HEADER OXIDOREDUCTASE 13-JUN-05 1ZZD
TITLE STRUCTURES OF YEAST RIBONUCLEOTIDE REDUCTASE I
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RIBONUCLEOTIDE REDUCTASE;
COMPND 5 EC: 1.17.4.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN 2;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: RIBONUCLEOTIDE REDUCTASE SMALL SUBUNIT 2;
COMPND 11 EC: 1.17.4.1;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: RNR1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PWJ751-3;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: CHEMICALLY SYNTHESIZED, THIS SEQUENE OCCURS NATURALLY
SOURCE 14 IN YEAST.
KEYWDS EUKARYOTIC, RIBONUCLEOTIDE REDUCTASE, DNTP REGULATION, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.XU,C.FABER,T.UCHIKI,J.W.FAIRMAN,J.RACCA,C.DEALWIS
REVDAT 4 03-APR-24 1ZZD 1 REMARK
REVDAT 3 24-FEB-09 1ZZD 1 VERSN
REVDAT 2 04-APR-06 1ZZD 1 JRNL
REVDAT 1 07-MAR-06 1ZZD 0
JRNL AUTH H.XU,C.FABER,T.UCHIKI,J.W.FAIRMAN,J.RACCA,C.DEALWIS
JRNL TITL STRUCTURES OF EUKARYOTIC RIBONUCLEOTIDE REDUCTASE I PROVIDE
JRNL TITL 2 INSIGHTS INTO DNTP REGULATION
JRNL REF PROC.NATL.ACAD.SCI.USA V. 103 4022 2006
JRNL REFN ISSN 0027-8424
JRNL PMID 16537479
JRNL DOI 10.1073/PNAS.0600443103
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0007
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 23454
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) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2626
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1673
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.15
REMARK 3 BIN R VALUE (WORKING SET) : 0.2860
REMARK 3 BIN FREE R VALUE SET COUNT : 185
REMARK 3 BIN FREE R VALUE : 0.3620
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5183
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 58
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.40
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): 0.788
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.331
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.227
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.671
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.905
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5305 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7182 ; 1.728 ; 1.942
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 642 ; NULL ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 251 ; NULL ;24.104
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 921 ; NULL ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ; NULL ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 779 ; NULL ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4032 ; NULL ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2638 ; NULL ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3624 ; NULL ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 237 ; NULL ; 0.200
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): 35 ; NULL ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 1 ; NULL ; 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): 3291 ; NULL ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5197 ; NULL ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2306 ; NULL ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1985 ; NULL ; 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 : 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 1ZZD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUL-05.
REMARK 100 THE DEPOSITION ID IS D_1000033299.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-MAR-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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 RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26145
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : 0.11000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 0.73600
REMARK 200 R SYM FOR SHELL (I) : 0.73600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NATIVE STRUCTURE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, SODIUM ACETATE, AMMONIUM
REMARK 280 SULFATE, PH 6.5, EVAPORATION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+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 54.16050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 58.84100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 54.16050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 58.84100
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 300 REMARK: THE SECOND PART OF THE ACTIVE BIOLOGICAL DIMER ASSEMBLY IS
REMARK 300 GENERATED BY THE TWO FOLD AXIS: -X, -Y+1, Z.
