Header list of 1uw0.pdb file
Complete list - r 25 2 Bytes
HEADER LIGASE 27-JAN-04 1UW0
TITLE SOLUTION STRUCTURE OF THE ZINC-FINGER DOMAIN FROM DNA
TITLE 2 LIGASE IIIA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA LIGASE III;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ZINC-FINGER DOMAIN, RESIDUES 1-117;
COMPND 5 SYNONYM: POLYDEOXYRIBONUCLEOTIDE SYNTHASE [ATP];
COMPND 6 EC: 6.5.1.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: CODON PLUS RP;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS DNA REPAIR, ZINC FINGER, LIGASE, PARP-LIKE FINGER, CELL
KEYWDS 2 DIVISION, DNA REPLICATION, NUCLEAR PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 28
AUTHOR A.W.KULCZYK,J.-C.YANG,D.NEUHAUS
REVDAT 3 24-FEB-09 1UW0 1 VERSN
REVDAT 2 03-MAY-05 1UW0 1 ATOM
REVDAT 1 05-AUG-04 1UW0 0
JRNL AUTH A.W.KULCZYK,J.-C.YANG,D.NEUHAUS
JRNL TITL SOLUTION STRUCTURE AND DNA BINDING OF THE
JRNL TITL 2 ZINC-FINGER DOMAIN FROM DNA LIGASE IIIALPHA
JRNL REF J.MOL.BIOL. V. 341 723 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15288782
JRNL DOI 10.1016/J.JMB.2004.06.035
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN
REMARK 3 THE JRNL CITATION ABOVE
REMARK 4
REMARK 4 1UW0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JAN-04.
REMARK 100 THE PDBE ID CODE IS EBI-14459.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY; TOCSY; HSQC;
REMARK 210 CBCANH; CBCACONH; HBHANH;
REMARK 210 HBHACONH; HCCH-TOCSY;
REMARK 210 HCCH-COSY; 15N NOESY-HSQC;
REMARK 210 15N HSQC-NOESY-HSQC;
REMARK 210 13C NOESY-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500; 600; 800
REMARK 210 SPECTROMETER MODEL : DRX500; DMX600; AVANCE 800
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR, SPARKY, XPLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 28
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOW RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE
REMARK 210 NMR SPECTROSCOPY ON 13C, 15N-LABELED DNA-LIGASE III ZINC
REMARK 210 FINGER DOMAIN.
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 INTERACTS WITH DNA-REPAIR PROTEIN XRCC1 AND CAN CORRECT
REMARK 400 DEFECTIVE DNA STRAND-BREAK REPAIR AND SISTER CHROMATID EXCHANGE
REMARK 400 FOLLOWING TREATMENT WITH IONIZING RADIATION AND ALKYLATING
REMARK 400 AGENTS.
