HEADER TRANSFERASE/TRANSFERASE REGULATOR 29-JUL-07 2QRV
TITLE STRUCTURE OF DNMT3A-DNMT3L C-TERMINAL DOMAIN COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (CYTOSINE-5)-METHYLTRANSFERASE 3A;
COMPND 3 CHAIN: A, D, E, H;
COMPND 4 FRAGMENT: RESIDUES 623 TO 908;
COMPND 5 SYNONYM: DNMT3A, DNA METHYLTRANSFERASE HSAIIIA, DNA MTASE HSAIIIA,
COMPND 6 M.HSAIIIA;
COMPND 7 EC: 2.1.1.37;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: DNA (CYTOSINE-5)-METHYLTRANSFERASE 3-LIKE;
COMPND 11 CHAIN: B, C, F, G;
COMPND 12 FRAGMENT: RESIDUES 160 TO 386;
COMPND 13 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: DNMT3A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PXC528;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: DNMT3L;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PXC510
KEYWDS DNA METHYLTRANSFERASE 3A (DNMT3A) AND ITS REGULATORY FACTOR, DNA
KEYWDS 2 METHYLTRANSFERASE 3-LIKE PROTEIN (DNMT3L), NUCLEUS, S-ADENOSYL-L-
KEYWDS 3 METHIONINE, TRANSFERASE-TRANSFERASE REGULATOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.JIA,X.CHENG
REVDAT 3 30-AUG-23 2QRV 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2QRV 1 VERSN
REVDAT 1 04-DEC-07 2QRV 0
JRNL AUTH D.JIA,R.Z.JURKOWSKA,X.ZHANG,A.JELTSCH,X.CHENG
JRNL TITL STRUCTURE OF DNMT3A BOUND TO DNMT3L SUGGESTS A MODEL FOR DE
JRNL TITL 2 NOVO DNA METHYLATION.
JRNL REF NATURE V. 449 248 2007
JRNL REFN ISSN 0028-0836
JRNL PMID 17713477
JRNL DOI 10.1038/NATURE06146
REMARK 2
REMARK 2 RESOLUTION. 2.89 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) : 2.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 332407.340
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 81.9
REMARK 3 NUMBER OF REFLECTIONS : 54424
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) : 0.259
REMARK 3 FREE R VALUE : 0.281
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2756
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.89
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.99
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 38.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2410
REMARK 3 BIN R VALUE (WORKING SET) : 0.4670
REMARK 3 BIN FREE R VALUE : 0.4600
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 121
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.042
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 14553
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 104
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 85.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 101.3
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 9.92000
REMARK 3 B22 (A**2) : 9.92000
REMARK 3 B33 (A**2) : -19.84000
REMARK 3 B12 (A**2) : 24.85000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.49
REMARK 3 ESD FROM SIGMAA (A) : 0.58
REMARK 3 LOW RESOLUTION CUTOFF (A) : 40.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.55
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.64
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.50
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) : 4.840 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 7.650 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 6.400 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 9.070 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.28
REMARK 3 BSOL : 36.80
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 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : SAH.PAR
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 : DNA-RNA_REP.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : SAH.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE NON-CRYSTALLOGRAPHIC SYMMETRY WAS
REMARK 3 USED AS RESTRAINS IN THE CNS REFINEMENT, AND WAS RELEASED FOR
REMARK 3 THE SIDE CHAINS AT THE LATER CYCLES TO ACCOUNT FOR DIFFERENT
REMARK 3 INTERACTION ENVIRONMENTS OF CRYSTAL PACKING WITH EACH MOLECULE.
REMARK 3 THE GROUP B-FACTOR FOR EACH RESIDUE WAS REFINED AT THE EARLIER
REMARK 3 STAGE OF REFINEMENT AND THE INDIVIDUAL B-FACTOR FOR EACH ATOM
REMARK 3 WAS REFINED AT THE LATER CYCLES.
REMARK 4
REMARK 4 2QRV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-AUG-07.
REMARK 100 THE DEPOSITION ID IS D_1000043976.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-APR-06; NULL
REMARK 200 TEMPERATURE (KELVIN) : 173.0; 173.0
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; NULL
REMARK 200 RADIATION SOURCE : APS; NULL
REMARK 200 BEAMLINE : 22-ID; NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0, 0.9792, 0.9785,0.9719; NULL
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; NULL
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD; NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65264
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.890
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.99
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.48800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: 2PV0
REMARK 200
REMARK 200 REMARK: THERE ARE TWO TETRAMER COMPLEXES PER ASYMMETRIC UNIT.
REMARK 200 TETRAMER FORMED BY CHAINS A,B,C,D IS MORE STABLE THAN THE
REMARK 200 TETRAMER FORMED BY CHAINS E,F,G,H. WITHIN EACH TETRAMER, THE
REMARK 200 DNMT3L MOLECULES HAVE HIGHER B-FACTOR THAN THAT OF DNMT3A,
REMARK 200 INDICATING DNMT3L MOLECULES - LOCATED IN THE OUTER SURFACES OF
REMARK 200 TETRAMER - ARE MORE MOBILE.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: THE FINAL PROTEIN SOLUTION CONTAINED
REMARK 280 ~100 TO 133 MICRO M COMPLEX IN 20 MILLI M TRIS/HCL, PH 8.0, 100
REMARK 280 MILLI M NACL, 5 % GLYCEROL, AND 0.1 % MERCAPTOETHANOL. CRYSTALS
REMARK 280 WERE OBTAINED WITH THE MOTHER LIQUOR CONTAINING 2~5 % PEG 3000,
REMARK 280 100 MM TRIS/HCL, PH 8.0, 5 % GLYCEROL AT 16C, VAPOR DIFFUSION,
REMARK 280 HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 200.94050
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 116.01305
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 16.56300
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 200.94050
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 116.01305
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 16.56300
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 200.94050
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 116.01305
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 16.56300
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 232.02610
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 33.12600
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 232.02610
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 33.12600
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 232.02610
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 33.12600
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300 REMARK: THERE WERE TWO TETRAMER COMPLEXES PER CRYSTALLOGRAPHIC
REMARK 300 ASYMMETRIC UNIT. EACH TETRAMER CONTAINS TWO PAIRS OF DNMT3A-3L
REMARK 300 HETERO-DIMERS (3L-3A-3A-3L) WITH TWO 3L-3A INTERFACES AND ONE 3A-3A
REMARK 300 INTERFACE.