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: TETRAMERIC
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 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 117.68200
REMARK 350 BIOMT3 2 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 1
REMARK 465 TYR A 2
REMARK 465 VAL A 3
REMARK 465 TYR A 4
REMARK 465 LYS A 5
REMARK 465 ARG A 6
REMARK 465 ASP A 7
REMARK 465 GLY A 8
REMARK 465 ARG A 9
REMARK 465 LYS A 10
REMARK 465 GLU A 11
REMARK 465 PRO A 12
REMARK 465 VAL A 13
REMARK 465 GLN A 14
REMARK 465 PHE A 15
REMARK 465 ASP A 16
REMARK 465 LYS A 17
REMARK 465 ILE A 18
REMARK 465 THR A 19
REMARK 465 ALA A 20
REMARK 465 ARG A 21
REMARK 465 ILE A 22
REMARK 465 SER A 23
REMARK 465 ARG A 24
REMARK 465 LEU A 25
REMARK 465 CYS A 26
REMARK 465 TYR A 27
REMARK 465 GLY A 28
REMARK 465 LEU A 29
REMARK 465 ASP A 30
REMARK 465 PRO A 31
REMARK 465 LYS A 32
REMARK 465 HIS A 33
REMARK 465 ILE A 34
REMARK 465 ASP A 35
REMARK 465 ALA A 36
REMARK 465 VAL A 37
REMARK 465 LYS A 38
REMARK 465 VAL A 39
REMARK 465 THR A 40
REMARK 465 GLN A 41
REMARK 465 ARG A 42
REMARK 465 ILE A 43
REMARK 465 ILE A 44
REMARK 465 SER A 45
REMARK 465 GLY A 46
REMARK 465 VAL A 47
REMARK 465 TYR A 48
REMARK 465 GLU A 49
REMARK 465 GLY A 50
REMARK 465 VAL A 51
REMARK 465 THR A 52
REMARK 465 THR A 53
REMARK 465 ILE A 54
REMARK 465 GLU A 55
REMARK 465 LEU A 56
REMARK 465 ASP A 57
REMARK 465 ASN A 58
REMARK 465 LEU A 59
REMARK 465 ALA A 60
REMARK 465 ALA A 61
REMARK 465 GLU A 62
REMARK 465 THR A 63
REMARK 465 CYS A 64
REMARK 465 ALA A 65
REMARK 465 TYR A 66
REMARK 465 MET A 67
REMARK 465 THR A 68
REMARK 465 THR A 69
REMARK 465 VAL A 70
REMARK 465 HIS A 71
REMARK 465 PRO A 72
REMARK 465 ASP A 73
REMARK 465 TYR A 74
REMARK 465 ALA A 75
REMARK 465 THR A 76
REMARK 465 LEU A 77
REMARK 465 ALA A 78
REMARK 465 ALA A 79
REMARK 465 ARG A 80
REMARK 465 ILE A 81
REMARK 465 ALA A 82
REMARK 465 ILE A 83
REMARK 465 SER A 84
REMARK 465 ASN A 85
REMARK 465 LEU A 86
REMARK 465 HIS A 87
REMARK 465 LYS A 88
REMARK 465 GLN A 89
REMARK 465 THR A 90
REMARK 465 ASP A 287
REMARK 465 GLN A 288
REMARK 465 GLY A 289
REMARK 465 GLY A 290
REMARK 465 ASN A 291
REMARK 465 LYS A 292
REMARK 465 ARG A 293
REMARK 465 PRO A 294
REMARK 465 GLY A 295
REMARK 465 ARG A 631
REMARK 465 ARG A 632
REMARK 465 VAL A 633
REMARK 465 LEU A 634
REMARK 465 SER A 635
REMARK 465 GLY A 636
REMARK 465 GLU A 637
REMARK 465 ALA A 747
REMARK 465 ALA A 748
REMARK 465 SER A 749
