HEADER HYDROLASE/DNA 26-APR-00 1EWN
TITLE CRYSTAL STRUCTURE OF THE HUMAN AAG DNA REPAIR GLYCOSYLASE COMPLEXED
TITLE 2 WITH 1,N6-ETHENOADENINE-DNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-D(*GP*AP*CP*AP*TP*GP*(EDA)P*TP*TP*GP*CP*C)-3');
COMPND 3 CHAIN: D;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: 1,N6-ETHENOADENINE-DNA;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: DNA (5'-D(P*GP*CP*AP*AP*TP*CP*AP*TP*GP*TP*CP*A)-3');
COMPND 8 CHAIN: E;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: 3-METHYL-ADENINE DNA GLYCOSYLASE;
COMPND 12 CHAIN: A;
COMPND 13 FRAGMENT: E125Q;
COMPND 14 SYNONYM: ALKYLADENINE DNA GLYCOSYLASE, AAG;
COMPND 15 EC: 3.2.2.21;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 MOL_ID: 3;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PLM1
KEYWDS DNA REPAIR, GLYCOSYLASE, AAG, ANPG, MPG, 3-METHYLADENINE DNA
KEYWDS 2 GLYCOSYLASE, HYDROLASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.Y.LAU,M.D.WYATT,B.J.GLASSNER,L.D.SAMSON,T.ELLENBERGER
REVDAT 4 07-FEB-24 1EWN 1 REMARK
REVDAT 3 03-NOV-21 1EWN 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1EWN 1 VERSN
REVDAT 1 11-DEC-00 1EWN 0
JRNL AUTH A.Y.LAU,M.D.WYATT,B.J.GLASSNER,L.D.SAMSON,T.ELLENBERGER
JRNL TITL MOLECULAR BASIS FOR DISCRIMINATING BETWEEN NORMAL AND
JRNL TITL 2 DAMAGED BASES BY THE HUMAN ALKYLADENINE GLYCOSYLASE, AAG.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 97 13573 2000
JRNL REFN ISSN 0027-8424
JRNL PMID 11106395
JRNL DOI 10.1073/PNAS.97.25.13573
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 500.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 18163
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 SET) : 0.230
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1793
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1537
REMARK 3 NUCLEIC ACID ATOMS : 490
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 80
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.00
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.220
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 POWELL CONJUGATE GRADIENT MINIMIZATION AND TORSION ANGLE-RESTRAINED
REMARK 3 MOLECULAR DYNAMICS
REMARK 4
REMARK 4 1EWN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-APR-00.
REMARK 100 THE DEPOSITION ID IS D_1000010968.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-99
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0100
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRANDEIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18163
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 500.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 8.000
REMARK 200 R MERGE (I) : 0.04200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 8.00
REMARK 200 R MERGE FOR SHELL (I) : 0.20100
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: NULL
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, MGCL2, TRIS-HCL, GLYCEROL,
REMARK 280 PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 21.07250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 62.75850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.66800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 62.75850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.07250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.66800
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, 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. (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 LYS A 80
REMARK 465 GLY A 81
REMARK 465 LEU A 200
REMARK 465 ARG A 201
REMARK 465 LYS A 202
REMARK 465 GLY A 203
REMARK 465 THR A 204
REMARK 465 ALA A 205
REMARK 465 SER A 206
REMARK 465 ARG A 207
REMARK 465 LEU A 249
REMARK 465 GLU A 250
REMARK 465 PRO A 251
REMARK 465 SER A 252
REMARK 465 GLU A 253
REMARK 465 PRO A 254
REMARK 465 THR A 296
REMARK 465 GLN A 297
REMARK 465 ALA A 298
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 HIS A 82 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 131 CG CD OE1 OE2
