HEADER TRANSFERASE 20-JUL-04 1U2Z
TITLE CRYSTAL STRUCTURE OF HISTONE K79 METHYLTRANSFERASE DOT1P FROM YEAST
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-79 SPECIFIC;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN;
COMPND 5 SYNONYM: HISTONE H3-K79 METHYLTRANSFERASE, H3-K79-HMTASE, DISRUPTER
COMPND 6 OF TELOMERE SILENCING PROTEIN 1;
COMPND 7 EC: 2.1.1.43;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: DOT1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PXC415
KEYWDS HISTONE METHYLTRANSFERASE, NUCLEOSOME, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.SAWADA,Z.YANG,J.R.HORTON,R.E.COLLINS,X.ZHANG,X.CHENG
REVDAT 4 13-MAR-24 1U2Z 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1U2Z 1 VERSN
REVDAT 2 24-JAN-06 1U2Z 1 JRNL
REVDAT 1 07-SEP-04 1U2Z 0
JRNL AUTH K.SAWADA,Z.YANG,J.R.HORTON,R.E.COLLINS,X.ZHANG,X.CHENG
JRNL TITL STRUCTURE OF THE CONSERVED CORE OF THE YEAST DOT1P, A
JRNL TITL 2 NUCLEOSOMAL HISTONE H3 LYSINE 79 METHYLTRANSFERASE
JRNL REF J.BIOL.CHEM. V. 279 43296 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15292170
JRNL DOI 10.1074/JBC.M405902200
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1019720.490
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 78422
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) : 0.213
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3958
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 12051
REMARK 3 BIN R VALUE (WORKING SET) : 0.2720
REMARK 3 BIN FREE R VALUE : 0.3130
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 641
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9298
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 78
REMARK 3 SOLVENT ATOMS : 533
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.80000
REMARK 3 B22 (A**2) : 4.90000
REMARK 3 B33 (A**2) : -4.10000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.77000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM SIGMAA (A) : 0.24
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.34
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.33
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.040
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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 : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 43.29
REMARK 3
REMARK 3 NCS MODEL : CONSTR
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : SAM.PARAM
REMARK 3 PARAMETER FILE 4 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 5 : ION.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1U2Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-JUL-04.
