873 EXPRESSION TAG
SEQADV 6E49 HIS C -7 UNP P15873 EXPRESSION TAG
SEQADV 6E49 HIS C -6 UNP P15873 EXPRESSION TAG
SEQADV 6E49 HIS C -5 UNP P15873 EXPRESSION TAG
SEQADV 6E49 HIS C -4 UNP P15873 EXPRESSION TAG
SEQADV 6E49 SER C -3 UNP P15873 EXPRESSION TAG
SEQADV 6E49 GLN C -2 UNP P15873 EXPRESSION TAG
SEQADV 6E49 ASP C -1 UNP P15873 EXPRESSION TAG
SEQADV 6E49 PRO C 0 UNP P15873 EXPRESSION TAG
SEQRES 1 A 272 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 A 272 PRO MET LEU GLU ALA LYS PHE GLU GLU ALA SER LEU PHE
SEQRES 3 A 272 LYS ARG ILE ILE ASP GLY PHE LYS ASP CYS VAL GLN LEU
SEQRES 4 A 272 VAL ASN PHE GLN CYS LYS GLU ASP GLY ILE ILE ALA GLN
SEQRES 5 A 272 ALA VAL ASP ASP SER ARG VAL LEU LEU VAL SER LEU GLU
SEQRES 6 A 272 ILE GLY VAL GLU ALA PHE GLN GLU TYR ARG CYS ASP HIS
SEQRES 7 A 272 PRO VAL THR LEU GLY MET ASP LEU THR SER LEU SER LYS
SEQRES 8 A 272 ILE LEU ARG CYS GLY ASN ASN THR ASP THR LEU THR LEU
SEQRES 9 A 272 ILE ALA ASP ASN THR PRO ASP SER ILE ILE LEU LEU PHE
SEQRES 10 A 272 GLU ASP THR LYS LYS ASP ARG ILE ALA GLU TYR SER LEU
SEQRES 11 A 272 LYS LEU MET ASP ILE ASP ALA ASP PHE LEU LYS ILE GLU
SEQRES 12 A 272 GLU LEU GLN TYR ASP SER THR LEU SER LEU PRO SER SER
SEQRES 13 A 272 GLU PHE SER LYS ILE VAL ARG ASP LEU SER GLN LEU SER
SEQRES 14 A 272 ASP SER ILE ASN ILE MET ILE THR LYS GLU THR ILE LYS
SEQRES 15 A 272 PHE VAL ALA ASP GLY ASP ILE GLY SER GLY SER VAL ILE
SEQRES 16 A 272 ILE LYS PRO PHE VAL ASP MET GLU HIS PRO GLU THR SER
SEQRES 17 A 272 ILE LYS LEU GLU MET ASP GLN PRO VAL ASP LEU THR PHE
SEQRES 18 A 272 GLY ALA LYS TYR LEU LEU ASP ILE ILE LYS GLY SER SER
SEQRES 19 A 272 LEU SER ASP ARG VAL GLY ILE ARG LEU SER SER GLU ALA
SEQRES 20 A 272 PRO ALA LEU PHE GLN PHE ASP LEU LYS SER GLY PHE LEU
SEQRES 21 A 272 GLN PHE PHE LEU ALA PRO LYS PHE ASN ASP GLU GLU
SEQRES 1 B 272 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 B 272 PRO MET LEU GLU ALA LYS PHE GLU GLU ALA SER LEU PHE
SEQRES 3 B 272 LYS ARG ILE ILE ASP GLY PHE LYS ASP CYS VAL GLN LEU
SEQRES 4 B 272 VAL ASN PHE GLN CYS LYS GLU ASP GLY ILE ILE ALA GLN
SEQRES 5 B 272 ALA VAL ASP ASP SER ARG VAL LEU LEU VAL SER LEU GLU
SEQRES 6 B 272 ILE GLY VAL GLU ALA PHE GLN GLU TYR ARG CYS ASP HIS
SEQRES 7 B 272 PRO VAL THR LEU GLY MET ASP LEU THR SER LEU SER LYS
