HEADER TRANSFERASE 31-JUL-98 1BOO
TITLE PVUII DNA METHYLTRANSFERASE (CYTOSINE-N4-SPECIFIC)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (N-4 CYTOSINE-SPECIFIC METHYLTRANSFERASE PVU II);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: STARTING FROM THE INTERNAL TRANSLATION INITIATOR AT MET14;
COMPND 5 EC: 2.1.1.113;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PROTEUS VULGARIS;
SOURCE 3 ORGANISM_TAXID: 585;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI STR. K-12 SUBSTR. DH10B;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 316385;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: DH10B
KEYWDS TYPE II DNA-(CYTOSINE N4) METHYLTRANSFERASE, AMINO METHYLATION,
KEYWDS 2 SELENOMETHIONINE, MULTIWAVELENGTH ANOMALOUS DIFFRACTION, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.GONG,M.O'GARA,R.M.BLUMENTHAL,X.CHENG
REVDAT 5 21-DEC-22 1BOO 1 REMARK SEQADV
REVDAT 4 24-FEB-09 1BOO 1 VERSN
REVDAT 3 01-APR-03 1BOO 1 JRNL
REVDAT 2 22-DEC-99 1BOO 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 12-AUG-98 1BOO 0
JRNL AUTH W.GONG,M.O'GARA,R.M.BLUMENTHAL,X.CHENG
JRNL TITL STRUCTURE OF PVU II DNA-(CYTOSINE N4) METHYLTRANSFERASE, AN
JRNL TITL 2 EXAMPLE OF DOMAIN PERMUTATION AND PROTEIN FOLD ASSIGNMENT.
JRNL REF NUCLEIC ACIDS RES. V. 25 2702 1997
JRNL REFN ISSN 0305-1048
JRNL PMID 9207015
JRNL DOI 10.1093/NAR/25.14.2702
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.O'GARA,G.M.ADAMS,W.GONG,R.KOBAYASHI,R.M.BLUMENTHAL,X.CHENG
REMARK 1 TITL EXPRESSION, PURIFICATION, MASS SPECTROMETRY, CRYSTALLIZATION
REMARK 1 TITL 2 AND MULTIWAVELENGTH ANOMALOUS DIFFRACTION OF SELENOMETHIONYL
REMARK 1 TITL 3 PVUII DNA METHYLTRANSFERASE (CYTOSINE-N4-SPECIFIC)
REMARK 1 REF EUR.J.BIOCHEM. V. 247 1009 1997
REMARK 1 REFN ISSN 0014-2956
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 14886
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.283
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : 2219
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 0
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 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) : 0.020
REMARK 3 BOND ANGLES (DEGREES) : 2.900
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 2.200
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 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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BOO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE DEPOSITION ID IS D_1000008126.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 289
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98233,0.98211,0.92,1.072
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14886
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.680
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.22600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.2, 0.2 M SODIUM