REMARK 100 THE DEPOSITION ID IS D_1000023179.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-NOV-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X26C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79720
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.190
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.30200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, GLYCEROL, HEPES, PH 7.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K
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 73.13750
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 150
REMARK 465 GLY A 151
REMARK 465 HIS A 152
REMARK 465 HIS A 153
REMARK 465 HIS A 154
REMARK 465 HIS A 155
REMARK 465 HIS A 156
REMARK 465 HIS A 157
REMARK 465 LYS A 158
REMARK 465 LYS A 159
REMARK 465 PRO A 160
REMARK 465 LEU A 161
REMARK 465 LYS A 162
REMARK 465 LYS A 163
REMARK 465 GLY A 164
REMARK 465 ARG A 165
REMARK 465 ALA A 166
REMARK 465 ASN A 167
REMARK 465 LYS A 168
REMARK 465 LYS A 169
REMARK 465 ASN A 170
REMARK 465 ASP A 171
REMARK 465 ARG A 172
REMARK 465 ASP A 173
REMARK 465 SER A 174
REMARK 465 PRO A 175
REMARK 465 THR A 217
REMARK 465 ASN A 218
REMARK 465 SER A 219
REMARK 465 PRO A 220
REMARK 465 GLN A 221
REMARK 465 PRO A 222
REMARK 465 THR A 223
REMARK 465 SER A 224
REMARK 465 LEU A 225
REMARK 465 THR A 226
REMARK 465 SER A 227
REMARK 465 ASP A 228
REMARK 465 ASN A 229
REMARK 465 ASP A 230
REMARK 465 THR A 231
REMARK 465 SER A 232
REMARK 465 SER A 233
REMARK 465 VAL A 234
REMARK 465 ALA A 568
REMARK 465 ARG A 569
REMARK 465 GLY A 570
REMARK 465 ARG A 571
REMARK 465 ARG A 572
REMARK 465 ASN A 573
REMARK 465 GLY A 575
REMARK 465 THR A 576
REMARK 465 PRO A 577
REMARK 465 ARG A 582
REMARK 465 MET B 150
REMARK 465 GLY B 151
REMARK 465 HIS B 152
REMARK 465 HIS B 153
REMARK 465 HIS B 154
REMARK 465 HIS B 155
REMARK 465 HIS B 156
REMARK 465 HIS B 157
REMARK 465 LYS B 158
REMARK 465 LYS B 159
REMARK 465 PRO B 160
REMARK 465 LEU B 161
REMARK 465 LYS B 162
REMARK 465 LYS B 163
REMARK 465 GLY B 164
REMARK 465 ARG B 165
REMARK 465 ALA B 166
REMARK 465 ASN B 167
REMARK 465 LYS B 168
REMARK 465 LYS B 169
REMARK 465 ASN B 170
REMARK 465 ASP B 171
REMARK 465 ARG B 172
REMARK 465 ASP B 173
REMARK 465 SER B 174
REMARK 465 PRO B 175
REMARK 465 SER B 176
REMARK 465 ASN B 218
REMARK 465 SER B 219
REMARK 465 PRO B 220
REMARK 465 GLN B 221
REMARK 465 PRO B 222
REMARK 465 THR B 223
REMARK 465 SER B 224
REMARK 465 LEU B 225
REMARK 465 THR B 226
REMARK 465 SER B 227
REMARK 465 ASP B 228
REMARK 465 ASN B 229
REMARK 465 ASP B 230
REMARK 465 THR B 231
REMARK 465 SER B 232
REMARK 465 SER B 233
REMARK 465 VAL B 234
REMARK 465 ALA B 567
REMARK 465 ALA B 568
REMARK 465 ARG B 569