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 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
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 614
REMARK 465 GLY A 615
REMARK 465 HIS A 616
REMARK 465 HIS A 617
REMARK 465 HIS A 618
REMARK 465 HIS A 619
REMARK 465 HIS A 620
REMARK 465 HIS A 621
REMARK 465 MET A 622
REMARK 465 THR A 828
REMARK 465 ILE A 829
REMARK 465 THR A 830
REMARK 465 THR A 831
REMARK 465 ARG A 832
REMARK 465 SER A 833
REMARK 465 ASN A 834
REMARK 465 SER A 835
REMARK 465 ILE A 836
REMARK 465 LYS A 837
REMARK 465 GLN A 838
REMARK 465 GLY A 839
REMARK 465 LYS A 840
REMARK 465 ASP A 841
REMARK 465 GLY B 157
REMARK 465 SER B 158
REMARK 465 MET B 159
REMARK 465 TRP B 160
REMARK 465 ARG B 161
REMARK 465 SER B 162
REMARK 465 GLN B 163
REMARK 465 LEU B 164
REMARK 465 LYS B 165
REMARK 465 ALA B 166
REMARK 465 PHE B 167
REMARK 465 TYR B 168
REMARK 465 ASP B 169
REMARK 465 ARG B 170
REMARK 465 GLU B 171
REMARK 465 SER B 172
REMARK 465 GLU B 173
REMARK 465 ASN B 174
REMARK 465 PRO B 175
REMARK 465 LEU B 176
REMARK 465 GLU B 177
REMARK 465 SER B 211
REMARK 465 GLY B 212
REMARK 465 SER B 213
REMARK 465 ASP B 214
REMARK 465 PRO B 215
REMARK 465 LEU B 317
REMARK 465 GLN B 318
REMARK 465 ASN B 319
REMARK 465 ALA B 320
REMARK 465 LYS B 354
REMARK 465 LEU B 355
REMARK 465 ALA B 356
REMARK 465 ALA B 357
REMARK 465 LYS B 358
REMARK 465 TRP B 359
REMARK 465 PRO B 360
REMARK 465 THR B 380
REMARK 465 GLU B 381
REMARK 465 LEU B 382
REMARK 465 THR B 383
REMARK 465 SER B 384
REMARK 465 SER B 385
REMARK 465 LEU B 386
REMARK 465 GLY C 157
REMARK 465 SER C 158
REMARK 465 MET C 159
REMARK 465 TRP C 160
REMARK 465 ARG C 161
REMARK 465 SER C 162
REMARK 465 GLN C 163
REMARK 465 LEU C 164
REMARK 465 LYS C 165
REMARK 465 ALA C 166
REMARK 465 PHE C 167
REMARK 465 TYR C 168
REMARK 465 ASP C 169
REMARK 465 ARG C 170
REMARK 465 GLU C 171
REMARK 465 SER C 172
REMARK 465 GLU C 173
REMARK 465 ASN C 174
REMARK 465 PRO C 175
REMARK 465 LEU C 176
REMARK 465 GLU C 177
REMARK 465 SER C 211
REMARK 465 GLY C 212
REMARK 465 SER C 213
REMARK 465 ASP C 214
REMARK 465 PRO C 215
REMARK 465 LEU C 317
REMARK 465 GLN C 318
REMARK 465 ASN C 319
REMARK 465 ALA C 320
REMARK 465 LYS C 354
REMARK 465 LEU C 355
REMARK 465 ALA C 356
REMARK 465 ALA C 357
REMARK 465 LYS C 358
REMARK 465 TRP C 359
REMARK 465 PRO C 360
REMARK 465 THR C 380
REMARK 465 GLU C 381
REMARK 465 LEU C 382
REMARK 465 THR C 383
REMARK 465 SER C 384
REMARK 465 SER C 385
REMARK 465 LEU C 386
REMARK 465 MET D 614
REMARK 465 GLY D 615
REMARK 465 HIS D 616
REMARK 465 HIS D 617
REMARK 465 HIS D 618
REMARK 465 HIS D 619
REMARK 465 HIS D 620
REMARK 465 HIS D 621
REMARK 465 MET D 622
REMARK 465 PRO D 623
REMARK 465 ALA D 624
REMARK 465 GLU D 625
REMARK 465 THR D 828
REMARK 465 ILE D 829
REMARK 465 THR D 830
REMARK 465 THR D 831
REMARK 465 ARG D 832
REMARK 465 SER D 833
REMARK 465 ASN D 834
REMARK 465 SER D 835
REMARK 465 ILE D 836
REMARK 465 LYS D 837
REMARK 465 GLN D 838
REMARK 465 GLY D 839
REMARK 465 LYS D 840
REMARK 465 ASP D 841
REMARK 465 GLN D 842
REMARK 465 HIS D 843
REMARK 465 MET E 614
REMARK 465 GLY E 615
REMARK 465 HIS E 616
REMARK 465 HIS E 617
REMARK 465 HIS E 618
REMARK 465 HIS E 619
REMARK 465 HIS E 620
REMARK 465 HIS E 621
REMARK 465 MET E 622
REMARK 465 THR E 828
REMARK 465 ILE E 829
REMARK 465 THR E 830
REMARK 465 THR E 831
REMARK 465 ARG E 832
REMARK 465 SER E 833
REMARK 465 ASN E 834
REMARK 465 SER E 835
REMARK 465 ILE E 836
REMARK 465 LYS E 837
REMARK 465 GLN E 838
REMARK 465 GLY E 839
REMARK 465 LYS E 840
REMARK 465 ASP E 841
REMARK 465 GLN E 842
REMARK 465 HIS E 843
REMARK 465 GLY F 157
REMARK 465 SER F 158
REMARK 465 MET F 159
REMARK 465 TRP F 160
REMARK 465 ARG F 161
REMARK 465 SER F 162
REMARK 465 GLN F 163
REMARK 465 LEU F 164
REMARK 465 LYS F 165
REMARK 465 ALA F 166
REMARK 465 PHE F 167
REMARK 465 TYR F 168
REMARK 465 ASP F 169
REMARK 465 ARG F 170
REMARK 465 GLU F 171
REMARK 465 SER F 172
REMARK 465 GLU F 173
REMARK 465 ASN F 174
REMARK 465 PRO F 175
REMARK 465 LEU F 176
REMARK 465 GLU F 177
REMARK 465 SER F 211