REMARK 280 ACETATE 20% POLYETHYLENE GLYCOL 400
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 56.20000
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: 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. (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 14
REMARK 465 LEU A 15
REMARK 465 PRO A 179
REMARK 465 TYR A 180
REMARK 465 SER A 181
REMARK 465 ASP A 182
REMARK 465 ARG A 183
REMARK 465 MET A 184
REMARK 465 LYS A 185
REMARK 465 LYS A 186
REMARK 465 LEU A 187
REMARK 465 ILE A 188
REMARK 465 GLU A 189
REMARK 465 ASP A 190
REMARK 465 PRO A 191
REMARK 465 ASP A 192
REMARK 465 LYS A 193
REMARK 465 PHE A 194
REMARK 465 TYR A 195
REMARK 465 THR A 196
REMARK 465 PRO A 197
REMARK 465 LYS A 198
REMARK 465 THR A 199
REMARK 465 ARG A 200
REMARK 465 PRO A 201
REMARK 465 SER A 202
REMARK 465 GLY A 203
REMARK 465 HIS A 204
REMARK 465 ASP A 205
REMARK 465 ILE A 206
REMARK 465 GLY A 207
REMARK 465 LYS A 208
REMARK 465 SER A 209
REMARK 465 PHE A 210
REMARK 465 SER A 211
REMARK 465 LYS A 212
REMARK 465 ASP A 213
REMARK 465 ASN A 214
REMARK 465 GLY A 215
REMARK 465 GLY A 216
REMARK 465 ILE A 336
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 GLN A 59 CG CD OE1 NE2
REMARK 470 ARG A 60 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 61 CG CD CE NZ
REMARK 470 LYS A 62 CG CD CE NZ
REMARK 470 GLU A 63 CG CD OE1 OE2
REMARK 470 TYR A 64 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASN A 66 CG OD1 ND2
REMARK 470 GLU A 68 CG CD OE1 OE2
REMARK 470 GLU A 71 CG CD OE1 OE2
REMARK 470 LEU A 139 CG CD1 CD2
REMARK 470 GLN A 233 CG CD OE1 NE2
REMARK 470 LYS A 239 CG CD CE NZ
REMARK 470 LYS A 244 CG CD CE NZ
REMARK 470 ASP A 309 CG OD1 OD2
REMARK 470 ASN A 310 CG OD1 ND2
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 MET A 30 CG - SD - CE ANGL. DEV. = 9.8 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 PRO A 43 -166.40 -55.08
REMARK 500 LEU A 58 70.85 27.15
REMARK 500 GLN A 59 -125.41 89.99
REMARK 500 ARG A 60 160.05 151.98
REMARK 500 LYS A 61 102.67 -22.61
REMARK 500 LYS A 62 113.48 167.02
REMARK 500 TYR A 64 -76.91 115.77
REMARK 500 LEU A 67 86.58 171.82
REMARK 500 GLU A 68 -42.98 -22.17
REMARK 500 GLU A 129 139.10 -171.98
REMARK 500 PRO A 140 -5.94 -56.07
REMARK 500 VAL A 146 -82.97 -87.20
REMARK 500 LYS A 148 -80.97 -75.94
REMARK 500 ASN A 231 -64.29 -125.76
REMARK 500 LEU A 254 -70.11 -68.36
REMARK 500 THR A 279 -71.34 -55.70
REMARK 500 LEU A 308 -168.32 -120.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 401
DBREF 1BOO A 14 336 UNP P11409 MTP2_PROVU 14 336
SEQADV 1BOO GLU A 44 UNP P11409 ASP 44 CONFLICT
SEQRES 1 A 323 MET LEU ASN PHE GLY LYS LYS PRO ALA TYR THR THR SER
SEQRES 2 A 323 ASN GLY SER MET TYR ILE GLY ASP SER LEU GLU LEU LEU
SEQRES 3 A 323 GLU SER PHE PRO GLU GLU SER ILE SER LEU VAL MET THR