REMARK 465 GLY B 570
REMARK 465 ARG B 571
REMARK 465 ARG B 572
REMARK 465 ASN B 573
REMARK 465 GLY B 575
REMARK 465 THR B 576
REMARK 465 ARG B 582
REMARK 465 MET C 150
REMARK 465 GLY C 151
REMARK 465 HIS C 152
REMARK 465 HIS C 153
REMARK 465 HIS C 154
REMARK 465 HIS C 155
REMARK 465 HIS C 156
REMARK 465 HIS C 157
REMARK 465 LYS C 158
REMARK 465 LYS C 159
REMARK 465 PRO C 160
REMARK 465 LEU C 161
REMARK 465 LYS C 162
REMARK 465 LYS C 163
REMARK 465 GLY C 164
REMARK 465 ARG C 165
REMARK 465 ALA C 166
REMARK 465 ASN C 167
REMARK 465 LYS C 168
REMARK 465 LYS C 169
REMARK 465 ASN C 170
REMARK 465 ASP C 171
REMARK 465 ARG C 172
REMARK 465 ASP C 173
REMARK 465 SER C 174
REMARK 465 PRO C 175
REMARK 465 ASN C 218
REMARK 465 SER C 219
REMARK 465 PRO C 220
REMARK 465 GLN C 221
REMARK 465 PRO C 222
REMARK 465 THR C 223
REMARK 465 SER C 224
REMARK 465 LEU C 225
REMARK 465 THR C 226
REMARK 465 SER C 227
REMARK 465 ASP C 228
REMARK 465 ASN C 229
REMARK 465 ASP C 230
REMARK 465 THR C 231
REMARK 465 SER C 232
REMARK 465 SER C 233
REMARK 465 VAL C 234
REMARK 465 GLY C 570
REMARK 465 ARG C 571
REMARK 465 ARG C 572
REMARK 465 ASN C 573
REMARK 465 GLY C 575
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 OG SER C 282 OE2 GLU C 286 1.97
REMARK 500 NE ARG C 533 OE2 GLU C 549 2.13
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 PRO B 283 CA PRO B 283 C -0.120
REMARK 500
REMARK 500 REMARK: NULL
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 PRO A 283 C - N - CA ANGL. DEV. = 21.5 DEGREES
REMARK 500 PRO A 283 C - N - CD ANGL. DEV. = -29.8 DEGREES
REMARK 500 PRO B 283 C - N - CD ANGL. DEV. = -19.3 DEGREES
REMARK 500 PHE C 255 CB - CG - CD2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 PHE C 255 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 PRO C 283 C - N - CA ANGL. DEV. = 16.0 DEGREES
REMARK 500 PRO C 283 C - N - CD ANGL. DEV. = -30.1 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 192 80.37 -65.80
REMARK 500 THR A 208 60.35 -119.68
REMARK 500 LYS A 256 -73.83 -83.58
REMARK 500 ARG A 257 89.08 -39.06
REMARK 500 SER A 258 -114.46 51.20
REMARK 500 THR A 259 -134.20 109.07
REMARK 500 ALA A 260 -138.41 67.98
REMARK 500 ILE A 261 -86.97 -17.91
REMARK 500 TYR A 364 123.36 -36.33
REMARK 500 ASN A 518 -133.50 -134.24
REMARK 500 PRO B 192 85.09 -68.48
REMARK 500 LYS B 256 -73.03 -64.97
REMARK 500 ARG B 257 163.20 -45.95
REMARK 500 SER B 258 -81.11 -37.15
REMARK 500 THR B 259 115.44 73.69
REMARK 500 ALA B 260 -8.19 172.65
REMARK 500 TYR B 262 129.01 -173.23
REMARK 500 SER B 512 152.04 -48.25
REMARK 500 PRO C 192 79.48 -66.77
REMARK 500 ARG C 216 -78.96 -100.48
REMARK 500 SER C 353 -33.73 -135.92