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 16 CYS A 21 N - CA - CB ANGL. DEV. = -9.7 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 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 1 LYS A 22 53.64 -100.74
REMARK 500 1 PHE A 40 -58.34 -149.81
REMARK 500 1 ILE A 70 98.43 54.36
REMARK 500 1 ASP A 72 -165.56 53.34
REMARK 500 1 THR A 74 36.74 -152.96
REMARK 500 1 LEU A 82 173.72 -49.93
REMARK 500 1 SER A 99 -164.90 52.42
REMARK 500 1 LYS A 100 80.06 53.65
REMARK 500 1 THR A 104 58.43 -155.42
REMARK 500 1 LYS A 108 81.76 52.40
REMARK 500 2 LYS A 12 -65.68 -138.05
REMARK 500 2 CYS A 21 148.70 -172.49
REMARK 500 2 LYS A 22 45.99 -107.45
REMARK 500 2 PHE A 40 100.11 55.26
REMARK 500 2 ILE A 70 101.83 55.18
REMARK 500 2 ASP A 72 -173.06 53.17
REMARK 500 2 THR A 74 50.23 -102.80
REMARK 500 2 LEU A 82 -179.87 -53.25
REMARK 500 2 SER A 98 46.73 -100.67
REMARK 500 2 LYS A 100 48.98 -144.89
REMARK 500 2 ALA A 101 56.97 -141.67
REMARK 500 2 LYS A 107 179.91 53.19
REMARK 500 3 LYS A 22 44.66 -105.38
REMARK 500 3 VAL A 26 112.95 -165.45
REMARK 500 3 PHE A 40 -58.74 -147.33
REMARK 500 3 ILE A 70 98.29 54.41
REMARK 500 3 ASP A 72 -166.01 53.33
REMARK 500 3 THR A 74 38.04 -149.28
REMARK 500 3 LEU A 82 -175.06 -69.81
REMARK 500 3 SER A 98 -65.50 -96.44
REMARK 500 3 SER A 99 94.70 52.39
REMARK 500 4 GLN A 4 107.92 57.69
REMARK 500 4 LYS A 22 51.27 -101.09
REMARK 500 4 PHE A 40 -58.83 -148.00
REMARK 500 4 ILE A 70 97.97 53.78
REMARK 500 4 ASP A 72 -170.54 53.08
REMARK 500 4 LEU A 82 -165.85 -113.28
REMARK 500 4 LYS A 100 -59.70 -143.44
REMARK 500 4 THR A 104 73.49 52.57
REMARK 500 4 LYS A 106 -60.18 -131.78
REMARK 500 5 CYS A 21 -44.45 -172.98
REMARK 500 5 LYS A 22 44.15 70.08
REMARK 500 5 PHE A 40 -58.37 -152.90
REMARK 500 5 ILE A 70 94.71 52.84
REMARK 500 5 ASP A 72 -165.25 53.46
REMARK 500 5 GLU A 75 -58.60 -143.49
REMARK 500 5 LEU A 82 -164.28 -108.81
REMARK 500 5 SER A 98 58.60 -105.09
REMARK 500 5 LYS A 100 40.06 -143.32
REMARK 500 5 ALA A 101 41.90 -142.58
REMARK 500 6 LYS A 12 -59.80 -130.05
REMARK 500 6 LYS A 22 46.96 -103.83
REMARK 500 6 PHE A 40 -58.69 -149.95
REMARK 500 6 ILE A 70 101.03 54.54
REMARK 500 6 ASP A 72 -169.90 53.41
REMARK 500 6 THR A 74 35.98 -148.22
REMARK 500 6 LEU A 82 176.91 -51.02
REMARK 500 6 SER A 98 66.59 -100.62
REMARK 500 6 LYS A 106 94.65 52.56