SEQRES 4 A 323 SER PRO PRO PHE ALA LEU GLN ARG LYS LYS GLU TYR GLY
SEQRES 5 A 323 ASN LEU GLU GLN HIS GLU TYR VAL ASP TRP PHE LEU SER
SEQRES 6 A 323 PHE ALA LYS VAL VAL ASN LYS LYS LEU LYS PRO ASP GLY
SEQRES 7 A 323 SER PHE VAL VAL ASP PHE GLY GLY ALA TYR MET LYS GLY
SEQRES 8 A 323 VAL PRO ALA ARG SER ILE TYR ASN PHE ARG VAL LEU ILE
SEQRES 9 A 323 ARG MET ILE ASP GLU VAL GLY PHE PHE LEU ALA GLU ASP
SEQRES 10 A 323 PHE TYR TRP PHE ASN PRO SER LYS LEU PRO SER PRO ILE
SEQRES 11 A 323 GLU TRP VAL ASN LYS ARG LYS ILE ARG VAL LYS ASP ALA
SEQRES 12 A 323 VAL ASN THR VAL TRP TRP PHE SER LYS THR GLU TRP PRO
SEQRES 13 A 323 LYS SER ASP ILE THR LYS VAL LEU ALA PRO TYR SER ASP
SEQRES 14 A 323 ARG MET LYS LYS LEU ILE GLU ASP PRO ASP LYS PHE TYR
SEQRES 15 A 323 THR PRO LYS THR ARG PRO SER GLY HIS ASP ILE GLY LYS
SEQRES 16 A 323 SER PHE SER LYS ASP ASN GLY GLY SER ILE PRO PRO ASN
SEQRES 17 A 323 LEU LEU GLN ILE SER ASN SER GLU SER ASN GLY GLN TYR
SEQRES 18 A 323 LEU ALA ASN CYS LYS LEU MET GLY ILE LYS ALA HIS PRO
SEQRES 19 A 323 ALA ARG PHE PRO ALA LYS LEU PRO GLU PHE PHE ILE ARG
SEQRES 20 A 323 MET LEU THR GLU PRO ASP ASP LEU VAL VAL ASP ILE PHE
SEQRES 21 A 323 GLY GLY SER ASN THR THR GLY LEU VAL ALA GLU ARG GLU
SEQRES 22 A 323 SER ARG LYS TRP ILE SER PHE GLU MET LYS PRO GLU TYR
SEQRES 23 A 323 VAL ALA ALA SER ALA PHE ARG PHE LEU ASP ASN ASN ILE
SEQRES 24 A 323 SER GLU GLU LYS ILE THR ASP ILE TYR ASN ARG ILE LEU
SEQRES 25 A 323 ASN GLY GLU SER LEU ASP LEU ASN SER ILE ILE
HET SAH A 401 26
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
FORMUL 2 SAH C14 H20 N6 O5 S
HELIX 1 HC ASP A 34 SER A 41 1 8
HELIX 2 HZ LYS A 253 LEU A 262 1 10
HELIX 3 HA THR A 278 ARG A 285 1 8
HELIX 4 HB PRO A 297 ALA A 304 1 8
HELIX 5 HB1 GLU A 314 LEU A 325 1 12
SHEET 1 S31 1 TYR A 23 THR A 25 0
SHEET 1 S3 1 GLY A 28 TYR A 31 0
SHEET 1 S4 1 SER A 48 THR A 52 0
SHEET 1 S5 1 GLY A 91 PHE A 97 0
SHEET 1 S6 1 ALA A 128 PHE A 134 0
SHEET 1 S7 1 VAL A 157 SER A 164 0
SHEET 1 S8 1 LEU A 222 ILE A 225 0
SHEET 1 S1 1 LEU A 268 ASP A 271 0
SHEET 1 S2 1 LYS A 289 GLU A 294 0
SHEET 1 S32 1 SER A 329 LEU A 332 0
SHEET 1 S51 1 TYR A 101 MET A 102 0
SHEET 1 S52 1 VAL A 105 ALA A 107 0
SITE 1 AC1 18 GLY A 33 ASP A 34 SER A 35 SER A 53
SITE 2 AC1 18 PRO A 55 HIS A 246 ALA A 248 ARG A 249
SITE 3 AC1 18 PHE A 250 ILE A 272 PHE A 273 GLY A 274
SITE 4 AC1 18 GLY A 275 SER A 276 THR A 278 GLU A 294
SITE 5 AC1 18 MET A 295 TYR A 299
CRYST1 48.800 112.400 59.300 90.00 109.20 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 0.020492 0.000000 0.007136 0.00000
SCALE2 0.000000 0.008897 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017857 0.00000
MTRIX1 1 0.697500 -0.604100 0.385500 19.35190 1
MTRIX2 1 -0.601600 -0.785900 -0.143000 106.80000 1
MTRIX3 1 0.389300 -0.132200 -0.911600 81.29650 1
(ATOM LINES ARE NOT SHOWN.)
END