REMARK 500 TYR C 364 127.64 -38.81
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 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH C 803
DBREF 1U2Z A 158 582 UNP Q04089 DOT1_YEAST 158 582
DBREF 1U2Z B 158 582 UNP Q04089 DOT1_YEAST 158 582
DBREF 1U2Z C 158 582 UNP Q04089 DOT1_YEAST 158 582
SEQADV 1U2Z MET A 150 UNP Q04089 EXPRESSION TAG
SEQADV 1U2Z GLY A 151 UNP Q04089 EXPRESSION TAG
SEQADV 1U2Z HIS A 152 UNP Q04089 EXPRESSION TAG
SEQADV 1U2Z HIS A 153 UNP Q04089 EXPRESSION TAG
SEQADV 1U2Z HIS A 154 UNP Q04089 EXPRESSION TAG
SEQADV 1U2Z HIS A 155 UNP Q04089 EXPRESSION TAG
SEQADV 1U2Z HIS A 156 UNP Q04089 EXPRESSION TAG
SEQADV 1U2Z HIS A 157 UNP Q04089 EXPRESSION TAG
SEQADV 1U2Z MET B 150 UNP Q04089 EXPRESSION TAG
SEQADV 1U2Z GLY B 151 UNP Q04089 EXPRESSION TAG
SEQADV 1U2Z HIS B 152 UNP Q04089 EXPRESSION TAG
SEQADV 1U2Z HIS B 153 UNP Q04089 EXPRESSION TAG
SEQADV 1U2Z HIS B 154 UNP Q04089 EXPRESSION TAG
SEQADV 1U2Z HIS B 155 UNP Q04089 EXPRESSION TAG
SEQADV 1U2Z HIS B 156 UNP Q04089 EXPRESSION TAG
SEQADV 1U2Z HIS B 157 UNP Q04089 EXPRESSION TAG
SEQADV 1U2Z MET C 150 UNP Q04089 EXPRESSION TAG
SEQADV 1U2Z GLY C 151 UNP Q04089 EXPRESSION TAG
SEQADV 1U2Z HIS C 152 UNP Q04089 EXPRESSION TAG
SEQADV 1U2Z HIS C 153 UNP Q04089 EXPRESSION TAG
SEQADV 1U2Z HIS C 154 UNP Q04089 EXPRESSION TAG
SEQADV 1U2Z HIS C 155 UNP Q04089 EXPRESSION TAG
SEQADV 1U2Z HIS C 156 UNP Q04089 EXPRESSION TAG
SEQADV 1U2Z HIS C 157 UNP Q04089 EXPRESSION TAG
SEQRES 1 A 433 MET GLY HIS HIS HIS HIS HIS HIS LYS LYS PRO LEU LYS
SEQRES 2 A 433 LYS GLY ARG ALA ASN LYS LYS ASN ASP ARG ASP SER PRO
SEQRES 3 A 433 SER SER THR PHE VAL ASP TRP ASN GLY PRO CYS LEU ARG
SEQRES 4 A 433 LEU GLN TYR PRO LEU PHE ASP ILE GLU TYR LEU ARG SER
SEQRES 5 A 433 HIS GLU ILE TYR SER GLY THR PRO ILE GLN SER ILE SER
SEQRES 6 A 433 LEU ARG THR ASN SER PRO GLN PRO THR SER LEU THR SER
SEQRES 7 A 433 ASP ASN ASP THR SER SER VAL THR THR ALA LYS LEU GLN
SEQRES 8 A 433 SER ILE LEU PHE SER ASN TYR MET GLU GLU TYR LYS VAL
SEQRES 9 A 433 ASP PHE LYS ARG SER THR ALA ILE TYR ASN PRO MET SER
SEQRES 10 A 433 GLU ILE GLY LYS LEU ILE GLU TYR SER CYS LEU VAL PHE
SEQRES 11 A 433 LEU PRO SER PRO TYR ALA GLU GLN LEU LYS GLU THR ILE
SEQRES 12 A 433 LEU PRO ASP LEU ASN ALA SER PHE ASP ASN SER ASP THR
SEQRES 13 A 433 LYS GLY PHE VAL ASN ALA ILE ASN LEU TYR ASN LYS MET
SEQRES 14 A 433 ILE ARG GLU ILE PRO ARG GLN ARG ILE ILE ASP HIS LEU
SEQRES 15 A 433 GLU THR ILE ASP LYS ILE PRO ARG SER PHE ILE HIS ASP
SEQRES 16 A 433 PHE LEU HIS ILE VAL TYR THR ARG SER ILE HIS PRO GLN
SEQRES 17 A 433 ALA ASN LYS LEU LYS HIS TYR LYS ALA PHE SER ASN TYR
SEQRES 18 A 433 VAL TYR GLY GLU LEU LEU PRO ASN PHE LEU SER ASP VAL