REMARK 500 7 LYS A 12 -57.34 -120.16
REMARK 500 7 LYS A 22 46.27 -104.05
REMARK 500 7 PHE A 40 -58.27 -152.61
REMARK 500 7 ILE A 70 99.21 54.97
REMARK 500 7 ASP A 72 -176.73 53.17
REMARK 500 7 THR A 74 42.88 -100.25
REMARK 500 7 LEU A 82 -166.10 -109.76
REMARK 500 8 LYS A 12 -163.64 -105.05
REMARK 500 8 LYS A 22 48.40 -102.89
REMARK 500 8 ILE A 70 96.82 53.60
REMARK 500 8 ASP A 72 -172.90 51.49
REMARK 500 8 THR A 74 -51.56 -171.91
REMARK 500 8 LEU A 82 172.74 -48.90
REMARK 500 8 SER A 98 54.51 -102.17
REMARK 500 8 LYS A 107 -166.09 -113.81
REMARK 500 9 LYS A 22 44.04 -105.50
REMARK 500 9 PHE A 40 -58.93 -148.17
REMARK 500 9 THR A 66 -51.91 -172.38
REMARK 500 9 ILE A 70 99.79 55.69
REMARK 500 9 ASP A 72 -172.33 53.26
REMARK 500 9 THR A 74 36.56 -144.42
REMARK 500 9 LEU A 82 174.44 -49.80
REMARK 500 9 SER A 98 50.91 -98.14
REMARK 500 9 LYS A 107 71.66 52.68
REMARK 500 10 GLU A 3 -66.02 -127.96
REMARK 500 10 CYS A 21 149.14 -174.83
REMARK 500 10 PHE A 40 98.78 54.35
REMARK 500 10 ILE A 70 100.01 54.49
REMARK 500 10 ASP A 72 -163.65 53.83
REMARK 500 10 LEU A 73 73.87 -103.87
REMARK 500 10 THR A 74 -160.00 -167.85
REMARK 500 10 GLU A 81 50.94 -165.10
REMARK 500 10 SER A 98 40.06 -102.76
REMARK 500 10 LYS A 100 -65.38 -123.06
REMARK 500 10 LYS A 108 -60.64 -131.24
REMARK 500 11 GLU A 3 -65.33 -140.45
REMARK 500 11 PHE A 40 -59.12 -145.18
REMARK 500 11 THR A 66 -55.30 -165.14
REMARK 500 11 ILE A 70 99.22 55.28
REMARK 500 11 ASP A 72 -164.75 53.47
REMARK 500 11 THR A 74 37.03 -153.42
REMARK 500 11 SER A 98 62.84 -101.07
REMARK 500 12 GLU A 3 -61.45 -123.43
REMARK 500 12 PHE A 40 -58.62 -151.38
REMARK 500 12 THR A 66 53.18 -95.98
REMARK 500 12 ASP A 72 177.34 54.14
REMARK 500 12 THR A 74 -51.35 -172.38
REMARK 500 12 LYS A 106 86.38 52.70
REMARK 500 13 LYS A 12 39.36 -149.65
REMARK 500 13 ILE A 70 99.07 54.21
REMARK 500 13 ASP A 72 -163.99 54.62
REMARK 500 13 LEU A 73 70.84 -116.08
REMARK 500 13 THR A 74 -163.70 -170.68
REMARK 500 13 LEU A 82 173.56 -49.38
REMARK 500 13 SER A 98 55.78 -101.26
REMARK 500 13 LYS A 100 -59.19 -143.58
REMARK 500 13 ALA A 101 40.11 -145.09
REMARK 500 13 THR A 104 89.75 46.61
REMARK 500 14 LYS A 12 -59.86 -143.51
REMARK 500 14 CYS A 21 -43.65 -172.94
REMARK 500 14 LYS A 22 44.85 70.06
REMARK 500 14 PHE A 40 -58.59 -150.49
REMARK 500 14 ILE A 70 101.49 54.77