REMARK 465 ALA A 750
REMARK 465 ALA A 751
REMARK 465 ILE A 752
REMARK 465 GLN A 753
REMARK 465 PHE A 754
REMARK 465 THR A 755
REMARK 465 ILE A 756
REMARK 465 ASP A 757
REMARK 465 GLN A 758
REMARK 465 LYS A 759
REMARK 465 ILE A 760
REMARK 465 ALA A 761
REMARK 465 ASP A 762
REMARK 465 GLN A 763
REMARK 465 ALA A 764
REMARK 465 THR A 765
REMARK 465 GLU A 766
REMARK 465 ASN A 767
REMARK 465 VAL A 768
REMARK 465 ALA A 769
REMARK 465 ASP A 770
REMARK 465 ILE A 771
REMARK 465 SER A 772
REMARK 465 ASN A 773
REMARK 465 LEU A 774
REMARK 465 LYS A 775
REMARK 465 ARG A 776
REMARK 465 PRO A 777
REMARK 465 SER A 778
REMARK 465 TYR A 779
REMARK 465 MET A 780
REMARK 465 PRO A 781
REMARK 465 SER A 782
REMARK 465 SER A 783
REMARK 465 ALA A 784
REMARK 465 SER A 785
REMARK 465 TYR A 786
REMARK 465 ALA A 787
REMARK 465 ALA A 788
REMARK 465 SER A 789
REMARK 465 ASP A 790
REMARK 465 PHE A 791
REMARK 465 VAL A 792
REMARK 465 PRO A 793
REMARK 465 ALA A 794
REMARK 465 ALA A 795
REMARK 465 VAL A 796
REMARK 465 THR A 797
REMARK 465 ALA A 798
REMARK 465 ASN A 799
REMARK 465 ALA A 800
REMARK 465 THR A 801
REMARK 465 ILE A 802
REMARK 465 PRO A 803
REMARK 465 SER A 804
REMARK 465 LEU A 805
REMARK 465 ASP A 806
REMARK 465 SER A 807
REMARK 465 SER A 808
REMARK 465 SER A 809
REMARK 465 GLU A 810
REMARK 465 ALA A 811
REMARK 465 SER A 812
REMARK 465 ARG A 813
REMARK 465 GLU A 814
REMARK 465 ALA A 815
REMARK 465 SER A 816
REMARK 465 PRO A 817
REMARK 465 ALA A 818
REMARK 465 PRO A 819
REMARK 465 THR A 820
REMARK 465 GLY A 821
REMARK 465 SER A 822
REMARK 465 HIS A 823
REMARK 465 SER A 824
REMARK 465 LEU A 825
REMARK 465 THR A 826
REMARK 465 LYS A 827
REMARK 465 GLY A 828
REMARK 465 MET A 829
REMARK 465 ALA A 830
REMARK 465 GLU A 831
REMARK 465 LEU A 832
REMARK 465 ASN A 833
REMARK 465 VAL A 834
REMARK 465 GLN A 835
REMARK 465 GLU A 836
REMARK 465 SER A 837
REMARK 465 LYS A 838
REMARK 465 VAL A 839
REMARK 465 GLU A 840
REMARK 465 VAL A 841
REMARK 465 PRO A 842
REMARK 465 GLU A 843
REMARK 465 VAL A 844
REMARK 465 PRO A 845
REMARK 465 ALA A 846
REMARK 465 PRO A 847
REMARK 465 THR A 848
REMARK 465 LYS A 849
REMARK 465 ASN A 850
REMARK 465 GLU A 851
REMARK 465 GLU A 852
REMARK 465 LYS A 853
REMARK 465 ALA A 854
REMARK 465 ALA A 855
REMARK 465 PRO A 856
REMARK 465 ILE A 857
REMARK 465 VAL A 858
REMARK 465 ASP A 859
REMARK 465 ASP A 860
REMARK 465 GLU A 861
REMARK 465 GLU A 862
REMARK 465 THR A 863
REMARK 465 GLU A 864