SEQRES 8 B 272 ILE LEU ARG CYS GLY ASN ASN THR ASP THR LEU THR LEU
SEQRES 9 B 272 ILE ALA ASP ASN THR PRO ASP SER ILE ILE LEU LEU PHE
SEQRES 10 B 272 GLU ASP THR LYS LYS ASP ARG ILE ALA GLU TYR SER LEU
SEQRES 11 B 272 LYS LEU MET ASP ILE ASP ALA ASP PHE LEU LYS ILE GLU
SEQRES 12 B 272 GLU LEU GLN TYR ASP SER THR LEU SER LEU PRO SER SER
SEQRES 13 B 272 GLU PHE SER LYS ILE VAL ARG ASP LEU SER GLN LEU SER
SEQRES 14 B 272 ASP SER ILE ASN ILE MET ILE THR LYS GLU THR ILE LYS
SEQRES 15 B 272 PHE VAL ALA ASP GLY ASP ILE GLY SER GLY SER VAL ILE
SEQRES 16 B 272 ILE LYS PRO PHE VAL ASP MET GLU HIS PRO GLU THR SER
SEQRES 17 B 272 ILE LYS LEU GLU MET ASP GLN PRO VAL ASP LEU THR PHE
SEQRES 18 B 272 GLY ALA LYS TYR LEU LEU ASP ILE ILE LYS GLY SER SER
SEQRES 19 B 272 LEU SER ASP ARG VAL GLY ILE ARG LEU SER SER GLU ALA
SEQRES 20 B 272 PRO ALA LEU PHE GLN PHE ASP LEU LYS SER GLY PHE LEU
SEQRES 21 B 272 GLN PHE PHE LEU ALA PRO LYS PHE ASN ASP GLU GLU
SEQRES 1 C 272 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 C 272 PRO MET LEU GLU ALA LYS PHE GLU GLU ALA SER LEU PHE
SEQRES 3 C 272 LYS ARG ILE ILE ASP GLY PHE LYS ASP CYS VAL GLN LEU
SEQRES 4 C 272 VAL ASN PHE GLN CYS LYS GLU ASP GLY ILE ILE ALA GLN
SEQRES 5 C 272 ALA VAL ASP ASP SER ARG VAL LEU LEU VAL SER LEU GLU
SEQRES 6 C 272 ILE GLY VAL GLU ALA PHE GLN GLU TYR ARG CYS ASP HIS
SEQRES 7 C 272 PRO VAL THR LEU GLY MET ASP LEU THR SER LEU SER LYS
SEQRES 8 C 272 ILE LEU ARG CYS GLY ASN ASN THR ASP THR LEU THR LEU
SEQRES 9 C 272 ILE ALA ASP ASN THR PRO ASP SER ILE ILE LEU LEU PHE
SEQRES 10 C 272 GLU ASP THR LYS LYS ASP ARG ILE ALA GLU TYR SER LEU
SEQRES 11 C 272 LYS LEU MET ASP ILE ASP ALA ASP PHE LEU LYS ILE GLU
SEQRES 12 C 272 GLU LEU GLN TYR ASP SER THR LEU SER LEU PRO SER SER
SEQRES 13 C 272 GLU PHE SER LYS ILE VAL ARG ASP LEU SER GLN LEU SER
SEQRES 14 C 272 ASP SER ILE ASN ILE MET ILE THR LYS GLU THR ILE LYS
SEQRES 15 C 272 PHE VAL ALA ASP GLY ASP ILE GLY SER GLY SER VAL ILE
SEQRES 16 C 272 ILE LYS PRO PHE VAL ASP MET GLU HIS PRO GLU THR SER
SEQRES 17 C 272 ILE LYS LEU GLU MET ASP GLN PRO VAL ASP LEU THR PHE
SEQRES 18 C 272 GLY ALA LYS TYR LEU LEU ASP ILE ILE LYS GLY SER SER
SEQRES 19 C 272 LEU SER ASP ARG VAL GLY ILE ARG LEU SER SER GLU ALA
SEQRES 20 C 272 PRO ALA LEU PHE GLN PHE ASP LEU LYS SER GLY PHE LEU