REMARK 500 14 ASP A 72 -170.75 53.58
REMARK 500 14 LEU A 82 175.10 -49.77
REMARK 500 14 LYS A 108 73.45 -117.19
REMARK 500 15 GLN A 4 164.04 57.89
REMARK 500 15 LYS A 12 -65.68 -140.62
REMARK 500 15 CYS A 21 -43.58 -173.04
REMARK 500 15 ILE A 70 99.34 54.54
REMARK 500 15 ASP A 72 -173.52 53.00
REMARK 500 15 THR A 74 -51.62 -170.00
REMARK 500 15 LEU A 82 -175.30 -59.25
REMARK 500 15 LYS A 107 -65.07 -135.81
REMARK 500 15 LYS A 108 -58.82 -144.73
REMARK 500 16 ALA A 2 -59.68 -143.38
REMARK 500 16 LYS A 12 -58.11 -136.03
REMARK 500 16 CYS A 21 -44.41 -165.20
REMARK 500 16 LYS A 22 74.22 78.12
REMARK 500 16 GLU A 23 -172.88 -176.11
REMARK 500 16 PHE A 40 -58.88 -153.55
REMARK 500 16 ILE A 53 -60.45 -97.48
REMARK 500 16 ILE A 70 97.67 54.30
REMARK 500 16 ASP A 72 -178.22 52.67
REMARK 500 16 THR A 74 -51.63 -172.17
REMARK 500 16 LEU A 82 165.55 -47.67
REMARK 500 17 ALA A 11 102.04 -59.95
REMARK 500 17 PHE A 40 -58.80 -146.71
REMARK 500 17 ILE A 70 101.02 54.86
REMARK 500 17 ASP A 72 -162.75 54.64
REMARK 500 17 THR A 74 35.87 -148.03
REMARK 500 17 LEU A 82 176.68 -51.26
REMARK 500 17 SER A 98 69.64 -102.41
REMARK 500 17 SER A 99 -165.32 -106.55
REMARK 500 18 GLU A 3 -58.18 -120.67
REMARK 500 18 PHE A 40 -68.41 63.06
REMARK 500 18 ASP A 72 -165.37 51.24
REMARK 500 18 THR A 74 -54.85 -155.72
REMARK 500 18 GLU A 81 54.89 -169.30
REMARK 500 18 LEU A 82 -70.36 -111.40
REMARK 500 18 ALA A 101 75.56 52.70
REMARK 500 19 GLU A 42 -66.93 -103.05
REMARK 500 19 ILE A 70 92.32 53.17
REMARK 500 19 ASP A 72 -167.09 53.33
REMARK 500 19 THR A 74 37.11 -148.23
REMARK 500 19 LEU A 82 170.30 -48.06
REMARK 500 19 SER A 98 69.54 -103.46
REMARK 500 20 LYS A 12 -58.47 -127.46
REMARK 500 20 VAL A 26 84.25 -155.68
REMARK 500 20 PHE A 40 97.83 54.31
REMARK 500 20 ILE A 70 99.11 54.14
REMARK 500 20 ASP A 72 -164.17 51.94
REMARK 500 20 LEU A 82 -164.80 -111.10
REMARK 500 20 SER A 98 60.56 -103.69
REMARK 500 20 ALA A 101 81.28 53.01
REMARK 500 21 ALA A 2 -71.40 64.34
REMARK 500 21 GLU A 3 42.72 -140.76
REMARK 500 21 LYS A 22 49.76 -101.93
REMARK 500 21 PHE A 40 -69.12 62.96
REMARK 500 21 ILE A 70 98.74 54.36
REMARK 500 21 ASP A 72 -164.04 53.42
REMARK 500 21 SER A 98 67.29 -100.59
REMARK 500 21 LYS A 108 50.37 -119.65
REMARK 500 22 CYS A 21 149.33 -175.24
REMARK 500 22 PHE A 40 -58.56 -145.51