REMARK 465 PHE A 865
REMARK 465 ASP A 866
REMARK 465 ILE A 867
REMARK 465 TYR A 868
REMARK 465 ASN A 869
REMARK 465 SER A 870
REMARK 465 LYS A 871
REMARK 465 VAL A 872
REMARK 465 ILE A 873
REMARK 465 ALA A 874
REMARK 465 CYS A 875
REMARK 465 ALA A 876
REMARK 465 ILE A 877
REMARK 465 ASP A 878
REMARK 465 ASN A 879
REMARK 465 PRO A 880
REMARK 465 GLU A 881
REMARK 465 ALA A 882
REMARK 465 CYS A 883
REMARK 465 GLU A 884
REMARK 465 MET A 885
REMARK 465 CYS A 886
REMARK 465 SER A 887
REMARK 465 GLY A 888
REMARK 465 LYS B -1
REMARK 465 GLU B 0
REMARK 465 ILE B 1
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 NH2 ARG A 520 OD2 ASP A 648 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 100 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP A 140 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 182 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP A 226 CB - CG - OD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ASP B 4 CB - CG - OD2 ANGL. DEV. = 6.5 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 LYS A 92 60.03 19.06
REMARK 500 GLN A 93 125.71 178.24
REMARK 500 ALA A 108 2.32 -65.95
REMARK 500 THR A 109 -15.73 -147.49
REMARK 500 ASN A 127 30.44 -141.60
REMARK 500 SER A 154 -8.31 -141.41
REMARK 500 ILE A 159 -74.90 -102.26
REMARK 500 ASN A 160 62.26 -111.95
REMARK 500 LYS A 212 78.39 -113.54
REMARK 500 GLU A 225 146.19 -179.78
REMARK 500 THR A 244 42.64 -94.75
REMARK 500 ALA A 245 -148.46 53.18
REMARK 500 PRO A 303 0.43 -65.31
REMARK 500 HIS A 318 27.04 -75.46
REMARK 500 GLU A 321 -82.91 9.73
REMARK 500 ARG A 324 -158.08 -89.30
REMARK 500 ALA A 325 99.74 158.35
REMARK 500 GLU A 377 4.89 -69.82
REMARK 500 SER A 425 -157.36 -106.80
REMARK 500 ALA A 452 -2.97 -57.19
REMARK 500 GLU A 458 79.57 -18.73
REMARK 500 ASP A 459 -135.33 175.60
REMARK 500 ASP A 576 59.50 39.10
REMARK 500 THR A 602 -21.60 -148.93
REMARK 500 ALA A 604 79.03 -165.42
REMARK 500 ALA A 609 -104.03 41.07
REMARK 500 GLU A 619 99.00 -34.19
REMARK 500 CYS A 620 -101.26 37.29
REMARK 500 GLN A 639 106.29 130.11
REMARK 500 ASN A 642 114.81 -37.71
REMARK 500 ASP A 651 -9.85 -53.73
REMARK 500 TRP A 655 25.77 -69.91
REMARK 500 MET A 659 -66.34 -139.12
REMARK 500 THR A 665 42.12 -83.37
REMARK 500 ASN A 667 -4.61 88.01
REMARK 500 ASP A 707 -49.87 -23.10
REMARK 500 GLN A 708 -116.83 -110.47
REMARK 500 ARG A 717 -77.53 -79.16
REMARK 500 ALA A 718 70.25 -100.51
REMARK 500 TYR A 741 -124.26 -80.60