SEQRES 21 C 272 GLN PHE PHE LEU ALA PRO LYS PHE ASN ASP GLU GLU
SEQRES 1 D 17 ASN GLY ILE ALA ALA MET LEU GLN ARG HIS SER ARG LYS
SEQRES 2 D 17 ARG PHE GLN LEU
SEQRES 1 E 17 ASN GLY ILE ALA ALA MET LEU GLN ARG HIS SER ARG LYS
SEQRES 2 E 17 ARG PHE GLN LEU
SEQRES 1 F 17 ASN GLY ILE ALA ALA MET LEU GLN ARG HIS SER ARG LYS
SEQRES 2 F 17 ARG PHE GLN LEU
FORMUL 7 HOH *8(H2 O)
HELIX 1 AA1 GLU A 8 LYS A 20 1 13
HELIX 2 AA2 GLU A 55 PHE A 57 5 3
HELIX 3 AA3 LEU A 72 LEU A 79 1 8
HELIX 4 AA4 SER A 141 GLN A 153 1 13
HELIX 5 AA5 HIS A 190 SER A 194 5 5
HELIX 6 AA6 ALA A 209 ILE A 216 1 8
HELIX 7 AA7 LYS A 217 LEU A 221 5 5
HELIX 8 AA8 GLU B 8 LYS B 20 1 13
HELIX 9 AA9 GLU B 55 PHE B 57 5 3
HELIX 10 AB1 LEU B 72 LEU B 79 1 8
HELIX 11 AB2 SER B 141 GLN B 153 1 13
HELIX 12 AB3 HIS B 190 SER B 194 5 5
HELIX 13 AB4 ALA B 209 ILE B 216 1 8
HELIX 14 AB5 LYS B 217 LEU B 221 5 5
HELIX 15 AB6 GLU C 8 ASP C 21 1 14
HELIX 16 AB7 GLU C 55 PHE C 57 5 3
HELIX 17 AB8 LEU C 72 LEU C 79 1 8
HELIX 18 AB9 SER C 141 GLN C 153 1 13
HELIX 19 AC1 HIS C 190 SER C 194 5 5
HELIX 20 AC2 ALA C 209 ILE C 216 1 8
HELIX 21 AC3 LYS C 217 LEU C 221 5 5
HELIX 22 AC4 GLY D 816 GLN D 822 1 7
HELIX 23 AC5 ILE E 817 ARG E 823 1 7
HELIX 24 AC6 ILE F 817 ARG F 823 1 7
SHEET 1 AA1 9 GLU A 59 CYS A 62 0
SHEET 2 AA1 9 LEU A 2 PHE A 6 -1 N LYS A 5 O GLU A 59
SHEET 3 AA1 9 THR A 87 ALA A 92 -1 O LEU A 88 N PHE A 6
SHEET 4 AA1 9 SER A 98 GLU A 104 -1 O LEU A 102 N THR A 89
SHEET 5 AA1 9 ILE A 111 LYS A 117 -1 O ALA A 112 N PHE A 103
SHEET 6 AA1 9 GLY B 176 ILE B 182 -1 O SER B 177 N SER A 115
SHEET 7 AA1 9 THR B 166 ASP B 172 -1 N ALA B 171 O GLY B 178
SHEET 8 AA1 9 SER B 157 THR B 163 -1 N ASN B 159 O VAL B 170
SHEET 9 AA1 9 VAL B 203 GLY B 208 -1 O LEU B 205 N ILE B 160
SHEET 1 AA2 9 VAL A 66 ASP A 71 0
SHEET 2 AA2 9 LEU A 25 LYS A 31 -1 N PHE A 28 O LEU A 68
SHEET 3 AA2 9 GLY A 34 VAL A 40 -1 O ILE A 36 N GLN A 29
SHEET 4 AA2 9 LEU A 46 GLY A 53 -1 O LEU A 50 N ALA A 37
SHEET 5 AA2 9 GLY A 244 LEU A 250 -1 O GLN A 247 N SER A 49
SHEET 6 AA2 9 ALA A 233 LEU A 241 -1 N ALA A 235 O LEU A 250
SHEET 7 AA2 9 ARG A 224 SER A 230 -1 N GLY A 226 O GLN A 238
SHEET 8 AA2 9 SER A 135 PRO A 140 -1 N LEU A 137 O ILE A 227
SHEET 9 AA2 9 LYS A 196 MET A 199 -1 O GLU A 198 N THR A 136
SHEET 1 AA3 9 VAL A 203 GLY A 208 0