REMARK 465 GLY F 212
REMARK 465 SER F 213
REMARK 465 ASP F 214
REMARK 465 PRO F 215
REMARK 465 LEU F 317
REMARK 465 GLN F 318
REMARK 465 ASN F 319
REMARK 465 ALA F 320
REMARK 465 LYS F 354
REMARK 465 LEU F 355
REMARK 465 ALA F 356
REMARK 465 ALA F 357
REMARK 465 LYS F 358
REMARK 465 TRP F 359
REMARK 465 PRO F 360
REMARK 465 THR F 380
REMARK 465 GLU F 381
REMARK 465 LEU F 382
REMARK 465 THR F 383
REMARK 465 SER F 384
REMARK 465 SER F 385
REMARK 465 LEU F 386
REMARK 465 GLY G 157
REMARK 465 SER G 158
REMARK 465 MET G 159
REMARK 465 TRP G 160
REMARK 465 ARG G 161
REMARK 465 SER G 162
REMARK 465 GLN G 163
REMARK 465 LEU G 164
REMARK 465 LYS G 165
REMARK 465 ALA G 166
REMARK 465 PHE G 167
REMARK 465 TYR G 168
REMARK 465 ASP G 169
REMARK 465 ARG G 170
REMARK 465 GLU G 171
REMARK 465 SER G 172
REMARK 465 GLU G 173
REMARK 465 ASN G 174
REMARK 465 PRO G 175
REMARK 465 LEU G 176
REMARK 465 GLU G 177
REMARK 465 SER G 211
REMARK 465 GLY G 212
REMARK 465 SER G 213
REMARK 465 ASP G 214
REMARK 465 PRO G 215
REMARK 465 LEU G 317
REMARK 465 GLN G 318
REMARK 465 ASN G 319
REMARK 465 ALA G 320
REMARK 465 LYS G 354
REMARK 465 LEU G 355
REMARK 465 ALA G 356
REMARK 465 ALA G 357
REMARK 465 LYS G 358
REMARK 465 TRP G 359
REMARK 465 PRO G 360
REMARK 465 THR G 380
REMARK 465 GLU G 381
REMARK 465 LEU G 382
REMARK 465 THR G 383
REMARK 465 SER G 384
REMARK 465 SER G 385
REMARK 465 LEU G 386
REMARK 465 MET H 614
REMARK 465 GLY H 615
REMARK 465 HIS H 616
REMARK 465 HIS H 617
REMARK 465 HIS H 618
REMARK 465 HIS H 619
REMARK 465 HIS H 620
REMARK 465 HIS H 621
REMARK 465 MET H 622
REMARK 465 PRO H 623
REMARK 465 ALA H 624
REMARK 465 GLU H 625
REMARK 465 THR H 828
REMARK 465 ILE H 829
REMARK 465 THR H 830
REMARK 465 THR H 831
REMARK 465 ARG H 832
REMARK 465 SER H 833
REMARK 465 ASN H 834
REMARK 465 SER H 835
REMARK 465 ILE H 836
REMARK 465 LYS H 837
REMARK 465 GLN H 838
REMARK 465 GLY H 839
REMARK 465 LYS H 840
REMARK 465 ASP H 841
REMARK 465 GLN H 842
REMARK 465 HIS H 843
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 GLU A 625 CG CD OE1 OE2
REMARK 470 LYS A 626 CG CD CE NZ
REMARK 470 LYS A 628 CG CD CE NZ
REMARK 470 LYS A 689 CG CD CE NZ
REMARK 470 ASN A 713 CG OD1 ND2
REMARK 470 LYS A 762 CG CD CE NZ
REMARK 470 ARG A 767 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 779 CG CD CE NZ
REMARK 470 GLU A 813 CG CD OE1 OE2
REMARK 470 ILE A 820 CG1 CG2 CD1
REMARK 470 ARG A 827 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 842 CG CD OE1 NE2
REMARK 470 PHE A 847 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL A 908 CG1 CG2
REMARK 470 HIS B 250 CG ND1 CD2 CE1 NE2
REMARK 470 THR B 251 OG1 CG2
REMARK 470 CYS B 252 SG
REMARK 470 ASP B 253 CG OD1 OD2
REMARK 470 ARG B 254 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 278 CB CG CD NE CZ NH1 NH2
REMARK 470 HIS C 250 CG ND1 CD2 CE1 NE2
REMARK 470 THR C 251 OG1 CG2
REMARK 470 CYS C 252 SG
REMARK 470 ASP C 253 CG OD1 OD2
REMARK 470 ARG C 254 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 278 CB CG CD NE CZ NH1 NH2
REMARK 470 LYS D 626 CG CD CE NZ
REMARK 470 LYS D 628 CG CD CE NZ
REMARK 470 LYS D 689 CG CD CE NZ
REMARK 470 ASN D 713 CG OD1 ND2
REMARK 470 LYS D 762 CG CD CE NZ
REMARK 470 ARG D 767 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 779 CG CD CE NZ
REMARK 470 GLU D 813 CG CD OE1 OE2
REMARK 470 ILE D 820 CG1 CG2 CD1
REMARK 470 ARG D 827 CG CD NE CZ NH1 NH2
REMARK 470 PHE D 847 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL D 908 CG1 CG2
REMARK 470 GLU E 625 CG CD OE1 OE2
REMARK 470 LYS E 626 CG CD CE NZ
REMARK 470 LYS E 628 CG CD CE NZ
REMARK 470 LYS E 689 CG CD CE NZ
REMARK 470 ASN E 713 CG OD1 ND2
REMARK 470 LYS E 762 CG CD CE NZ
REMARK 470 ARG E 767 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 779 CG CD CE NZ
REMARK 470 GLU E 813 CG CD OE1 OE2
REMARK 470 ILE E 820 CG1 CG2 CD1
REMARK 470 ARG E 827 CG CD NE CZ NH1 NH2
REMARK 470 PHE E 847 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL E 908 CG1 CG2
REMARK 470 HIS F 250 CG ND1 CD2 CE1 NE2
REMARK 470 THR F 251 OG1 CG2
REMARK 470 CYS F 252 SG
REMARK 470 ASP F 253 CG OD1 OD2