SEQRES 19 A 433 TYR GLN GLN CYS GLN LEU LYS LYS GLY ASP THR PHE MET
SEQRES 20 A 433 ASP LEU GLY SER GLY VAL GLY ASN CYS VAL VAL GLN ALA
SEQRES 21 A 433 ALA LEU GLU CYS GLY CYS ALA LEU SER PHE GLY CYS GLU
SEQRES 22 A 433 ILE MET ASP ASP ALA SER ASP LEU THR ILE LEU GLN TYR
SEQRES 23 A 433 GLU GLU LEU LYS LYS ARG CYS LYS LEU TYR GLY MET ARG
SEQRES 24 A 433 LEU ASN ASN VAL GLU PHE SER LEU LYS LYS SER PHE VAL
SEQRES 25 A 433 ASP ASN ASN ARG VAL ALA GLU LEU ILE PRO GLN CYS ASP
SEQRES 26 A 433 VAL ILE LEU VAL ASN ASN PHE LEU PHE ASP GLU ASP LEU
SEQRES 27 A 433 ASN LYS LYS VAL GLU LYS ILE LEU GLN THR ALA LYS VAL
SEQRES 28 A 433 GLY CYS LYS ILE ILE SER LEU LYS SER LEU ARG SER LEU
SEQRES 29 A 433 THR TYR GLN ILE ASN PHE TYR ASN VAL GLU ASN ILE PHE
SEQRES 30 A 433 ASN ARG LEU LYS VAL GLN ARG TYR ASP LEU LYS GLU ASP
SEQRES 31 A 433 SER VAL SER TRP THR HIS SER GLY GLY GLU TYR TYR ILE
SEQRES 32 A 433 SER THR VAL MET GLU ASP VAL ASP GLU SER LEU PHE SER
SEQRES 33 A 433 PRO ALA ALA ARG GLY ARG ARG ASN ARG GLY THR PRO VAL
SEQRES 34 A 433 LYS TYR THR ARG
SEQRES 1 B 433 MET GLY HIS HIS HIS HIS HIS HIS LYS LYS PRO LEU LYS
SEQRES 2 B 433 LYS GLY ARG ALA ASN LYS LYS ASN ASP ARG ASP SER PRO
SEQRES 3 B 433 SER SER THR PHE VAL ASP TRP ASN GLY PRO CYS LEU ARG
SEQRES 4 B 433 LEU GLN TYR PRO LEU PHE ASP ILE GLU TYR LEU ARG SER
SEQRES 5 B 433 HIS GLU ILE TYR SER GLY THR PRO ILE GLN SER ILE SER
SEQRES 6 B 433 LEU ARG THR ASN SER PRO GLN PRO THR SER LEU THR SER
SEQRES 7 B 433 ASP ASN ASP THR SER SER VAL THR THR ALA LYS LEU GLN
SEQRES 8 B 433 SER ILE LEU PHE SER ASN TYR MET GLU GLU TYR LYS VAL
SEQRES 9 B 433 ASP PHE LYS ARG SER THR ALA ILE TYR ASN PRO MET SER
SEQRES 10 B 433 GLU ILE GLY LYS LEU ILE GLU TYR SER CYS LEU VAL PHE
SEQRES 11 B 433 LEU PRO SER PRO TYR ALA GLU GLN LEU LYS GLU THR ILE
SEQRES 12 B 433 LEU PRO ASP LEU ASN ALA SER PHE ASP ASN SER ASP THR
SEQRES 13 B 433 LYS GLY PHE VAL ASN ALA ILE ASN LEU TYR ASN LYS MET
SEQRES 14 B 433 ILE ARG GLU ILE PRO ARG GLN ARG ILE ILE ASP HIS LEU
SEQRES 15 B 433 GLU THR ILE ASP LYS ILE PRO ARG SER PHE ILE HIS ASP
SEQRES 16 B 433 PHE LEU HIS ILE VAL TYR THR ARG SER ILE HIS PRO GLN
SEQRES 17 B 433 ALA ASN LYS LEU LYS HIS TYR LYS ALA PHE SER ASN TYR
SEQRES 18 B 433 VAL TYR GLY GLU LEU LEU PRO ASN PHE LEU SER ASP VAL
SEQRES 19 B 433 TYR GLN GLN CYS GLN LEU LYS LYS GLY ASP THR PHE MET
SEQRES 20 B 433 ASP LEU GLY SER GLY VAL GLY ASN CYS VAL VAL GLN ALA
SEQRES 21 B 433 ALA LEU GLU CYS GLY CYS ALA LEU SER PHE GLY CYS GLU
SEQRES 22 B 433 ILE MET ASP ASP ALA SER ASP LEU THR ILE LEU GLN TYR
SEQRES 23 B 433 GLU GLU LEU LYS LYS ARG CYS LYS LEU TYR GLY MET ARG
