HEADER TRANSFERASE/DNA 22-NOV-16 5TZV
TITLE BINARY COMPLEX CRYSTAL STRUCTURE OF DNA POLYMERASE BETA WITH G:T
TITLE 2 MISMATCH AT THE PRIMER TERMINUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA POLYMERASE BETA;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.7.7.7,4.2.99.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: DNA (5'-D(*CP*CP*GP*AP*CP*AP*GP*CP*GP*CP*AP*TP*CP*AP*GP*C)-
COMPND 8 3');
COMPND 9 CHAIN: T;
COMPND 10 ENGINEERED: YES;
COMPND 11 OTHER_DETAILS: TEMPLATE STRAND;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: DNA (5'-D(*GP*CP*TP*GP*AP*TP*GP*CP*GP*T)-3');
COMPND 14 CHAIN: P;
COMPND 15 ENGINEERED: YES;
COMPND 16 OTHER_DETAILS: PRIMER STRAND;
COMPND 17 MOL_ID: 4;
COMPND 18 MOLECULE: DNA (5'-D(P*GP*TP*CP*GP*G)-3');
COMPND 19 CHAIN: D;
COMPND 20 ENGINEERED: YES;
COMPND 21 OTHER_DETAILS: DOWNSTREAM PRIMER
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: POLB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PWL11;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 18 ORGANISM_COMMON: HUMAN;
SOURCE 19 ORGANISM_TAXID: 9606;
SOURCE 20 MOL_ID: 4;
SOURCE 21 SYNTHETIC: YES;
SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 23 ORGANISM_COMMON: HUMAN;
SOURCE 24 ORGANISM_TAXID: 9606
KEYWDS DNA POLYMERASE, FIDELITY, MISMATCH EXTENSION, TRANSFERASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.H.WILSON,V.K.BATRA
REVDAT 2 04-OCT-23 5TZV 1 JRNL LINK
REVDAT 1 07-DEC-16 5TZV 0
SPRSDE 07-DEC-16 5TZV 5J0V
JRNL AUTH V.K.BATRA,W.A.BEARD,L.C.PEDERSEN,S.H.WILSON
JRNL TITL STRUCTURES OF DNA POLYMERASE MISPAIRED DNA TERMINI
JRNL TITL 2 TRANSITIONING TO PRE-CATALYTIC COMPLEXES SUPPORT AN
JRNL TITL 3 INDUCED-FIT FIDELITY MECHANISM.
JRNL REF STRUCTURE V. 24 1863 2016
JRNL REFN ISSN 0969-2126
JRNL PMID 27642161
JRNL DOI 10.1016/J.STR.2016.08.006
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1_2155
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.10
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 30071
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.010
REMARK 3 FREE R VALUE TEST SET COUNT : 3009
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 22.1015 - 5.4873 1.00 1350 135 0.1492 0.1711
REMARK 3 2 5.4873 - 4.3665 1.00 1323 143 0.1524 0.1770
REMARK 3 3 4.3665 - 3.8177 1.00 1304 156 0.1488 0.1874
REMARK 3 4 3.8177 - 3.4701 1.00 1300 149 0.1473 0.2197
REMARK 3 5 3.4701 - 3.2222 1.00 1288 149 0.1530 0.2149
REMARK 3 6 3.2222 - 3.0328 1.00 1323 143 0.1875 0.2346
REMARK 3 7 3.0328 - 2.8812 1.00 1323 117 0.2173 0.2802
REMARK 3 8 2.8812 - 2.7560 0.99 1292 138 0.2017 0.2889
REMARK 3 9 2.7560 - 2.6501 1.00 1296 161 0.2000 0.2147
REMARK 3 10 2.6501 - 2.5588 1.00 1297 146 0.1958 0.2365
REMARK 3 11 2.5588 - 2.4789 0.99 1271 146 0.1971 0.3124
REMARK 3 12 2.4789 - 2.4081 0.99 1290 158 0.1928 0.2436
REMARK 3 13 2.4081 - 2.3448 0.99 1286 156 0.1931 0.2767
REMARK 3 14 2.3448 - 2.2877 0.99 1274 137 0.1806 0.2603
REMARK 3 15 2.2877 - 2.2357 0.99 1313 133 0.1763 0.2323
REMARK 3 16 2.2357 - 2.1882 0.99 1258 131 0.1818 0.2466
REMARK 3 17 2.1882 - 2.1444 0.99 1316 146 0.1805 0.2686
REMARK 3 18 2.1444 - 2.1040 0.98 1245 152 0.1779 0.2506
REMARK 3 19 2.1040 - 2.0665 0.98 1298 149 0.1778 0.2497
REMARK 3 20 2.0665 - 2.0314 0.98 1264 138 0.1792 0.2468
REMARK 3 21 2.0314 - 1.9987 0.90 1151 126 0.1938 0.2566
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.060
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 3376
REMARK 3 ANGLE : 0.915 4675
REMARK 3 CHIRALITY : 0.050 514
REMARK 3 PLANARITY : 0.005 495
REMARK 3 DIHEDRAL : 18.080 1941
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5TZV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-NOV-16.