REMARK 500 PHE B 3 71.36 34.08
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1ZZD A 1 888 UNP P21524 RIR1_YEAST 1 888
DBREF 1ZZD B -1 7 UNP P49723 RIR4_YEAST 337 345
SEQRES 1 A 888 MET TYR VAL TYR LYS ARG ASP GLY ARG LYS GLU PRO VAL
SEQRES 2 A 888 GLN PHE ASP LYS ILE THR ALA ARG ILE SER ARG LEU CYS
SEQRES 3 A 888 TYR GLY LEU ASP PRO LYS HIS ILE ASP ALA VAL LYS VAL
SEQRES 4 A 888 THR GLN ARG ILE ILE SER GLY VAL TYR GLU GLY VAL THR
SEQRES 5 A 888 THR ILE GLU LEU ASP ASN LEU ALA ALA GLU THR CYS ALA
SEQRES 6 A 888 TYR MET THR THR VAL HIS PRO ASP TYR ALA THR LEU ALA
SEQRES 7 A 888 ALA ARG ILE ALA ILE SER ASN LEU HIS LYS GLN THR THR
SEQRES 8 A 888 LYS GLN PHE SER LYS VAL VAL GLU ASP LEU TYR ARG TYR
SEQRES 9 A 888 VAL ASN ALA ALA THR GLY LYS PRO ALA PRO MET ILE SER
SEQRES 10 A 888 ASP ASP VAL TYR ASN ILE VAL MET GLU ASN LYS ASP LYS
SEQRES 11 A 888 LEU ASN SER ALA ILE VAL TYR ASP ARG ASP PHE GLN TYR
SEQRES 12 A 888 SER TYR PHE GLY PHE LYS THR LEU GLU ARG SER TYR LEU
SEQRES 13 A 888 LEU ARG ILE ASN GLY GLN VAL ALA GLU ARG PRO GLN HIS
SEQRES 14 A 888 LEU ILE MET ARG VAL ALA LEU GLY ILE HIS GLY ARG ASP
SEQRES 15 A 888 ILE GLU ALA ALA LEU GLU THR TYR ASN LEU MET SER LEU
SEQRES 16 A 888 LYS TYR PHE THR HIS ALA SER PRO THR LEU PHE ASN ALA
SEQRES 17 A 888 GLY THR PRO LYS PRO GLN MET SER SER CYS PHE LEU VAL
SEQRES 18 A 888 ALA MET LYS GLU ASP SER ILE GLU GLY ILE TYR ASP THR
SEQRES 19 A 888 LEU LYS GLU CYS ALA LEU ILE SER LYS THR ALA GLY GLY
SEQRES 20 A 888 ILE GLY LEU HIS ILE HIS ASN ILE ARG SER THR GLY SER
SEQRES 21 A 888 TYR ILE ALA GLY THR ASN GLY THR SER ASN GLY LEU ILE
SEQRES 22 A 888 PRO MET ILE ARG VAL PHE ASN ASN THR ALA ARG TYR VAL
SEQRES 23 A 888 ASP GLN GLY GLY ASN LYS ARG PRO GLY ALA PHE ALA LEU
SEQRES 24 A 888 TYR LEU GLU PRO TRP HIS ALA ASP ILE PHE ASP PHE ILE
SEQRES 25 A 888 ASP ILE ARG LYS ASN HIS GLY LYS GLU GLU ILE ARG ALA
SEQRES 26 A 888 ARG ASP LEU PHE PRO ALA LEU TRP ILE PRO ASP LEU PHE
SEQRES 27 A 888 MET LYS ARG VAL GLU GLU ASN GLY THR TRP THR LEU PHE
SEQRES 28 A 888 SER PRO THR SER ALA PRO GLY LEU SER ASP CYS TYR GLY
SEQRES 29 A 888 ASP GLU PHE GLU ALA LEU TYR THR ARG TYR GLU LYS GLU
SEQRES 30 A 888 GLY ARG GLY LYS THR ILE LYS ALA GLN LYS LEU TRP TYR
SEQRES 31 A 888 SER ILE LEU GLU ALA GLN THR GLU THR GLY THR PRO PHE
SEQRES 32 A 888 VAL VAL TYR LYS ASP ALA CYS ASN ARG LYS SER ASN GLN
SEQRES 33 A 888 LYS ASN LEU GLY VAL ILE LYS SER SER ASN LEU CYS CYS