SEQRES 24 B 433 LEU ASN ASN VAL GLU PHE SER LEU LYS LYS SER PHE VAL
SEQRES 25 B 433 ASP ASN ASN ARG VAL ALA GLU LEU ILE PRO GLN CYS ASP
SEQRES 26 B 433 VAL ILE LEU VAL ASN ASN PHE LEU PHE ASP GLU ASP LEU
SEQRES 27 B 433 ASN LYS LYS VAL GLU LYS ILE LEU GLN THR ALA LYS VAL
SEQRES 28 B 433 GLY CYS LYS ILE ILE SER LEU LYS SER LEU ARG SER LEU
SEQRES 29 B 433 THR TYR GLN ILE ASN PHE TYR ASN VAL GLU ASN ILE PHE
SEQRES 30 B 433 ASN ARG LEU LYS VAL GLN ARG TYR ASP LEU LYS GLU ASP
SEQRES 31 B 433 SER VAL SER TRP THR HIS SER GLY GLY GLU TYR TYR ILE
SEQRES 32 B 433 SER THR VAL MET GLU ASP VAL ASP GLU SER LEU PHE SER
SEQRES 33 B 433 PRO ALA ALA ARG GLY ARG ARG ASN ARG GLY THR PRO VAL
SEQRES 34 B 433 LYS TYR THR ARG
SEQRES 1 C 433 MET GLY HIS HIS HIS HIS HIS HIS LYS LYS PRO LEU LYS
SEQRES 2 C 433 LYS GLY ARG ALA ASN LYS LYS ASN ASP ARG ASP SER PRO
SEQRES 3 C 433 SER SER THR PHE VAL ASP TRP ASN GLY PRO CYS LEU ARG
SEQRES 4 C 433 LEU GLN TYR PRO LEU PHE ASP ILE GLU TYR LEU ARG SER
SEQRES 5 C 433 HIS GLU ILE TYR SER GLY THR PRO ILE GLN SER ILE SER
SEQRES 6 C 433 LEU ARG THR ASN SER PRO GLN PRO THR SER LEU THR SER
SEQRES 7 C 433 ASP ASN ASP THR SER SER VAL THR THR ALA LYS LEU GLN
SEQRES 8 C 433 SER ILE LEU PHE SER ASN TYR MET GLU GLU TYR LYS VAL
SEQRES 9 C 433 ASP PHE LYS ARG SER THR ALA ILE TYR ASN PRO MET SER
SEQRES 10 C 433 GLU ILE GLY LYS LEU ILE GLU TYR SER CYS LEU VAL PHE
SEQRES 11 C 433 LEU PRO SER PRO TYR ALA GLU GLN LEU LYS GLU THR ILE
SEQRES 12 C 433 LEU PRO ASP LEU ASN ALA SER PHE ASP ASN SER ASP THR
SEQRES 13 C 433 LYS GLY PHE VAL ASN ALA ILE ASN LEU TYR ASN LYS MET
SEQRES 14 C 433 ILE ARG GLU ILE PRO ARG GLN ARG ILE ILE ASP HIS LEU
SEQRES 15 C 433 GLU THR ILE ASP LYS ILE PRO ARG SER PHE ILE HIS ASP
SEQRES 16 C 433 PHE LEU HIS ILE VAL TYR THR ARG SER ILE HIS PRO GLN
SEQRES 17 C 433 ALA ASN LYS LEU LYS HIS TYR LYS ALA PHE SER ASN TYR
SEQRES 18 C 433 VAL TYR GLY GLU LEU LEU PRO ASN PHE LEU SER ASP VAL
SEQRES 19 C 433 TYR GLN GLN CYS GLN LEU LYS LYS GLY ASP THR PHE MET
SEQRES 20 C 433 ASP LEU GLY SER GLY VAL GLY ASN CYS VAL VAL GLN ALA
SEQRES 21 C 433 ALA LEU GLU CYS GLY CYS ALA LEU SER PHE GLY CYS GLU
SEQRES 22 C 433 ILE MET ASP ASP ALA SER ASP LEU THR ILE LEU GLN TYR
SEQRES 23 C 433 GLU GLU LEU LYS LYS ARG CYS LYS LEU TYR GLY MET ARG
SEQRES 24 C 433 LEU ASN ASN VAL GLU PHE SER LEU LYS LYS SER PHE VAL
SEQRES 25 C 433 ASP ASN ASN ARG VAL ALA GLU LEU ILE PRO GLN CYS ASP
SEQRES 26 C 433 VAL ILE LEU VAL ASN ASN PHE LEU PHE ASP GLU ASP LEU
SEQRES 27 C 433 ASN LYS LYS VAL GLU LYS ILE LEU GLN THR ALA LYS VAL
SEQRES 28 C 433 GLY CYS LYS ILE ILE SER LEU LYS SER LEU ARG SER LEU
SEQRES 29 C 433 THR TYR GLN ILE ASN PHE TYR ASN VAL GLU ASN ILE PHE