REMARK 100 THE DEPOSITION ID IS D_1000225085.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-MAR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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 MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : VIRAMAX
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 92
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30098
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.18100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 1BPX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM IMIDAZOLE, 350 MM SODIUM
REMARK 280 CHLORIDE, 17% PEG3350, PH 7.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 39.70000
REMARK 290 SMTRY3 2 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, T, P, D
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 1
REMARK 465 SER A 2
REMARK 465 LYS A 3
REMARK 465 ARG A 4
REMARK 465 LYS A 5
REMARK 465 LYS A 206
REMARK 465 GLN A 207
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASN A 245 CG OD1 ND2
REMARK 470 ASP A 246 CG OD1 OD2
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 NE1 TRP A 325 O HOH A 501 1.98
REMARK 500 NH1 ARG A 112 O HOH A 502 2.08
REMARK 500 O HOH A 875 O HOH A 878 2.11
REMARK 500 O HOH T 118 O HOH T 156 2.11
REMARK 500 O HOH T 169 O HOH T 184 2.13
REMARK 500 O HOH A 638 O HOH A 889 2.13
REMARK 500 O HOH A 857 O HOH P 115 2.14
REMARK 500 NH1 ARG A 283 O ILE A 293 2.14
REMARK 500 O HOH T 142 O HOH T 179 2.16
REMARK 500 O HOH A 605 O HOH A 633 2.16
REMARK 500 O HOH A 637 O HOH A 821 2.16
REMARK 500 OP2 DA T 14 O HOH T 101 2.16
REMARK 500 O HOH D 102 O HOH D 128 2.17
REMARK 500 OD1 ASP A 192 O HOH A 503 2.18
REMARK 500 O HOH A 794 O HOH A 805 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 DG D 1 P DG D 1 OP3 -0.104
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 PRO A 50 36.49 -86.05
REMARK 500 ASP A 170 115.79 -160.85
REMARK 500 CYS A 178 -139.78 -102.53
REMARK 500 LYS A 230 117.72 -161.24
REMARK 500 ASP A 246 75.27 57.70
REMARK 500 ASN A 294 -165.32 -121.19
REMARK 500 ARG A 333 32.74 -94.08
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 NA A 403 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 30 O
REMARK 620 2 SER A 171 OG 43.2
REMARK 620 3 HOH A 620 O 46.6 3.9
REMARK 620 4 HOH A 686 O 45.4 2.2 2.0
REMARK 620 5 HOH A 774 O 43.3 3.6 3.8 4.0
REMARK 620 6 HOH A 820 O 45.7 4.5 2.2 3.6 2.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 60 O
REMARK 620 2 LEU A 62 O 91.9
REMARK 620 3 VAL A 65 O 89.7 99.5
REMARK 620 4 HOH A 811 O 88.9 92.8 167.7
REMARK 620 5 DC D 3 OP1 172.0 95.9 91.1 88.6
REMARK 620 6 HOH D 116 O 91.7 172.8 86.8 81.0 80.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 401 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 101 O
REMARK 620 2 VAL A 103 O 91.6