REMARK 470 ARG F 254 CG CD NE CZ NH1 NH2
REMARK 470 ARG F 278 CB CG CD NE CZ NH1 NH2
REMARK 470 HIS G 250 CG ND1 CD2 CE1 NE2
REMARK 470 THR G 251 OG1 CG2
REMARK 470 CYS G 252 SG
REMARK 470 ASP G 253 CG OD1 OD2
REMARK 470 ARG G 254 CG CD NE CZ NH1 NH2
REMARK 470 ARG G 278 CB CG CD NE CZ NH1 NH2
REMARK 470 LYS H 626 CG CD CE NZ
REMARK 470 LYS H 628 CG CD CE NZ
REMARK 470 LYS H 689 CG CD CE NZ
REMARK 470 ASN H 713 CG OD1 ND2
REMARK 470 LYS H 762 CG CD CE NZ
REMARK 470 ARG H 767 CG CD NE CZ NH1 NH2
REMARK 470 LYS H 779 CG CD CE NZ
REMARK 470 GLU H 813 CG CD OE1 OE2
REMARK 470 ILE H 820 CG1 CG2 CD1
REMARK 470 ARG H 827 CG CD NE CZ NH1 NH2
REMARK 470 PHE H 847 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL H 908 CG1 CG2
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 O VAL A 686 NH2 ARG A 732 2.07
REMARK 500 OE1 GLU E 861 N HIS E 869 2.18
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 LEU A 644 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
REMARK 500 PRO A 845 C - N - CA ANGL. DEV. = 19.2 DEGREES
REMARK 500 PRO A 845 C - N - CD ANGL. DEV. = -37.4 DEGREES
REMARK 500 PRO D 845 C - N - CA ANGL. DEV. = 11.4 DEGREES
REMARK 500 ASN D 875 N - CA - C ANGL. DEV. = -17.5 DEGREES
REMARK 500 PRO E 800 C - N - CA ANGL. DEV. = 10.8 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 ALA A 624 118.46 172.52
REMARK 500 LYS A 676 -38.59 -27.94
REMARK 500 ARG A 684 43.97 -67.70
REMARK 500 TRP A 694 25.72 -75.92
REMARK 500 ASN A 707 -79.36 -19.56
REMARK 500 ASP A 708 14.71 -66.01
REMARK 500 GLU A 721 -167.46 -117.97
REMARK 500 LEU A 726 -29.82 -37.86
REMARK 500 ASN A 753 156.16 177.31
REMARK 500 VAL A 781 18.83 -143.54
REMARK 500 ALA A 783 33.68 -69.06
REMARK 500 ASP A 807 88.31 -173.79
REMARK 500 LYS A 808 103.74 -56.20
REMARK 500 HIS A 843 -83.61 -87.95
REMARK 500 PRO A 845 -10.50 45.28
REMARK 500 ASN A 849 48.51 30.64
REMARK 500 GLU A 850 10.64 84.48
REMARK 500 SER A 874 -167.20 63.66
REMARK 500 ALA A 880 -70.59 -63.73
REMARK 500 LEU A 884 -88.92 -60.24
REMARK 500 LEU A 885 -39.43 -37.02
REMARK 500 ALA A 899 -59.62 -23.53
REMARK 500 PRO A 900 19.05 -67.92
REMARK 500 THR B 181 162.29 -48.34
REMARK 500 PHE B 196 -13.54 76.32
REMARK 500 VAL B 222 -74.02 -94.27
REMARK 500 THR B 225 -64.60 -21.23
REMARK 500 TRP B 235 25.48 -79.39
REMARK 500 HIS B 250 34.14 80.96
REMARK 500 ARG B 254 107.41 174.87
REMARK 500 PRO B 255 128.24 -34.21
REMARK 500 PRO B 256 -69.72 -26.99
REMARK 500 ARG B 265 -72.39 -58.06
REMARK 500 PRO B 272 -159.96 -80.93
REMARK 500 SER B 276 97.51 -36.21
REMARK 500 PRO B 277 -76.13 -56.37
REMARK 500 ARG B 278 -169.47 -122.27
REMARK 500 ASN B 291 -177.19 -56.44
REMARK 500 MET B 304 148.02 170.42
REMARK 500 ASP B 311 104.38 -163.31
REMARK 500 HIS B 313 -29.40 -154.18
REMARK 500 SER B 325 166.85 175.25
REMARK 500 PRO B 328 144.27 -27.49
REMARK 500 ALA B 336 50.60 -68.02
REMARK 500 LEU B 337 -75.61 -116.54
REMARK 500 VAL B 338 132.57 -38.15
REMARK 500 LYS B 362 -29.26 -38.44
REMARK 500 PHE C 196 -7.43 75.14
REMARK 500 GLU C 197 140.73 178.80
REMARK 500 VAL C 222 -69.97 -96.83
REMARK 500
REMARK 500 THIS ENTRY HAS 179 RAMACHANDRAN OUTLIERS.
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 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH D 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH E 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH H 8
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2PV0 RELATED DB: PDB
REMARK 900 DNMT3L
REMARK 900 RELATED ID: 2PVC RELATED DB: PDB
REMARK 900 DNMT3L-HISTONE H3 TAIL
DBREF 2QRV A 623 908 UNP Q9Y6K1 DNM3A_HUMAN 624 909
DBREF 2QRV B 160 386 UNP Q9UJW3 DNM3L_HUMAN 160 387
DBREF 2QRV C 160 386 UNP Q9UJW3 DNM3L_HUMAN 160 387
DBREF 2QRV D 625 908 UNP Q9Y6K1 DNM3A_HUMAN 624 909
DBREF 2QRV E 623 908 UNP Q9Y6K1 DNM3A_HUMAN 624 909
DBREF 2QRV F 160 386 UNP Q9UJW3 DNM3L_HUMAN 160 387
DBREF 2QRV G 160 386 UNP Q9UJW3 DNM3L_HUMAN 160 387
DBREF 2QRV H 623 908 UNP Q9Y6K1 DNM3A_HUMAN 624 909