REMARK 500 22 THR A 66 57.69 -92.97
REMARK 500 22 ASP A 72 -165.23 52.86
REMARK 500 22 LEU A 82 -79.79 -94.77
REMARK 500 23 CYS A 21 132.00 179.59
REMARK 500 23 PHE A 40 -58.94 -147.07
REMARK 500 23 HIS A 52 -172.29 -58.50
REMARK 500 23 ILE A 70 94.86 52.93
REMARK 500 23 ASP A 72 -163.91 52.70
REMARK 500 23 THR A 74 81.96 -66.70
REMARK 500 23 GLU A 75 -53.42 -166.27
REMARK 500 23 LEU A 82 -163.33 -111.79
REMARK 500 23 SER A 98 66.85 -106.44
REMARK 500 23 ALA A 101 -163.69 -126.54
REMARK 500 24 GLU A 3 -59.91 -126.60
REMARK 500 24 LYS A 12 38.99 -148.12
REMARK 500 24 PHE A 40 -58.86 -145.68
REMARK 500 24 ILE A 70 101.95 54.35
REMARK 500 24 ASP A 72 -161.70 53.81
REMARK 500 24 GLU A 75 -58.35 -129.15
REMARK 500 24 SER A 98 58.09 -96.53
REMARK 500 24 ALA A 101 81.22 52.69
REMARK 500 25 LYS A 12 -57.83 -120.10
REMARK 500 25 LYS A 22 56.71 -97.75
REMARK 500 25 PHE A 40 -59.14 -147.67
REMARK 500 25 THR A 66 58.26 -96.96
REMARK 500 25 ILE A 70 99.49 54.28
REMARK 500 25 ASP A 72 -165.18 53.74
REMARK 500 25 LEU A 82 178.63 -51.76
REMARK 500 25 SER A 98 52.66 -96.92
REMARK 500 26 CYS A 21 143.65 -175.18
REMARK 500 26 PHE A 40 -57.70 -152.76
REMARK 500 26 ILE A 70 98.25 54.07
REMARK 500 26 ASP A 72 -165.36 54.37
REMARK 500 26 LEU A 82 177.21 -51.12
REMARK 500 26 SER A 98 54.03 -96.01
REMARK 500 27 LYS A 22 44.25 -104.87
REMARK 500 27 PHE A 40 -58.77 -145.87
REMARK 500 27 ASP A 72 -175.16 50.95
REMARK 500 27 THR A 74 39.19 -145.64
REMARK 500 27 LEU A 82 177.58 -50.88
REMARK 500 27 SER A 98 51.41 -97.93
REMARK 500 27 LYS A 100 72.10 53.16
REMARK 500 27 LYS A 107 -63.92 -124.92
REMARK 500 27 LYS A 108 40.93 -141.97
REMARK 500 28 LYS A 12 38.02 -151.77
REMARK 500 28 CYS A 21 150.78 179.59
REMARK 500 28 PHE A 40 100.49 55.30
REMARK 500 28 ILE A 70 99.85 52.87
REMARK 500 28 ASP A 72 -163.74 55.42
REMARK 500 28 GLU A 75 -58.61 -138.65
REMARK 500 28 LEU A 82 -173.94 -69.08
REMARK 500 28 SER A 99 55.66 -155.07
REMARK 500 28 LYS A 107 -61.29 -124.14
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 1 ARG A 5 0.31 SIDE CHAIN
REMARK 500 1 ARG A 13 0.26 SIDE CHAIN
REMARK 500 1 ARG A 31 0.20 SIDE CHAIN
REMARK 500 1 ARG A 62 0.23 SIDE CHAIN
REMARK 500 1 ARG A 64 0.25 SIDE CHAIN
REMARK 500 2 ARG A 5 0.28 SIDE CHAIN
REMARK 500 2 ARG A 13 0.22 SIDE CHAIN
REMARK 500 2 ARG A 31 0.20 SIDE CHAIN
REMARK 500 2 ARG A 62 0.22 SIDE CHAIN