SEQRES 30 C 433 ASN ARG LEU LYS VAL GLN ARG TYR ASP LEU LYS GLU ASP
SEQRES 31 C 433 SER VAL SER TRP THR HIS SER GLY GLY GLU TYR TYR ILE
SEQRES 32 C 433 SER THR VAL MET GLU ASP VAL ASP GLU SER LEU PHE SER
SEQRES 33 C 433 PRO ALA ALA ARG GLY ARG ARG ASN ARG GLY THR PRO VAL
SEQRES 34 C 433 LYS TYR THR ARG
HET SAH A 801 26
HET SAH B 802 26
HET SAH C 803 26
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
FORMUL 4 SAH 3(C14 H20 N6 O5 S)
FORMUL 7 HOH *533(H2 O)
HELIX 1 1 ASP A 195 HIS A 202 1 8
HELIX 2 2 GLN A 211 LEU A 215 5 5
HELIX 3 3 ASN A 263 VAL A 278 1 16
HELIX 4 4 PRO A 283 ILE A 292 1 10
HELIX 5 5 ILE A 292 ASN A 302 1 11
HELIX 6 6 ASP A 304 ARG A 320 1 17
HELIX 7 7 PRO A 323 GLU A 332 1 10
HELIX 8 8 ARG A 339 ILE A 354 1 16
HELIX 9 9 HIS A 355 LYS A 362 5 8
HELIX 10 10 PHE A 367 VAL A 371 5 5
HELIX 11 11 LEU A 376 CYS A 387 1 12
HELIX 12 12 GLY A 403 GLY A 414 1 12
HELIX 13 13 MET A 424 TYR A 445 1 22
HELIX 14 14 ASN A 463 ILE A 470 1 8
HELIX 15 15 PRO A 471 CYS A 473 5 3
HELIX 16 16 ASP A 484 GLN A 496 1 13
HELIX 17 17 ASN A 524 ASN A 527 5 4
HELIX 18 18 ASP A 560 PHE A 564 5 5
HELIX 19 19 ASP B 195 HIS B 202 1 8
HELIX 20 20 GLN B 211 LEU B 215 5 5
HELIX 21 21 ASN B 263 VAL B 278 1 16
HELIX 22 22 PRO B 283 ASN B 302 1 20
HELIX 23 23 ASP B 304 GLU B 321 1 18
HELIX 24 24 PRO B 323 GLU B 332 1 10
HELIX 25 25 ARG B 339 ILE B 354 1 16
HELIX 26 26 HIS B 355 HIS B 363 5 9
HELIX 27 27 PHE B 367 VAL B 371 5 5
HELIX 28 28 LEU B 376 CYS B 387 1 12
HELIX 29 29 GLY B 403 GLY B 414 1 12
HELIX 30 30 MET B 424 TYR B 445 1 22
HELIX 31 31 ASN B 463 ILE B 470 1 8
HELIX 32 32 PRO B 471 CYS B 473 5 3
HELIX 33 33 ASP B 484 GLN B 496 1 13
HELIX 34 34 ASN B 518 VAL B 522 5 5
HELIX 35 35 ASN B 524 ASN B 527 5 4
HELIX 36 36 ASP B 560 PHE B 564 5 5
HELIX 37 37 ASP C 195 HIS C 202 1 8
HELIX 38 38 GLN C 211 LEU C 215 5 5
HELIX 39 39 ASN C 263 VAL C 278 1 16
HELIX 40 40 PRO C 283 ASN C 302 1 20
HELIX 41 41 ASP C 304 ARG C 320 1 17
HELIX 42 42 PRO C 323 GLU C 332 1 10
HELIX 43 43 ARG C 339 ILE C 354 1 16
HELIX 44 44 HIS C 355 LYS C 362 5 8
HELIX 45 45 PHE C 367 VAL C 371 5 5
HELIX 46 46 LEU C 376 CYS C 387 1 12
HELIX 47 47 GLY C 403 GLY C 414 1 12
HELIX 48 48 MET C 424 TYR C 445 1 22
HELIX 49 49 ASN C 463 ILE C 470 1 8
HELIX 50 50 PRO C 471 CYS C 473 5 3
HELIX 51 51 ASP C 484 GLN C 496 1 13
HELIX 52 52 ASN C 524 ASN C 527 5 4
HELIX 53 53 ASP C 560 SER C 565 5 6
SHEET 1 A 2 CYS A 186 ARG A 188 0
SHEET 2 A 2 LYS A 336 PRO A 338 -1 O ILE A 337 N LEU A 187
SHEET 1 B 2 THR A 236 GLN A 240 0
SHEET 2 B 2 MET A 248 LYS A 252 -1 O TYR A 251 N ALA A 237
SHEET 1 C 7 VAL A 452 LEU A 456 0