SEQRES 34 A 888 GLU ILE VAL GLU TYR SER ALA PRO ASP GLU THR ALA VAL
SEQRES 35 A 888 CYS ASN LEU ALA SER VAL ALA LEU PRO ALA PHE ILE GLU
SEQRES 36 A 888 THR SER GLU ASP GLY LYS THR SER THR TYR ASN PHE LYS
SEQRES 37 A 888 LYS LEU HIS GLU ILE ALA LYS VAL VAL THR ARG ASN LEU
SEQRES 38 A 888 ASN ARG VAL ILE ASP ARG ASN TYR TYR PRO VAL GLU GLU
SEQRES 39 A 888 ALA ARG LYS SER ASN MET ARG HIS ARG PRO ILE ALA LEU
SEQRES 40 A 888 GLY VAL GLN GLY LEU ALA ASP THR PHE MET LEU LEU ARG
SEQRES 41 A 888 LEU PRO PHE ASP SER GLU GLU ALA ARG LEU LEU ASN ILE
SEQRES 42 A 888 GLN ILE PHE GLU THR ILE TYR HIS ALA SER MET GLU ALA
SEQRES 43 A 888 SER CYS GLU LEU ALA GLN LYS ASP GLY PRO TYR GLU THR
SEQRES 44 A 888 PHE GLN GLY SER PRO ALA SER GLN GLY ILE LEU GLN PHE
SEQRES 45 A 888 ASP MET TRP ASP GLN LYS PRO TYR GLY MET TRP ASP TRP
SEQRES 46 A 888 ASP THR LEU ARG LYS ASP ILE MET LYS HIS GLY VAL ARG
SEQRES 47 A 888 ASN SER LEU THR MET ALA PRO MET PRO THR ALA SER THR
SEQRES 48 A 888 SER GLN ILE LEU GLY TYR ASN GLU CYS PHE GLU PRO VAL
SEQRES 49 A 888 THR SER ASN MET TYR SER ARG ARG VAL LEU SER GLY GLU
SEQRES 50 A 888 PHE GLN VAL VAL ASN PRO TYR LEU LEU ARG ASP LEU VAL
SEQRES 51 A 888 ASP LEU GLY ILE TRP ASP GLU GLY MET LYS GLN TYR LEU
SEQRES 52 A 888 ILE THR GLN ASN GLY SER ILE GLN GLY LEU PRO ASN VAL
SEQRES 53 A 888 PRO GLN GLU LEU LYS ASP LEU TYR LYS THR VAL TRP GLU
SEQRES 54 A 888 ILE SER GLN LYS THR ILE ILE ASN MET ALA ALA ASP ARG
SEQRES 55 A 888 SER VAL TYR ILE ASP GLN SER HIS SER LEU ASN LEU PHE
SEQRES 56 A 888 LEU ARG ALA PRO THR MET GLY LYS LEU THR SER MET HIS
SEQRES 57 A 888 PHE TYR GLY TRP LYS LYS GLY LEU LYS THR GLY MET TYR
SEQRES 58 A 888 TYR LEU ARG THR GLN ALA ALA SER ALA ALA ILE GLN PHE
SEQRES 59 A 888 THR ILE ASP GLN LYS ILE ALA ASP GLN ALA THR GLU ASN
SEQRES 60 A 888 VAL ALA ASP ILE SER ASN LEU LYS ARG PRO SER TYR MET
SEQRES 61 A 888 PRO SER SER ALA SER TYR ALA ALA SER ASP PHE VAL PRO
SEQRES 62 A 888 ALA ALA VAL THR ALA ASN ALA THR ILE PRO SER LEU ASP
SEQRES 63 A 888 SER SER SER GLU ALA SER ARG GLU ALA SER PRO ALA PRO
SEQRES 64 A 888 THR GLY SER HIS SER LEU THR LYS GLY MET ALA GLU LEU
SEQRES 65 A 888 ASN VAL GLN GLU SER LYS VAL GLU VAL PRO GLU VAL PRO
SEQRES 66 A 888 ALA PRO THR LYS ASN GLU GLU LYS ALA ALA PRO ILE VAL
SEQRES 67 A 888 ASP ASP GLU GLU THR GLU PHE ASP ILE TYR ASN SER LYS
SEQRES 68 A 888 VAL ILE ALA CYS ALA ILE ASP ASN PRO GLU ALA CYS GLU
SEQRES 69 A 888 MET CYS SER GLY
SEQRES 1 B 9 LYS GLU ILE ASN PHE ASP ASP ASP PHE