REMARK 500 2 ARG A 64 0.24 SIDE CHAIN
REMARK 500 3 ARG A 5 0.29 SIDE CHAIN
REMARK 500 3 ARG A 13 0.32 SIDE CHAIN
REMARK 500 3 ARG A 31 0.32 SIDE CHAIN
REMARK 500 3 ARG A 62 0.25 SIDE CHAIN
REMARK 500 3 ARG A 64 0.31 SIDE CHAIN
REMARK 500 4 ARG A 5 0.24 SIDE CHAIN
REMARK 500 4 ARG A 13 0.23 SIDE CHAIN
REMARK 500 4 ARG A 31 0.24 SIDE CHAIN
REMARK 500 4 ARG A 62 0.27 SIDE CHAIN
REMARK 500 4 ARG A 64 0.22 SIDE CHAIN
REMARK 500 5 ARG A 5 0.31 SIDE CHAIN
REMARK 500 5 ARG A 13 0.27 SIDE CHAIN
REMARK 500 5 ARG A 31 0.23 SIDE CHAIN
REMARK 500 5 ARG A 62 0.27 SIDE CHAIN
REMARK 500 5 ARG A 64 0.32 SIDE CHAIN
REMARK 500 6 ARG A 5 0.26 SIDE CHAIN
REMARK 500 6 ARG A 13 0.31 SIDE CHAIN
REMARK 500 6 ARG A 31 0.23 SIDE CHAIN
REMARK 500 6 ARG A 62 0.31 SIDE CHAIN
REMARK 500 6 ARG A 64 0.26 SIDE CHAIN
REMARK 500 7 ARG A 5 0.22 SIDE CHAIN
REMARK 500 7 ARG A 13 0.22 SIDE CHAIN
REMARK 500 7 ARG A 31 0.29 SIDE CHAIN
REMARK 500 7 ARG A 62 0.25 SIDE CHAIN
REMARK 500 7 ARG A 64 0.28 SIDE CHAIN
REMARK 500 8 ARG A 5 0.32 SIDE CHAIN
REMARK 500 8 ARG A 13 0.30 SIDE CHAIN
REMARK 500 8 ARG A 31 0.22 SIDE CHAIN
REMARK 500 8 ARG A 62 0.24 SIDE CHAIN
REMARK 500 8 ARG A 64 0.31 SIDE CHAIN
REMARK 500 9 ARG A 5 0.32 SIDE CHAIN
REMARK 500 9 ARG A 13 0.23 SIDE CHAIN
REMARK 500 9 ARG A 31 0.29 SIDE CHAIN
REMARK 500 9 ARG A 62 0.23 SIDE CHAIN
REMARK 500 9 ARG A 64 0.29 SIDE CHAIN
REMARK 500 10 ARG A 5 0.23 SIDE CHAIN
REMARK 500 10 ARG A 13 0.31 SIDE CHAIN
REMARK 500 10 ARG A 31 0.26 SIDE CHAIN
REMARK 500 10 ARG A 62 0.27 SIDE CHAIN
REMARK 500 10 ARG A 64 0.32 SIDE CHAIN
REMARK 500 11 ARG A 5 0.25 SIDE CHAIN
REMARK 500 11 ARG A 13 0.26 SIDE CHAIN
REMARK 500 11 ARG A 31 0.24 SIDE CHAIN
REMARK 500 11 ARG A 62 0.23 SIDE CHAIN
REMARK 500 11 ARG A 64 0.27 SIDE CHAIN
REMARK 500 12 ARG A 5 0.23 SIDE CHAIN
REMARK 500 12 ARG A 13 0.28 SIDE CHAIN
REMARK 500 12 ARG A 31 0.21 SIDE CHAIN
REMARK 500 12 ARG A 62 0.28 SIDE CHAIN
REMARK 500 12 ARG A 64 0.31 SIDE CHAIN
REMARK 500 13 ARG A 5 0.32 SIDE CHAIN
REMARK 500 13 ARG A 13 0.23 SIDE CHAIN
REMARK 500 13 ARG A 31 0.32 SIDE CHAIN
REMARK 500 13 ARG A 62 0.25 SIDE CHAIN
REMARK 500 13 ARG A 64 0.23 SIDE CHAIN
REMARK 500 14 ARG A 5 0.24 SIDE CHAIN
REMARK 500 14 ARG A 13 0.24 SIDE CHAIN
REMARK 500 14 ARG A 31 0.32 SIDE CHAIN
REMARK 500 14 ARG A 62 0.25 SIDE CHAIN