SEQADV 2QRV MET A 614 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV GLY A 615 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV HIS A 616 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV HIS A 617 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV HIS A 618 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV HIS A 619 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV HIS A 620 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV HIS A 621 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV MET A 622 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV GLY B 157 UNP Q9UJW3 EXPRESSION TAG
SEQADV 2QRV SER B 158 UNP Q9UJW3 EXPRESSION TAG
SEQADV 2QRV MET B 159 UNP Q9UJW3 EXPRESSION TAG
SEQADV 2QRV GLY C 157 UNP Q9UJW3 EXPRESSION TAG
SEQADV 2QRV SER C 158 UNP Q9UJW3 EXPRESSION TAG
SEQADV 2QRV MET C 159 UNP Q9UJW3 EXPRESSION TAG
SEQADV 2QRV MET D 614 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV GLY D 615 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV HIS D 616 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV HIS D 617 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV HIS D 618 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV HIS D 619 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV HIS D 620 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV HIS D 621 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV MET D 622 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV MET E 614 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV GLY E 615 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV HIS E 616 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV HIS E 617 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV HIS E 618 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV HIS E 619 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV HIS E 620 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV HIS E 621 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV MET E 622 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV GLY F 157 UNP Q9UJW3 EXPRESSION TAG
SEQADV 2QRV SER F 158 UNP Q9UJW3 EXPRESSION TAG
SEQADV 2QRV MET F 159 UNP Q9UJW3 EXPRESSION TAG
SEQADV 2QRV GLY G 157 UNP Q9UJW3 EXPRESSION TAG
SEQADV 2QRV SER G 158 UNP Q9UJW3 EXPRESSION TAG
SEQADV 2QRV MET G 159 UNP Q9UJW3 EXPRESSION TAG
SEQADV 2QRV MET H 614 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV GLY H 615 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV HIS H 616 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV HIS H 617 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV HIS H 618 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV HIS H 619 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV HIS H 620 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV HIS H 621 UNP Q9Y6K1 EXPRESSION TAG
SEQADV 2QRV MET H 622 UNP Q9Y6K1 EXPRESSION TAG
SEQRES 1 A 295 MET GLY HIS HIS HIS HIS HIS HIS MET PRO ALA GLU LYS
SEQRES 2 A 295 ARG LYS PRO ILE ARG VAL LEU SER LEU PHE ASP GLY ILE
SEQRES 3 A 295 ALA THR GLY LEU LEU VAL LEU LYS ASP LEU GLY ILE GLN
SEQRES 4 A 295 VAL ASP ARG TYR ILE ALA SER GLU VAL CYS GLU ASP SER
SEQRES 5 A 295 ILE THR VAL GLY MET VAL ARG HIS GLN GLY LYS ILE MET
SEQRES 6 A 295 TYR VAL GLY ASP VAL ARG SER VAL THR GLN LYS HIS ILE
SEQRES 7 A 295 GLN GLU TRP GLY PRO PHE ASP LEU VAL ILE GLY GLY SER
SEQRES 8 A 295 PRO CYS ASN ASP LEU SER ILE VAL ASN PRO ALA ARG LYS
SEQRES 9 A 295 GLY LEU TYR GLU GLY THR GLY ARG LEU PHE PHE GLU PHE
SEQRES 10 A 295 TYR ARG LEU LEU HIS ASP ALA ARG PRO LYS GLU GLY ASP
SEQRES 11 A 295 ASP ARG PRO PHE PHE TRP LEU PHE GLU ASN VAL VAL ALA
SEQRES 12 A 295 MET GLY VAL SER ASP LYS ARG ASP ILE SER ARG PHE LEU
SEQRES 13 A 295 GLU SER ASN PRO VAL MET ILE ASP ALA LYS GLU VAL SER
SEQRES 14 A 295 ALA ALA HIS ARG ALA ARG TYR PHE TRP GLY ASN LEU PRO
SEQRES 15 A 295 GLY MET ASN ARG PRO LEU ALA SER THR VAL ASN ASP LYS
SEQRES 16 A 295 LEU GLU LEU GLN GLU CYS LEU GLU HIS GLY ARG ILE ALA
SEQRES 17 A 295 LYS PHE SER LYS VAL ARG THR ILE THR THR ARG SER ASN
SEQRES 18 A 295 SER ILE LYS GLN GLY LYS ASP GLN HIS PHE PRO VAL PHE
SEQRES 19 A 295 MET ASN GLU LYS GLU ASP ILE LEU TRP CYS THR GLU MET