SHEET 2 C 7 LEU A 417 GLU A 422 1 N SER A 418 O GLU A 453
SHEET 3 C 7 THR A 394 LEU A 398 1 N PHE A 395 O PHE A 419
SHEET 4 C 7 VAL A 475 VAL A 478 1 O LEU A 477 N MET A 396
SHEET 5 C 7 LYS A 503 SER A 506 1 O ILE A 505 N ILE A 476
SHEET 6 C 7 GLU A 549 VAL A 555 -1 O TYR A 551 N SER A 506
SHEET 7 C 7 LEU A 529 ASP A 535 -1 N LYS A 530 O THR A 554
SHEET 1 D 2 CYS B 186 ARG B 188 0
SHEET 2 D 2 LYS B 336 PRO B 338 -1 O ILE B 337 N LEU B 187
SHEET 1 E 2 THR B 236 GLN B 240 0
SHEET 2 E 2 MET B 248 LYS B 252 -1 O TYR B 251 N ALA B 237
SHEET 1 F 7 VAL B 452 LEU B 456 0
SHEET 2 F 7 LEU B 417 GLU B 422 1 N SER B 418 O GLU B 453
SHEET 3 F 7 THR B 394 LEU B 398 1 N PHE B 395 O PHE B 419
SHEET 4 F 7 VAL B 475 VAL B 478 1 O LEU B 477 N MET B 396
SHEET 5 F 7 LYS B 503 SER B 506 1 O ILE B 505 N ILE B 476
SHEET 6 F 7 GLU B 549 VAL B 555 -1 O TYR B 551 N SER B 506
SHEET 7 F 7 LEU B 529 ASP B 535 -1 N LYS B 530 O THR B 554
SHEET 1 G 2 CYS C 186 ARG C 188 0
SHEET 2 G 2 LYS C 336 PRO C 338 -1 O ILE C 337 N LEU C 187
SHEET 1 H 2 THR C 236 GLN C 240 0
SHEET 2 H 2 MET C 248 LYS C 252 -1 O TYR C 251 N ALA C 237
SHEET 1 I 7 VAL C 452 LEU C 456 0
SHEET 2 I 7 LEU C 417 GLU C 422 1 N SER C 418 O GLU C 453
SHEET 3 I 7 THR C 394 LEU C 398 1 N PHE C 395 O PHE C 419
SHEET 4 I 7 VAL C 475 VAL C 478 1 O LEU C 477 N MET C 396
SHEET 5 I 7 LYS C 503 SER C 506 1 O ILE C 505 N ILE C 476
SHEET 6 I 7 GLU C 549 VAL C 555 -1 O TYR C 551 N SER C 506
SHEET 7 I 7 LEU C 529 ASP C 535 -1 N LYS C 530 O THR C 554
CISPEP 1 SER A 282 PRO A 283 0 13.49
CISPEP 2 SER B 282 PRO B 283 0 -9.55
CISPEP 3 SER C 282 PRO C 283 0 8.18
SITE 1 AC1 19 ASN A 369 TYR A 370 GLY A 373 LEU A 375
SITE 2 AC1 19 ASP A 397 GLY A 399 CYS A 405 GLU A 422
SITE 3 AC1 19 ILE A 423 MET A 424 SER A 459 PHE A 460
SITE 4 AC1 19 ASN A 479 HOH A 802 HOH A 814 HOH A 867
SITE 5 AC1 19 HOH A 874 HOH A 916 GLU C 197
SITE 1 AC2 18 ASN B 369 TYR B 370 GLY B 373 LEU B 375
SITE 2 AC2 18 ASP B 397 GLY B 399 CYS B 405 GLU B 422
SITE 3 AC2 18 ILE B 423 MET B 424 SER B 459 PHE B 460
SITE 4 AC2 18 ASN B 479 HOH B 805 HOH B 806 HOH B 810
SITE 5 AC2 18 HOH B 811 HOH B 812
SITE 1 AC3 19 ASN C 369 TYR C 370 GLY C 373 LEU C 375
SITE 2 AC3 19 ASP C 397 GLY C 399 CYS C 405 GLU C 422
SITE 3 AC3 19 ILE C 423 MET C 424 SER C 459 PHE C 460
SITE 4 AC3 19 ASN C 479 LEU C 487 HOH C 805 HOH C 825
SITE 5 AC3 19 HOH C 830 HOH C 858 HOH C 878
CRYST1 73.070 146.275 75.412 90.00 97.68 90.00 P 1 21 1 6
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 0.013686 0.000000 0.001845 0.00000
SCALE2 0.000000 0.006836 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013381 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