REMARK 500 14 ARG A 64 0.22 SIDE CHAIN
REMARK 500 15 ARG A 5 0.32 SIDE CHAIN
REMARK 500 15 ARG A 13 0.28 SIDE CHAIN
REMARK 500 15 ARG A 31 0.25 SIDE CHAIN
REMARK 500 15 ARG A 62 0.29 SIDE CHAIN
REMARK 500 15 ARG A 64 0.21 SIDE CHAIN
REMARK 500 16 ARG A 5 0.30 SIDE CHAIN
REMARK 500 16 ARG A 13 0.29 SIDE CHAIN
REMARK 500 16 ARG A 31 0.27 SIDE CHAIN
REMARK 500 16 ARG A 62 0.25 SIDE CHAIN
REMARK 500 16 ARG A 64 0.30 SIDE CHAIN
REMARK 500 17 ARG A 5 0.31 SIDE CHAIN
REMARK 500 17 ARG A 13 0.23 SIDE CHAIN
REMARK 500 17 ARG A 31 0.26 SIDE CHAIN
REMARK 500 17 ARG A 62 0.25 SIDE CHAIN
REMARK 500 17 ARG A 64 0.32 SIDE CHAIN
REMARK 500 18 ARG A 5 0.25 SIDE CHAIN
REMARK 500 18 ARG A 13 0.28 SIDE CHAIN
REMARK 500 18 ARG A 31 0.31 SIDE CHAIN
REMARK 500 18 ARG A 62 0.21 SIDE CHAIN
REMARK 500 18 ARG A 64 0.32 SIDE CHAIN
REMARK 500 19 ARG A 5 0.28 SIDE CHAIN
REMARK 500 19 ARG A 13 0.29 SIDE CHAIN
REMARK 500 19 ARG A 31 0.31 SIDE CHAIN
REMARK 500 19 ARG A 62 0.27 SIDE CHAIN
REMARK 500 19 ARG A 64 0.31 SIDE CHAIN
REMARK 500 20 ARG A 5 0.23 SIDE CHAIN
REMARK 500 20 ARG A 13 0.23 SIDE CHAIN
REMARK 500 20 ARG A 31 0.23 SIDE CHAIN
REMARK 500 20 ARG A 62 0.29 SIDE CHAIN
REMARK 500 20 ARG A 64 0.30 SIDE CHAIN
REMARK 500 21 ARG A 5 0.24 SIDE CHAIN
REMARK 500 21 ARG A 13 0.32 SIDE CHAIN
REMARK 500 21 ARG A 31 0.22 SIDE CHAIN
REMARK 500 21 ARG A 62 0.31 SIDE CHAIN
REMARK 500 21 ARG A 64 0.31 SIDE CHAIN
REMARK 500 22 ARG A 5 0.21 SIDE CHAIN
REMARK 500 22 ARG A 13 0.29 SIDE CHAIN
REMARK 500 22 ARG A 31 0.22 SIDE CHAIN
REMARK 500 22 ARG A 62 0.24 SIDE CHAIN
REMARK 500 22 ARG A 64 0.31 SIDE CHAIN
REMARK 500 23 ARG A 5 0.31 SIDE CHAIN
REMARK 500 23 ARG A 13 0.21 SIDE CHAIN
REMARK 500 23 ARG A 31 0.29 SIDE CHAIN
REMARK 500 23 ARG A 62 0.22 SIDE CHAIN
REMARK 500 23 ARG A 64 0.21 SIDE CHAIN
REMARK 500 24 ARG A 5 0.28 SIDE CHAIN
REMARK 500 24 ARG A 13 0.23 SIDE CHAIN
REMARK 500 24 ARG A 31 0.22 SIDE CHAIN
REMARK 500 24 ARG A 62 0.25 SIDE CHAIN
REMARK 500 24 ARG A 64 0.29 SIDE CHAIN
REMARK 500 25 ARG A 5 0.31 SIDE CHAIN
REMARK 500 25 ARG A 13 0.26 SIDE CHAIN
REMARK 500 25 ARG A 31 0.32 SIDE CHAIN
REMARK 500 25 ARG A 62 0.32 SIDE CHAIN
REMARK 500 25 ARG A 64 0.32 SIDE CHAIN
REMARK 500 26 ARG A 5 0.31 SIDE CHAIN
REMARK 500 26 ARG A 13 0.31 SIDE CHAIN
REMARK 500 26 ARG A 31 0.27 SIDE CHAIN
REMARK 500 26 ARG A 62 0.21 SIDE CHAIN