SEQRES 20 A 295 GLU ARG VAL PHE GLY PHE PRO VAL HIS TYR THR ASP VAL
SEQRES 21 A 295 SER ASN MET SER ARG LEU ALA ARG GLN ARG LEU LEU GLY
SEQRES 22 A 295 ARG SER TRP SER VAL PRO VAL ILE ARG HIS LEU PHE ALA
SEQRES 23 A 295 PRO LEU LYS GLU TYR PHE ALA CYS VAL
SEQRES 1 B 230 GLY SER MET TRP ARG SER GLN LEU LYS ALA PHE TYR ASP
SEQRES 2 B 230 ARG GLU SER GLU ASN PRO LEU GLU MET PHE GLU THR VAL
SEQRES 3 B 230 PRO VAL TRP ARG ARG GLN PRO VAL ARG VAL LEU SER LEU
SEQRES 4 B 230 PHE GLU ASP ILE LYS LYS GLU LEU THR SER LEU GLY PHE
SEQRES 5 B 230 LEU GLU SER GLY SER ASP PRO GLY GLN LEU LYS HIS VAL
SEQRES 6 B 230 VAL ASP VAL THR ASP THR VAL ARG LYS ASP VAL GLU GLU
SEQRES 7 B 230 TRP GLY PRO PHE ASP LEU VAL TYR GLY ALA THR PRO PRO
SEQRES 8 B 230 LEU GLY HIS THR CYS ASP ARG PRO PRO SER TRP TYR LEU
SEQRES 9 B 230 PHE GLN PHE HIS ARG LEU LEU GLN TYR ALA ARG PRO LYS
SEQRES 10 B 230 PRO GLY SER PRO ARG PRO PHE PHE TRP MET PHE VAL ASP
SEQRES 11 B 230 ASN LEU VAL LEU ASN LYS GLU ASP LEU ASP VAL ALA SER
SEQRES 12 B 230 ARG PHE LEU GLU MET GLU PRO VAL THR ILE PRO ASP VAL
SEQRES 13 B 230 HIS GLY GLY SER LEU GLN ASN ALA VAL ARG VAL TRP SER
SEQRES 14 B 230 ASN ILE PRO ALA ILE ARG SER ARG HIS TRP ALA LEU VAL
SEQRES 15 B 230 SER GLU GLU GLU LEU SER LEU LEU ALA GLN ASN LYS GLN
SEQRES 16 B 230 SER SER LYS LEU ALA ALA LYS TRP PRO THR LYS LEU VAL
SEQRES 17 B 230 LYS ASN CYS PHE LEU PRO LEU ARG GLU TYR PHE LYS TYR
SEQRES 18 B 230 PHE SER THR GLU LEU THR SER SER LEU
SEQRES 1 C 230 GLY SER MET TRP ARG SER GLN LEU LYS ALA PHE TYR ASP
SEQRES 2 C 230 ARG GLU SER GLU ASN PRO LEU GLU MET PHE GLU THR VAL
SEQRES 3 C 230 PRO VAL TRP ARG ARG GLN PRO VAL ARG VAL LEU SER LEU
SEQRES 4 C 230 PHE GLU ASP ILE LYS LYS GLU LEU THR SER LEU GLY PHE
SEQRES 5 C 230 LEU GLU SER GLY SER ASP PRO GLY GLN LEU LYS HIS VAL
SEQRES 6 C 230 VAL ASP VAL THR ASP THR VAL ARG LYS ASP VAL GLU GLU
SEQRES 7 C 230 TRP GLY PRO PHE ASP LEU VAL TYR GLY ALA THR PRO PRO
SEQRES 8 C 230 LEU GLY HIS THR CYS ASP ARG PRO PRO SER TRP TYR LEU
SEQRES 9 C 230 PHE GLN PHE HIS ARG LEU LEU GLN TYR ALA ARG PRO LYS
SEQRES 10 C 230 PRO GLY SER PRO ARG PRO PHE PHE TRP MET PHE VAL ASP
SEQRES 11 C 230 ASN LEU VAL LEU ASN LYS GLU ASP LEU ASP VAL ALA SER
SEQRES 12 C 230 ARG PHE LEU GLU MET GLU PRO VAL THR ILE PRO ASP VAL
SEQRES 13 C 230 HIS GLY GLY SER LEU GLN ASN ALA VAL ARG VAL TRP SER
SEQRES 14 C 230 ASN ILE PRO ALA ILE ARG SER ARG HIS TRP ALA LEU VAL
SEQRES 15 C 230 SER GLU GLU GLU LEU SER LEU LEU ALA GLN ASN LYS GLN
SEQRES 16 C 230 SER SER LYS LEU ALA ALA LYS TRP PRO THR LYS LEU VAL
SEQRES 17 C 230 LYS ASN CYS PHE LEU PRO LEU ARG GLU TYR PHE LYS TYR
SEQRES 18 C 230 PHE SER THR GLU LEU THR SER SER LEU
SEQRES 1 D 295 MET GLY HIS HIS HIS HIS HIS HIS MET PRO ALA GLU LYS
SEQRES 2 D 295 ARG LYS PRO ILE ARG VAL LEU SER LEU PHE ASP GLY ILE
SEQRES 3 D 295 ALA THR GLY LEU LEU VAL LEU LYS ASP LEU GLY ILE GLN
SEQRES 4 D 295 VAL ASP ARG TYR ILE ALA SER GLU VAL CYS GLU ASP SER
SEQRES 5 D 295 ILE THR VAL GLY MET VAL ARG HIS GLN GLY LYS ILE MET
SEQRES 6 D 295 TYR VAL GLY ASP VAL ARG SER VAL THR GLN LYS HIS ILE
SEQRES 7 D 295 GLN GLU TRP GLY PRO PHE ASP LEU VAL ILE GLY GLY SER
SEQRES 8 D 295 PRO CYS ASN ASP LEU SER ILE VAL ASN PRO ALA ARG LYS
SEQRES 9 D 295 GLY LEU TYR GLU GLY THR GLY ARG LEU PHE PHE GLU PHE
SEQRES 10 D 295 TYR ARG LEU LEU HIS ASP ALA ARG PRO LYS GLU GLY ASP
SEQRES 11 D 295 ASP ARG PRO PHE PHE TRP LEU PHE GLU ASN VAL VAL ALA
SEQRES 12 D 295 MET GLY VAL SER ASP LYS ARG ASP ILE SER ARG PHE LEU
SEQRES 13 D 295 GLU SER ASN PRO VAL MET ILE ASP ALA LYS GLU VAL SER
SEQRES 14 D 295 ALA ALA HIS ARG ALA ARG TYR PHE TRP GLY ASN LEU PRO
SEQRES 15 D 295 GLY MET ASN ARG PRO LEU ALA SER THR VAL ASN ASP LYS
SEQRES 16 D 295 LEU GLU LEU GLN GLU CYS LEU GLU HIS GLY ARG ILE ALA
SEQRES 17 D 295 LYS PHE SER LYS VAL ARG THR ILE THR THR ARG SER ASN
SEQRES 18 D 295 SER ILE LYS GLN GLY LYS ASP GLN HIS PHE PRO VAL PHE
SEQRES 19 D 295 MET ASN GLU LYS GLU ASP ILE LEU TRP CYS THR GLU MET
SEQRES 20 D 295 GLU ARG VAL PHE GLY PHE PRO VAL HIS TYR THR ASP VAL
SEQRES 21 D 295 SER ASN MET SER ARG LEU ALA ARG GLN ARG LEU LEU GLY