REMARK 620 3 ILE A 106 O 92.1 87.6
REMARK 620 4 HOH A 805 O 85.6 97.7 174.3
REMARK 620 5 DG P 9 OP1 170.7 96.0 93.5 88.1
REMARK 620 6 HOH P 116 O 81.3 170.9 86.9 87.5 91.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 404 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 101 O
REMARK 620 2 HOH A 659 O 82.4
REMARK 620 3 HOH A 803 O 149.0 92.6
REMARK 620 4 HOH A 805 O 85.0 166.3 101.0
REMARK 620 5 HOH A 871 O 117.1 85.1 92.7 96.0
REMARK 620 6 HOH P 116 O 73.4 96.3 76.8 85.1 169.4
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 404
DBREF 5TZV A 1 335 UNP P06746 DPOLB_HUMAN 1 335
DBREF 5TZV T 1 16 PDB 5TZV 5TZV 1 16
DBREF 5TZV P 1 10 PDB 5TZV 5TZV 1 10
DBREF 5TZV D 1 5 PDB 5TZV 5TZV 1 5
SEQRES 1 A 335 MET SER LYS ARG LYS ALA PRO GLN GLU THR LEU ASN GLY
SEQRES 2 A 335 GLY ILE THR ASP MET LEU THR GLU LEU ALA ASN PHE GLU
SEQRES 3 A 335 LYS ASN VAL SER GLN ALA ILE HIS LYS TYR ASN ALA TYR
SEQRES 4 A 335 ARG LYS ALA ALA SER VAL ILE ALA LYS TYR PRO HIS LYS
SEQRES 5 A 335 ILE LYS SER GLY ALA GLU ALA LYS LYS LEU PRO GLY VAL
SEQRES 6 A 335 GLY THR LYS ILE ALA GLU LYS ILE ASP GLU PHE LEU ALA
SEQRES 7 A 335 THR GLY LYS LEU ARG LYS LEU GLU LYS ILE ARG GLN ASP
SEQRES 8 A 335 ASP THR SER SER SER ILE ASN PHE LEU THR ARG VAL SER
SEQRES 9 A 335 GLY ILE GLY PRO SER ALA ALA ARG LYS PHE VAL ASP GLU
SEQRES 10 A 335 GLY ILE LYS THR LEU GLU ASP LEU ARG LYS ASN GLU ASP
SEQRES 11 A 335 LYS LEU ASN HIS HIS GLN ARG ILE GLY LEU LYS TYR PHE
SEQRES 12 A 335 GLY ASP PHE GLU LYS ARG ILE PRO ARG GLU GLU MET LEU
SEQRES 13 A 335 GLN MET GLN ASP ILE VAL LEU ASN GLU VAL LYS LYS VAL
SEQRES 14 A 335 ASP SER GLU TYR ILE ALA THR VAL CYS GLY SER PHE ARG
SEQRES 15 A 335 ARG GLY ALA GLU SER SER GLY ASP MET ASP VAL LEU LEU
SEQRES 16 A 335 THR HIS PRO SER PHE THR SER GLU SER THR LYS GLN PRO
SEQRES 17 A 335 LYS LEU LEU HIS GLN VAL VAL GLU GLN LEU GLN LYS VAL
SEQRES 18 A 335 HIS PHE ILE THR ASP THR LEU SER LYS GLY GLU THR LYS
SEQRES 19 A 335 PHE MET GLY VAL CYS GLN LEU PRO SER LYS ASN ASP GLU
SEQRES 20 A 335 LYS GLU TYR PRO HIS ARG ARG ILE ASP ILE ARG LEU ILE
SEQRES 21 A 335 PRO LYS ASP GLN TYR TYR CYS GLY VAL LEU TYR PHE THR
SEQRES 22 A 335 GLY SER ASP ILE PHE ASN LYS ASN MET ARG ALA HIS ALA
SEQRES 23 A 335 LEU GLU LYS GLY PHE THR ILE ASN GLU TYR THR ILE ARG
SEQRES 24 A 335 PRO LEU GLY VAL THR GLY VAL ALA GLY GLU PRO LEU PRO
SEQRES 25 A 335 VAL ASP SER GLU LYS ASP ILE PHE ASP TYR ILE GLN TRP
SEQRES 26 A 335 LYS TYR ARG GLU PRO LYS ASP ARG SER GLU
SEQRES 1 T 16 DC DC DG DA DC DA DG DC DG DC DA DT DC
SEQRES 2 T 16 DA DG DC
SEQRES 1 P 10 DG DC DT DG DA DT DG DC DG DT
SEQRES 1 D 5 DG DT DC DG DG
HET NA A 401 1
HET NA A 402 1
HET NA A 403 1
HET NA A 404 1
HETNAM NA SODIUM ION
FORMUL 5 NA 4(NA 1+)
FORMUL 9 HOH *591(H2 O)
HELIX 1 AA1 ASN A 12 VAL A 29 1 18
HELIX 2 AA2 ALA A 32 TYR A 49 1 18
