Header list of 1nzp.pdb file
Complete list - 23 20 Bytes
HEADER DNA BINDING PROTEIN/TRANSFERASE 19-FEB-03 1NZP
TITLE SOLUTION STRUCTURE OF THE LYASE DOMAIN OF HUMAN DNA POLYMERASE LAMBDA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA POLYMERASE LAMBDA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: POLYMERASE LAMBDA LYASE DOMAIN(RESIDUES 242 - 327);
COMPND 5 SYNONYM: POL LAMBDA, DNA POLYMERASE LAMBDA, DNA POLYMERASE BETA-2,
COMPND 6 POL BETA2;
COMPND 7 EC: 2.7.7.7;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: POLL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BLR (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET30A(+)
KEYWDS DNA POLYMERASE LAMBDA, POL LAMBDA, LYASE DOMAIN, 8 KDA DOMAIN, POL
KEYWDS 2 BETA-LIKE, DNA BINDING PROTEIN-TRANSFERASE COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 8
MDLTYP MINIMIZED AVERAGE
AUTHOR E.F.DEROSE,T.W.KIRBY,G.A.MUELLER,K.BEBENEK,M.GARCIA-DIAZ,L.BLANCO,
AUTHOR 2 T.A.KUNKEL,R.E.LONDON
REVDAT 3 23-FEB-22 1NZP 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1NZP 1 VERSN
REVDAT 1 05-AUG-03 1NZP 0
JRNL AUTH E.F.DEROSE,T.W.KIRBY,G.A.MUELLER,K.BEBENEK,M.GARCIA-DIAZ,
JRNL AUTH 2 L.BLANCO,T.A.KUNKEL,R.E.LONDON
JRNL TITL SOLUTION STRUCTURE OF THE LYASE DOMAIN OF HUMAN DNA
JRNL TITL 2 POLYMERASE LAMBDA
JRNL REF BIOCHEMISTRY V. 42 9564 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12911298
JRNL DOI 10.1021/BI034298S
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, ARIA 1.1
REMARK 3 AUTHORS : VARIAN, INC. (VNMR), M. NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURE WAS COMPUTED USING DEFAULT ARIA PARAMETERS.
REMARK 3 281 MANUALLY ASSIGNED NOE DISTANCE RESTRAINTS WERE USED
REMARK 3 IN ADDITION TO THE NOE RESTRAINTS AUTOMATICALLY ASSIGNED
REMARK 3 BY ARIA. ARIA ASSIGNED 790 UNAMBIGUOUS AND 191 AMBIGUOUS
REMARK 3 NOE RESTRAINTS.
REMARK 4
REMARK 4 1NZP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-FEB-03.
REMARK 100 THE DEPOSITION ID IS D_1000018394.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : 5MM TRIS, 100MM NACL, 5MM NAN3
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM POL LAMBDA 8 KDA DOMAIN U
REMARK 210 -15N,13C; 5MM TRIS-D11; 100MM
REMARK 210 NACL; 1MM DTT; 5MM NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, NMRVIEW 5.0.4, CNS
REMARK 210 1.0, ARIA 1.1
REMARK 210 METHOD USED : SIMULATED ANNEALING TORSION
REMARK 210 ANGLE DYNAMICS FOLLOW BY
REMARK 210 CARTESIAN DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 8
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: CHEMICAL SHIFT ASSIGMENTS WERE MADE FROM 3D HNCACB,
REMARK 210 CBCA(CO)NH, HNCO, H(CCO)NH, AND (H)C(CO)NH EXPERIMENTS.
REMARK 210 AROMATIC RESONANCES WERE ASSIGNED USING 2D (HB)CB(CGCD)HD
REMARK 210 AND (HB)CB(CGCDCE)HE EXPERIMENTS.