SEQRES 22 D 295 ARG SER TRP SER VAL PRO VAL ILE ARG HIS LEU PHE ALA
SEQRES 23 D 295 PRO LEU LYS GLU TYR PHE ALA CYS VAL
SEQRES 1 E 295 MET GLY HIS HIS HIS HIS HIS HIS MET PRO ALA GLU LYS
SEQRES 2 E 295 ARG LYS PRO ILE ARG VAL LEU SER LEU PHE ASP GLY ILE
SEQRES 3 E 295 ALA THR GLY LEU LEU VAL LEU LYS ASP LEU GLY ILE GLN
SEQRES 4 E 295 VAL ASP ARG TYR ILE ALA SER GLU VAL CYS GLU ASP SER
SEQRES 5 E 295 ILE THR VAL GLY MET VAL ARG HIS GLN GLY LYS ILE MET
SEQRES 6 E 295 TYR VAL GLY ASP VAL ARG SER VAL THR GLN LYS HIS ILE
SEQRES 7 E 295 GLN GLU TRP GLY PRO PHE ASP LEU VAL ILE GLY GLY SER
SEQRES 8 E 295 PRO CYS ASN ASP LEU SER ILE VAL ASN PRO ALA ARG LYS
SEQRES 9 E 295 GLY LEU TYR GLU GLY THR GLY ARG LEU PHE PHE GLU PHE
SEQRES 10 E 295 TYR ARG LEU LEU HIS ASP ALA ARG PRO LYS GLU GLY ASP
SEQRES 11 E 295 ASP ARG PRO PHE PHE TRP LEU PHE GLU ASN VAL VAL ALA
SEQRES 12 E 295 MET GLY VAL SER ASP LYS ARG ASP ILE SER ARG PHE LEU
SEQRES 13 E 295 GLU SER ASN PRO VAL MET ILE ASP ALA LYS GLU VAL SER
SEQRES 14 E 295 ALA ALA HIS ARG ALA ARG TYR PHE TRP GLY ASN LEU PRO
SEQRES 15 E 295 GLY MET ASN ARG PRO LEU ALA SER THR VAL ASN ASP LYS
SEQRES 16 E 295 LEU GLU LEU GLN GLU CYS LEU GLU HIS GLY ARG ILE ALA
SEQRES 17 E 295 LYS PHE SER LYS VAL ARG THR ILE THR THR ARG SER ASN
SEQRES 18 E 295 SER ILE LYS GLN GLY LYS ASP GLN HIS PHE PRO VAL PHE
SEQRES 19 E 295 MET ASN GLU LYS GLU ASP ILE LEU TRP CYS THR GLU MET
SEQRES 20 E 295 GLU ARG VAL PHE GLY PHE PRO VAL HIS TYR THR ASP VAL
SEQRES 21 E 295 SER ASN MET SER ARG LEU ALA ARG GLN ARG LEU LEU GLY
SEQRES 22 E 295 ARG SER TRP SER VAL PRO VAL ILE ARG HIS LEU PHE ALA
SEQRES 23 E 295 PRO LEU LYS GLU TYR PHE ALA CYS VAL
SEQRES 1 F 230 GLY SER MET TRP ARG SER GLN LEU LYS ALA PHE TYR ASP
SEQRES 2 F 230 ARG GLU SER GLU ASN PRO LEU GLU MET PHE GLU THR VAL
SEQRES 3 F 230 PRO VAL TRP ARG ARG GLN PRO VAL ARG VAL LEU SER LEU
SEQRES 4 F 230 PHE GLU ASP ILE LYS LYS GLU LEU THR SER LEU GLY PHE
SEQRES 5 F 230 LEU GLU SER GLY SER ASP PRO GLY GLN LEU LYS HIS VAL
SEQRES 6 F 230 VAL ASP VAL THR ASP THR VAL ARG LYS ASP VAL GLU GLU
SEQRES 7 F 230 TRP GLY PRO PHE ASP LEU VAL TYR GLY ALA THR PRO PRO
SEQRES 8 F 230 LEU GLY HIS THR CYS ASP ARG PRO PRO SER TRP TYR LEU
SEQRES 9 F 230 PHE GLN PHE HIS ARG LEU LEU GLN TYR ALA ARG PRO LYS
SEQRES 10 F 230 PRO GLY SER PRO ARG PRO PHE PHE TRP MET PHE VAL ASP
SEQRES 11 F 230 ASN LEU VAL LEU ASN LYS GLU ASP LEU ASP VAL ALA SER
SEQRES 12 F 230 ARG PHE LEU GLU MET GLU PRO VAL THR ILE PRO ASP VAL
SEQRES 13 F 230 HIS GLY GLY SER LEU GLN ASN ALA VAL ARG VAL TRP SER
SEQRES 14 F 230 ASN ILE PRO ALA ILE ARG SER ARG HIS TRP ALA LEU VAL
SEQRES 15 F 230 SER GLU GLU GLU LEU SER LEU LEU ALA GLN ASN LYS GLN
SEQRES 16 F 230 SER SER LYS LEU ALA ALA LYS TRP PRO THR LYS LEU VAL
SEQRES 17 F 230 LYS ASN CYS PHE LEU PRO LEU ARG GLU TYR PHE LYS TYR
SEQRES 18 F 230 PHE SER THR GLU LEU THR SER SER LEU
SEQRES 1 G 230 GLY SER MET TRP ARG SER GLN LEU LYS ALA PHE TYR ASP
SEQRES 2 G 230 ARG GLU SER GLU ASN PRO LEU GLU MET PHE GLU THR VAL
SEQRES 3 G 230 PRO VAL TRP ARG ARG GLN PRO VAL ARG VAL LEU SER LEU
SEQRES 4 G 230 PHE GLU ASP ILE LYS LYS GLU LEU THR SER LEU GLY PHE
SEQRES 5 G 230 LEU GLU SER GLY SER ASP PRO GLY GLN LEU LYS HIS VAL
SEQRES 6 G 230 VAL ASP VAL THR ASP THR VAL ARG LYS ASP VAL GLU GLU
SEQRES 7 G 230 TRP GLY PRO PHE ASP LEU VAL TYR GLY ALA THR PRO PRO
SEQRES 8 G 230 LEU GLY HIS THR CYS ASP ARG PRO PRO SER TRP TYR LEU
SEQRES 9 G 230 PHE GLN PHE HIS ARG LEU LEU GLN TYR ALA ARG PRO LYS
SEQRES 10 G 230 PRO GLY SER PRO ARG PRO PHE PHE TRP MET PHE VAL ASP
SEQRES 11 G 230 ASN LEU VAL LEU ASN LYS GLU ASP LEU ASP VAL ALA SER
SEQRES 12 G 230 ARG PHE LEU GLU MET GLU PRO VAL THR ILE PRO ASP VAL
SEQRES 13 G 230 HIS GLY GLY SER LEU GLN ASN ALA VAL ARG VAL TRP SER
SEQRES 14 G 230 ASN ILE PRO ALA ILE ARG SER ARG HIS TRP ALA LEU VAL
SEQRES 15 G 230 SER GLU GLU GLU LEU SER LEU LEU ALA GLN ASN LYS GLN
SEQRES 16 G 230 SER SER LYS LEU ALA ALA LYS TRP PRO THR LYS LEU VAL
SEQRES 17 G 230 LYS ASN CYS PHE LEU PRO LEU ARG GLU TYR PHE LYS TYR
SEQRES 18 G 230 PHE SER THR GLU LEU THR SER SER LEU