SHEET 2 AA3 9 SER A 157 THR A 163 -1 N ILE A 162 O VAL A 203
SHEET 3 AA3 9 THR A 166 ASP A 172 -1 O VAL A 170 N ASN A 159
SHEET 4 AA3 9 GLY A 176 ILE A 182 -1 O GLY A 178 N ALA A 171
SHEET 5 AA3 9 ILE C 111 LYS C 117 -1 O SER C 115 N SER A 177
SHEET 6 AA3 9 SER C 98 GLU C 104 -1 N PHE C 103 O ALA C 112
SHEET 7 AA3 9 THR C 87 ALA C 92 -1 N ILE C 91 O ILE C 100
SHEET 8 AA3 9 LEU C 2 PHE C 6 -1 N PHE C 6 O LEU C 88
SHEET 9 AA3 9 GLU C 59 CYS C 62 -1 O GLU C 59 N LYS C 5
SHEET 1 AA4 9 GLU B 59 CYS B 62 0
SHEET 2 AA4 9 LEU B 2 PHE B 6 -1 N LYS B 5 O GLU B 59
SHEET 3 AA4 9 THR B 87 ALA B 92 -1 O LEU B 88 N PHE B 6
SHEET 4 AA4 9 SER B 98 GLU B 104 -1 O LEU B 102 N THR B 89
SHEET 5 AA4 9 ILE B 111 LYS B 117 -1 O ALA B 112 N PHE B 103
SHEET 6 AA4 9 GLY C 176 ILE C 182 -1 O SER C 177 N SER B 115
SHEET 7 AA4 9 THR C 166 ASP C 172 -1 N ALA C 171 O GLY C 178
SHEET 8 AA4 9 SER C 157 THR C 163 -1 N ASN C 159 O VAL C 170
SHEET 9 AA4 9 VAL C 203 GLY C 208 -1 O LEU C 205 N ILE C 160
SHEET 1 AA5 9 VAL B 66 ASP B 71 0
SHEET 2 AA5 9 LEU B 25 LYS B 31 -1 N PHE B 28 O LEU B 68
SHEET 3 AA5 9 GLY B 34 VAL B 40 -1 O ILE B 36 N GLN B 29
SHEET 4 AA5 9 LEU B 46 GLY B 53 -1 O LEU B 50 N ALA B 37
SHEET 5 AA5 9 GLY B 244 LEU B 250 -1 O GLN B 247 N SER B 49
SHEET 6 AA5 9 ALA B 233 LEU B 241 -1 N PHE B 237 O PHE B 248
SHEET 7 AA5 9 ARG B 224 SER B 230 -1 N GLY B 226 O GLN B 238
SHEET 8 AA5 9 SER B 135 PRO B 140 -1 N LEU B 137 O ILE B 227
SHEET 9 AA5 9 LYS B 196 MET B 199 -1 O GLU B 198 N THR B 136
SHEET 1 AA6 9 VAL C 66 ASP C 71 0
SHEET 2 AA6 9 LEU C 25 LYS C 31 -1 N PHE C 28 O LEU C 68
SHEET 3 AA6 9 GLY C 34 VAL C 40 -1 O ILE C 36 N GLN C 29
SHEET 4 AA6 9 LEU C 46 GLY C 53 -1 O LEU C 50 N ALA C 37
SHEET 5 AA6 9 GLY C 244 LEU C 250 -1 O GLN C 247 N SER C 49
SHEET 6 AA6 9 ALA C 233 LEU C 241 -1 N PHE C 237 O PHE C 248
SHEET 7 AA6 9 ARG C 224 SER C 230 -1 N GLY C 226 O GLN C 238
SHEET 8 AA6 9 SER C 135 PRO C 140 -1 N LEU C 137 O ILE C 227
SHEET 9 AA6 9 LYS C 196 MET C 199 -1 O GLU C 198 N THR C 136
CRYST1 169.346 41.795 146.968 90.00 92.26 90.00 C 1 2 1 12
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 0.005905 0.000000 0.000233 0.00000
SCALE2 0.000000 0.023926 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006810 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