FORMUL 3 HOH *58(H2 O)
HELIX 1 1 GLN A 93 TYR A 104 1 12
HELIX 2 2 SER A 117 ASN A 127 1 11
HELIX 3 3 ASN A 127 ILE A 135 1 9
HELIX 4 4 VAL A 136 PHE A 141 5 6
HELIX 5 5 SER A 144 TYR A 155 1 12
HELIX 6 6 ARG A 166 GLY A 180 1 15
HELIX 7 7 ASP A 182 LEU A 195 1 14
HELIX 8 8 ALA A 201 ALA A 208 1 8
HELIX 9 9 SER A 227 THR A 244 1 18
HELIX 10 10 LEU A 272 VAL A 286 1 15
HELIX 11 11 ASP A 307 ILE A 312 1 6
HELIX 12 12 LYS A 320 ARG A 324 5 5
HELIX 13 13 PRO A 335 GLU A 344 1 10
HELIX 14 14 GLY A 358 CYS A 362 5 5
HELIX 15 15 TYR A 363 GLU A 377 1 15
HELIX 16 16 ALA A 385 GLY A 400 1 16
HELIX 17 17 LYS A 407 LYS A 413 1 7
HELIX 18 18 GLN A 416 GLY A 420 5 5
HELIX 19 19 ASN A 466 ASN A 488 1 23
HELIX 20 20 VAL A 492 ARG A 503 1 12
HELIX 21 21 GLY A 511 LEU A 519 1 9
HELIX 22 22 SER A 525 GLY A 555 1 31
HELIX 23 23 GLN A 571 ASP A 576 5 6
HELIX 24 24 ASP A 584 GLY A 596 1 13
HELIX 25 25 THR A 608 GLY A 616 1 9
HELIX 26 26 ASN A 642 ASP A 651 1 10
HELIX 27 27 ASP A 656 THR A 665 1 10
HELIX 28 28 PRO A 677 TYR A 684 1 8
HELIX 29 29 THR A 686 ILE A 690 5 5
HELIX 30 30 SER A 691 SER A 703 1 13
HELIX 31 31 VAL A 704 ILE A 706 5 3
HELIX 32 32 THR A 720 LYS A 734 1 15
SHEET 1 A 3 PHE A 198 HIS A 200 0
SHEET 2 A 3 LEU A 445 ALA A 449 -1 O SER A 447 N THR A 199
SHEET 3 A 3 ALA A 506 GLN A 510 1 O GLY A 508 N VAL A 448
SHEET 1 B 6 CYS A 218 ALA A 222 0
SHEET 2 B 6 GLY A 247 HIS A 251 1 O GLY A 249 N PHE A 219
SHEET 3 B 6 PHE A 297 LEU A 301 1 O TYR A 300 N LEU A 250
SHEET 4 B 6 LEU A 328 ILE A 334 1 O PHE A 329 N LEU A 299
SHEET 5 B 6 PHE A 403 TYR A 406 1 O PHE A 403 N LEU A 332
SHEET 6 B 6 THR A 738 MET A 740 -1 O MET A 740 N VAL A 404
SHEET 1 C 2 THR A 347 LEU A 350 0
SHEET 2 C 2 LYS A 381 LYS A 384 -1 O ILE A 383 N TRP A 348
SHEET 1 D 2 ILE A 454 GLU A 455 0
SHEET 2 D 2 THR A 464 TYR A 465 -1 O THR A 464 N GLU A 455
SHEET 1 E 2 MET A 628 TYR A 629 0
SHEET 2 E 2 VAL A 640 VAL A 641 -1 O VAL A 640 N TYR A 629
SHEET 1 F 2 LEU A 714 PHE A 715 0
SHEET 2 F 2 LEU A 743 ARG A 744 1 O ARG A 744 N LEU A 714
SSBOND 1 CYS A 218 CYS A 443 1555 1555 2.05
CISPEP 1 THR A 401 PRO A 402 0 2.89
CRYST1 108.321 117.682 64.518 90.00 90.00 90.00 P 21 21 2 4
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 0.009232 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008497 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015500 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