HELIX 3 AA3 SER A 55 LYS A 61 1 7
HELIX 4 AA4 GLY A 66 GLY A 80 1 15
HELIX 5 AA5 LEU A 82 ASP A 91 1 10
HELIX 6 AA6 ASP A 91 THR A 101 1 11
HELIX 7 AA7 GLY A 107 GLU A 117 1 11
HELIX 8 AA8 THR A 121 LYS A 127 1 7
HELIX 9 AA9 ASN A 128 LEU A 132 5 5
HELIX 10 AB1 ASN A 133 TYR A 142 1 10
HELIX 11 AB2 TYR A 142 LYS A 148 1 7
HELIX 12 AB3 ARG A 152 ASP A 170 1 19
HELIX 13 AB4 CYS A 178 ARG A 183 1 6
HELIX 14 AB5 LYS A 209 VAL A 221 1 13
HELIX 15 AB6 PRO A 261 ASP A 263 5 3
HELIX 16 AB7 GLN A 264 GLY A 274 1 11
HELIX 17 AB8 SER A 275 LYS A 289 1 15
HELIX 18 AB9 SER A 315 ILE A 323 1 9
HELIX 19 AC1 GLU A 329 ARG A 333 5 5
SHEET 1 AA1 2 ILE A 150 PRO A 151 0
SHEET 2 AA1 2 SER A 187 SER A 188 -1 O SER A 188 N ILE A 150
SHEET 1 AA2 5 ILE A 174 VAL A 177 0
SHEET 2 AA2 5 MET A 191 THR A 196 -1 O LEU A 194 N THR A 176
SHEET 3 AA2 5 ARG A 253 LEU A 259 1 O ARG A 258 N LEU A 195
SHEET 4 AA2 5 LYS A 234 CYS A 239 -1 N PHE A 235 O ILE A 257
SHEET 5 AA2 5 ILE A 224 LYS A 230 -1 N SER A 229 O MET A 236
SHEET 1 AA3 2 PHE A 291 ILE A 293 0
SHEET 2 AA3 2 ILE A 298 PRO A 300 -1 O ARG A 299 N THR A 292
LINK O SER A 30 NA NA A 403 1555 1655 2.42
LINK O LYS A 60 NA NA A 402 1555 1555 2.35
LINK O LEU A 62 NA NA A 402 1555 1555 2.41
LINK O VAL A 65 NA NA A 402 1555 1555 2.27
LINK O THR A 101 NA NA A 401 1555 1555 2.34
LINK O THR A 101 NA NA A 404 1555 1555 2.52
LINK O VAL A 103 NA NA A 401 1555 1555 2.46
LINK O ILE A 106 NA NA A 401 1555 1555 2.37
LINK OG SER A 171 NA NA A 403 1555 1555 2.41
LINK NA NA A 401 O HOH A 805 1555 1555 2.63
LINK NA NA A 401 OP1 DG P 9 1555 1555 2.38
LINK NA NA A 401 O HOH P 116 1555 1555 2.50
LINK NA NA A 402 O HOH A 811 1555 1555 2.79
LINK NA NA A 402 OP1 DC D 3 1555 1555 2.83
LINK NA NA A 402 O HOH D 116 1555 1555 2.30
LINK NA NA A 403 O HOH A 620 1555 1555 2.51
LINK NA NA A 403 O HOH A 686 1555 1455 2.35
LINK NA NA A 403 O HOH A 774 1555 1555 2.41
LINK NA NA A 403 O HOH A 820 1555 1455 2.73
LINK NA NA A 404 O HOH A 659 1555 1555 2.62
LINK NA NA A 404 O HOH A 803 1555 1555 2.39
LINK NA NA A 404 O HOH A 805 1555 1555 2.49
LINK NA NA A 404 O HOH A 871 1555 1555 2.29
LINK NA NA A 404 O HOH P 116 1555 1555 2.75
CISPEP 1 GLY A 274 SER A 275 0 -1.55
SITE 1 AC1 7 THR A 101 VAL A 103 ILE A 106 NA A 404
SITE 2 AC1 7 HOH A 805 DG P 9 HOH P 116
SITE 1 AC2 6 LYS A 60 LEU A 62 VAL A 65 HOH A 811
SITE 2 AC2 6 DC D 3 HOH D 116
SITE 1 AC3 6 SER A 30 SER A 171 HOH A 620 HOH A 686
SITE 2 AC3 6 HOH A 774 HOH A 820
SITE 1 AC4 7 THR A 101 NA A 401 HOH A 659 HOH A 803
SITE 2 AC4 7 HOH A 805 HOH A 871 HOH P 116
CRYST1 54.510 79.400 54.710 90.00 105.75 90.00 P 1 21 1 2
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 0.018345 0.000000 0.005174 0.00000
SCALE2 0.000000 0.012594 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018991 0.00000
(ATOM LINES ARE NOT SHOWN.)
END