REMARK 500 26 ARG A 64 0.30 SIDE CHAIN
REMARK 500 27 ARG A 5 0.30 SIDE CHAIN
REMARK 500 27 ARG A 13 0.22 SIDE CHAIN
REMARK 500 27 ARG A 31 0.31 SIDE CHAIN
REMARK 500 27 ARG A 62 0.26 SIDE CHAIN
REMARK 500 27 ARG A 64 0.28 SIDE CHAIN
REMARK 500 28 ARG A 5 0.27 SIDE CHAIN
REMARK 500 28 ARG A 13 0.23 SIDE CHAIN
REMARK 500 28 ARG A 31 0.26 SIDE CHAIN
REMARK 500 28 ARG A 62 0.31 SIDE CHAIN
REMARK 500 28 ARG A 64 0.29 SIDE CHAIN
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 ZN A1118 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 55 SG
REMARK 620 2 CYS A 21 SG 102.6
REMARK 620 3 CYS A 18 SG 117.1 101.6
REMARK 620 4 HIS A 52 ND1 119.1 117.9 97.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1118
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IMO RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF HUMAN DNA LIGASE IIIALPHA
REMARK 900 BRCT DOMAIN
REMARK 900 RELATED ID: 1IN1 RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF HUMAN DNA LIGASE IIIALPHA
REMARK 900 BRCT DOMAIN
DBREF 1UW0 A 1 117 UNP P49916 DNL3_HUMAN 1 117
SEQRES 1 A 117 MET ALA GLU GLN ARG PHE CYS VAL ASP TYR ALA LYS ARG
SEQRES 2 A 117 GLY THR ALA GLY CYS LYS LYS CYS LYS GLU LYS ILE VAL
SEQRES 3 A 117 LYS GLY VAL CYS ARG ILE GLY LYS VAL VAL PRO ASN PRO
SEQRES 4 A 117 PHE SER GLU SER GLY GLY ASP MET LYS GLU TRP TYR HIS
SEQRES 5 A 117 ILE LYS CYS MET PHE GLU LYS LEU GLU ARG ALA ARG ALA
SEQRES 6 A 117 THR THR LYS LYS ILE GLU ASP LEU THR GLU LEU GLU GLY
SEQRES 7 A 117 TRP GLU GLU LEU GLU ASP ASN GLU LYS GLU GLN ILE THR
SEQRES 8 A 117 GLN HIS ILE ALA ASP LEU SER SER LYS ALA ALA GLY THR
SEQRES 9 A 117 PRO LYS LYS LYS ALA VAL VAL GLN ALA LYS LEU THR THR
HET ZN A1118 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 HIS A 52 ALA A 63 1 12
HELIX 2 2 GLU A 83 SER A 99 1 17
SHEET 1 AA 3 ARG A 5 TYR A 10 0
SHEET 2 AA 3 CYS A 30 PRO A 37 -1 O ARG A 31 N ASP A 9
SHEET 3 AA 3 ASP A 46 MET A 47 -1 O MET A 47 N VAL A 36
SHEET 1 AB 2 ALA A 16 GLY A 17 0
SHEET 2 AB 2 LYS A 24 ILE A 25 -1 O ILE A 25 N ALA A 16
LINK ZN ZN A1118 SG CYS A 55 1555 1555 2.32
LINK ZN ZN A1118 SG CYS A 21 1555 1555 2.30
LINK ZN ZN A1118 SG CYS A 18 1555 1555 2.29
LINK ZN ZN A1118 ND1 HIS A 52 1555 1555 2.03
SITE 1 AC1 4 CYS A 18 CYS A 21 HIS A 52 CYS A 55
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - r 25 2 Bytes