REMARK 470 THR A 199 OG1 CG2
REMARK 470 VAL A 208 CG1 CG2
REMARK 470 LYS A 210 CG CD CE NZ
REMARK 470 GLN A 238 CG CD OE1 NE2
REMARK 470 GLU A 240 CG CD OE1 OE2
REMARK 470 GLU A 269 CG CD OE1 OE2
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 LEU A 83 -39.09 -19.98
REMARK 500 MET A 164 -26.75 -166.46
REMARK 500 GLN A 238 54.20 -142.96
REMARK 500 GLN A 294 34.57 -84.95
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 501 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET A 149 O
REMARK 620 2 SER A 171 OG 82.1
REMARK 620 3 SER A 172 O 168.8 89.1
REMARK 620 4 GLY A 174 O 99.9 162.8 86.5
REMARK 620 5 ALA A 177 O 94.5 99.8 93.9 97.1
REMARK 620 6 HOH A 541 O 85.7 80.7 86.0 82.4 179.5
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 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BNK RELATED DB: PDB
REMARK 900 CONTAINS THE SAME PROTEIN COMPLEXED WITH PYRROLIDINE-DNA
DBREF 1EWN A 80 298 UNP P29372 3MG_HUMAN 80 298
DBREF 1EWN D 1 12 PDB 1EWN 1EWN 1 12
DBREF 1EWN E 15 26 PDB 1EWN 1EWN 15 26
SEQADV 1EWN GLN A 125 UNP P29372 GLU 125 ENGINEERED MUTATION
SEQRES 1 D 12 DG DA DC DA DT DG EDA DT DT DG DC DC
SEQRES 1 E 12 DG DC DA DA DT DC DA DT DG DT DC DA
SEQRES 1 A 219 LYS GLY HIS LEU THR ARG LEU GLY LEU GLU PHE PHE ASP
SEQRES 2 A 219 GLN PRO ALA VAL PRO LEU ALA ARG ALA PHE LEU GLY GLN
SEQRES 3 A 219 VAL LEU VAL ARG ARG LEU PRO ASN GLY THR GLU LEU ARG
SEQRES 4 A 219 GLY ARG ILE VAL GLU THR GLN ALA TYR LEU GLY PRO GLU
SEQRES 5 A 219 ASP GLU ALA ALA HIS SER ARG GLY GLY ARG GLN THR PRO
SEQRES 6 A 219 ARG ASN ARG GLY MET PHE MET LYS PRO GLY THR LEU TYR
SEQRES 7 A 219 VAL TYR ILE ILE TYR GLY MET TYR PHE CYS MET ASN ILE
SEQRES 8 A 219 SER SER GLN GLY ASP GLY ALA CYS VAL LEU LEU ARG ALA
SEQRES 9 A 219 LEU GLU PRO LEU GLU GLY LEU GLU THR MET ARG GLN LEU
SEQRES 10 A 219 ARG SER THR LEU ARG LYS GLY THR ALA SER ARG VAL LEU
SEQRES 11 A 219 LYS ASP ARG GLU LEU CYS SER GLY PRO SER LYS LEU CYS
SEQRES 12 A 219 GLN ALA LEU ALA ILE ASN LYS SER PHE ASP GLN ARG ASP
SEQRES 13 A 219 LEU ALA GLN ASP GLU ALA VAL TRP LEU GLU ARG GLY PRO
SEQRES 14 A 219 LEU GLU PRO SER GLU PRO ALA VAL VAL ALA ALA ALA ARG
SEQRES 15 A 219 VAL GLY VAL GLY HIS ALA GLY GLU TRP ALA ARG LYS PRO
SEQRES 16 A 219 LEU ARG PHE TYR VAL ARG GLY SER PRO TRP VAL SER VAL
SEQRES 17 A 219 VAL ASP ARG VAL ALA GLU GLN ASP THR GLN ALA
MODRES 1EWN EDA D 7 DA
HET EDA D 7 23
HET NA A 501 1
HETNAM EDA 3-[2-DEOXY-RIBOFURANOSYL]-3H-1,3,4,5A,8-PENTAAZA-AS-
HETNAM 2 EDA INDACENE-5'-MONOPHOSPHATE
HETNAM NA SODIUM ION
FORMUL 1 EDA C12 H14 N5 O6 P
FORMUL 4 NA NA 1+
FORMUL 5 HOH *80(H2 O)
HELIX 1 1 GLY A 87 ASP A 92 1 6
HELIX 2 2 PRO A 94 LEU A 103 1 10
HELIX 3 3 SER A 137 ARG A 141 5 5
HELIX 4 4 ASN A 146 MET A 151 5 6
HELIX 5 5 GLY A 189 ARG A 197 1 9
HELIX 6 6 LYS A 210 LEU A 214 5 5
HELIX 7 7 GLY A 217 LEU A 225 1 9
HELIX 8 8 ASN A 228 ASP A 232 5 5
SHEET 1 A 6 LEU A 156 ILE A 161 0
SHEET 2 A 6 TYR A 165 SER A 171 -1 O TYR A 165 N ILE A 161
SHEET 3 A 6 CYS A 178 GLU A 188 -1 O VAL A 179 N ILE A 170
SHEET 4 A 6 GLU A 116 TYR A 127 -1 O ARG A 118 N LEU A 187
SHEET 5 A 6 VAL A 106 ARG A 110 -1 N LEU A 107 O GLY A 119
SHEET 6 A 6 VAL A 242 GLU A 245 -1 O TRP A 243 N VAL A 108
LINK O3' DG D 6 P EDA D 7 1555 1555 1.60
LINK O3' EDA D 7 P DT D 8 1555 1555 1.61
LINK O MET A 149 NA NA A 501 1555 1555 2.48
LINK OG SER A 171 NA NA A 501 1555 1555 2.47
LINK O SER A 172 NA NA A 501 1555 1555 2.40
LINK O GLY A 174 NA NA A 501 1555 1555 2.44
LINK O ALA A 177 NA NA A 501 1555 1555 2.43
LINK NA NA A 501 O HOH A 541 1555 1555 2.60
SITE 1 AC1 6 MET A 149 SER A 171 SER A 172 GLY A 174
SITE 2 AC1 6 ALA A 177 HOH A 541
CRYST1 42.145 57.336 125.517 90.00 90.00 90.00 P 21 21 21 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 0.023728 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017441 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007967 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