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 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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-8
REMARK 465 RES C SSSEQI
REMARK 465 MET A 241
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 1 PRO A 244 -119.91 -78.91
REMARK 500 1 SER A 245 89.10 58.61
REMARK 500 1 LYS A 248 -162.26 -129.58
REMARK 500 1 ASN A 251 174.28 -58.70
REMARK 500 1 ASN A 253 -81.89 -99.70
REMARK 500 1 LEU A 254 -2.32 58.56
REMARK 500 1 PRO A 292 -173.87 -66.17
REMARK 500 1 THR A 294 -40.26 -138.75
REMARK 500 1 HIS A 321 -74.62 -146.90
REMARK 500 1 LEU A 322 -72.07 -129.37
REMARK 500 2 SER A 246 10.82 -168.64
REMARK 500 2 ASN A 253 49.32 -157.92
REMARK 500 2 ASP A 272 87.18 -66.36
REMARK 500 2 THR A 294 -32.75 -136.39
REMARK 500 2 GLU A 318 -34.14 71.16
REMARK 500 2 SER A 319 109.25 58.24
REMARK 500 2 HIS A 321 11.83 -144.98
REMARK 500 3 GLN A 243 84.76 56.20
REMARK 500 3 PRO A 244 47.36 -80.00
REMARK 500 3 LYS A 248 77.42 55.02
REMARK 500 3 HIS A 255 2.35 -65.99
REMARK 500 3 THR A 294 -40.65 -131.13
REMARK 500 3 GLU A 318 -106.15 -141.45
REMARK 500 3 SER A 319 94.34 47.31
REMARK 500 3 LEU A 322 84.22 -59.00
REMARK 500 3 ARG A 323 101.52 -55.79
REMARK 500 4 PRO A 244 -175.95 -66.24
REMARK 500 4 SER A 245 -31.48 -168.43
REMARK 500 4 SER A 246 -86.74 60.55
REMARK 500 4 GLN A 247 -162.79 58.80
REMARK 500 4 HIS A 252 -56.16 -131.36
REMARK 500 4 ASN A 253 -68.03 -138.22
REMARK 500 4 LEU A 254 37.25 39.36
REMARK 500 4 ASP A 272 84.38 -157.22
REMARK 500 4 GLU A 318 -82.90 -42.09
REMARK 500 5 GLN A 247 -83.80 62.91
REMARK 500 5 SER A 288 21.11 -153.35
REMARK 500 5 HIS A 290 -66.55 -107.63
REMARK 500 5 PRO A 292 155.25 -48.87
REMARK 500 5 THR A 294 -43.55 -133.13
REMARK 500 5 GLU A 318 -90.09 -68.92
REMARK 500 5 SER A 319 -96.62 50.32
REMARK 500 6 SER A 246 -81.89 -70.95
REMARK 500 6 GLN A 247 -12.86 -167.75
REMARK 500 6 PRO A 292 -173.77 -68.96
REMARK 500 6 GLU A 318 7.57 59.65
REMARK 500 7 SER A 246 -77.12 -130.11
REMARK 500 7 LYS A 248 71.19 -103.60
REMARK 500 7 THR A 250 106.61 -47.05
REMARK 500 7 ASN A 253 19.72 -150.04
REMARK 500
REMARK 500 THIS ENTRY HAS 68 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1NZP A 242 327 UNP Q9UGP5 DPOL_HUMAN 242 327
SEQADV 1NZP MET A 241 UNP Q9UGP5 CLONING ARTIFACT
SEQRES 1 A 87 MET ALA GLN PRO SER SER GLN LYS ALA THR ASN HIS ASN
SEQRES 2 A 87 LEU HIS ILE THR GLU LYS LEU GLU VAL LEU ALA LYS ALA
SEQRES 3 A 87 TYR SER VAL GLN GLY ASP LYS TRP ARG ALA LEU GLY TYR
SEQRES 4 A 87 ALA LYS ALA ILE ASN ALA LEU LYS SER PHE HIS LYS PRO
SEQRES 5 A 87 VAL THR SER TYR GLN GLU ALA CYS SER ILE PRO GLY ILE
SEQRES 6 A 87 GLY LYS ARG MET ALA GLU LYS ILE ILE GLU ILE LEU GLU
SEQRES 7 A 87 SER GLY HIS LEU ARG LYS LEU ASP HIS
HELIX 1 1 LEU A 254 GLY A 271 1 18
HELIX 2 2 ASP A 272 LYS A 287 1 16
HELIX 3 3 SER A 295 SER A 301 1 7
HELIX 4 4 GLY A 306 GLU A 318 1 13
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 - 23 20 Bytes