SEQRES 1 H 295 MET GLY HIS HIS HIS HIS HIS HIS MET PRO ALA GLU LYS
SEQRES 2 H 295 ARG LYS PRO ILE ARG VAL LEU SER LEU PHE ASP GLY ILE
SEQRES 3 H 295 ALA THR GLY LEU LEU VAL LEU LYS ASP LEU GLY ILE GLN
SEQRES 4 H 295 VAL ASP ARG TYR ILE ALA SER GLU VAL CYS GLU ASP SER
SEQRES 5 H 295 ILE THR VAL GLY MET VAL ARG HIS GLN GLY LYS ILE MET
SEQRES 6 H 295 TYR VAL GLY ASP VAL ARG SER VAL THR GLN LYS HIS ILE
SEQRES 7 H 295 GLN GLU TRP GLY PRO PHE ASP LEU VAL ILE GLY GLY SER
SEQRES 8 H 295 PRO CYS ASN ASP LEU SER ILE VAL ASN PRO ALA ARG LYS
SEQRES 9 H 295 GLY LEU TYR GLU GLY THR GLY ARG LEU PHE PHE GLU PHE
SEQRES 10 H 295 TYR ARG LEU LEU HIS ASP ALA ARG PRO LYS GLU GLY ASP
SEQRES 11 H 295 ASP ARG PRO PHE PHE TRP LEU PHE GLU ASN VAL VAL ALA
SEQRES 12 H 295 MET GLY VAL SER ASP LYS ARG ASP ILE SER ARG PHE LEU
SEQRES 13 H 295 GLU SER ASN PRO VAL MET ILE ASP ALA LYS GLU VAL SER
SEQRES 14 H 295 ALA ALA HIS ARG ALA ARG TYR PHE TRP GLY ASN LEU PRO
SEQRES 15 H 295 GLY MET ASN ARG PRO LEU ALA SER THR VAL ASN ASP LYS
SEQRES 16 H 295 LEU GLU LEU GLN GLU CYS LEU GLU HIS GLY ARG ILE ALA
SEQRES 17 H 295 LYS PHE SER LYS VAL ARG THR ILE THR THR ARG SER ASN
SEQRES 18 H 295 SER ILE LYS GLN GLY LYS ASP GLN HIS PHE PRO VAL PHE
SEQRES 19 H 295 MET ASN GLU LYS GLU ASP ILE LEU TRP CYS THR GLU MET
SEQRES 20 H 295 GLU ARG VAL PHE GLY PHE PRO VAL HIS TYR THR ASP VAL
SEQRES 21 H 295 SER ASN MET SER ARG LEU ALA ARG GLN ARG LEU LEU GLY
SEQRES 22 H 295 ARG SER TRP SER VAL PRO VAL ILE ARG HIS LEU PHE ALA
SEQRES 23 H 295 PRO LEU LYS GLU TYR PHE ALA CYS VAL
HET SAH A 1 26
HET SAH D 4 26
HET SAH E 5 26
HET SAH H 8 26
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
FORMUL 9 SAH 4(C14 H20 N6 O5 S)
HELIX 1 1 ALA A 640 LEU A 649 1 10
HELIX 2 2 CYS A 662 HIS A 673 1 12
HELIX 3 3 ASP A 682 VAL A 686 5 5
HELIX 4 4 THR A 687 TRP A 694 1 8
HELIX 5 5 CYS A 706 SER A 710 5 5
HELIX 6 6 ARG A 725 ARG A 738 1 14
HELIX 7 7 GLY A 758 GLU A 770 1 13
HELIX 8 8 LYS A 779 VAL A 781 5 3
HELIX 9 9 GLU A 810 CYS A 814 5 5
HELIX 10 10 TRP A 856 GLY A 865 1 10
HELIX 11 11 SER A 877 ARG A 887 1 11
HELIX 12 12 SER A 890 ALA A 899 1 10
HELIX 13 13 PRO A 900 PHE A 905 5 6
HELIX 14 14 PRO B 183 ARG B 187 5 5
HELIX 15 15 VAL B 228 TRP B 235 1 8
HELIX 16 16 PRO B 256 ARG B 271 1 16
HELIX 17 17 ASN B 291 GLU B 303 1 13
HELIX 18 18 SER B 339 SER B 352 1 14
HELIX 19 19 THR B 361 ASN B 366 1 6
HELIX 20 20 CYS B 367 TYR B 374 5 8
HELIX 21 21 PRO C 183 ARG C 187 5 5
HELIX 22 22 VAL C 228 TRP C 235 1 8
HELIX 23 23 PRO C 256 ALA C 270 1 15
HELIX 24 24 ASN C 291 GLU C 303 1 13
HELIX 25 25 SER C 339 SER C 352 1 14
HELIX 26 26 THR C 361 ASN C 366 1 6
HELIX 27 27 CYS C 367 TYR C 374 5 8
HELIX 28 28 ALA D 640 LEU D 649 1 10
HELIX 29 29 CYS D 662 HIS D 673 1 12
HELIX 30 30 ASP D 682 VAL D 686 5 5
HELIX 31 31 THR D 687 TRP D 694 1 8
HELIX 32 32 CYS D 706 SER D 710 5 5
HELIX 33 33 ARG D 725 ARG D 738 1 14
HELIX 34 34 GLY D 758 LEU D 769 1 12
HELIX 35 35 LYS D 779 VAL D 781 5 3
HELIX 36 36 GLU D 810 LEU D 815 5 6
HELIX 37 37 TRP D 856 GLY D 865 1 10
HELIX 38 38 SER D 877 ARG D 887 1 11
HELIX 39 39 SER D 890 ALA D 899 1 10
HELIX 40 40 PRO D 900 PHE D 905 5 6
HELIX 41 41 ALA E 640 LEU E 649 1 10
HELIX 42 42 CYS E 662 HIS E 673 1 12
HELIX 43 43 ASP E 682 VAL E 686 5 5
HELIX 44 44 THR E 687 TRP E 694 1 8
HELIX 45 45 CYS E 706 SER E 710 5 5
HELIX 46 46 ARG E 725 ARG E 738 1 14
HELIX 47 47 GLY E 758 GLU E 770 1 13
HELIX 48 48 LYS E 779 VAL E 781 5 3
HELIX 49 49 GLU E 810 LEU E 815 5 6
HELIX 50 50 TRP E 856 PHE E 864 1 9
HELIX 51 51 SER E 877 SER E 888 1 12
HELIX 52 52 SER E 890 ALA E 899 1 10
HELIX 53 53 PRO E 900 PHE E 905 5 6
HELIX 54 54 PRO F 183 ARG F 187 5 5
HELIX 55 55 VAL F 228 TRP F 235 1 8
HELIX 56 56 PRO F 256 ALA F 270 1 15
HELIX 57 57 ASN F 291 GLU F 303 1 13
HELIX 58 58 SER F 339 SER F 352 1 14
HELIX 59 59 THR F 361 ASN F 366 1 6
HELIX 60 60 CYS F 367 TYR F 374 5 8
HELIX 61 61 PRO G 183 ARG G 187 5 5
HELIX 62 62 VAL G 228 TRP G 235 1 8
HELIX 63 63 PRO G 256 ALA G 270 1 15
HELIX 64 64 ASN G 291 GLU G 303 1 13
HELIX 65 65 SER G 339 SER G 352 1 14
HELIX 66 66 THR G 361 ASN G 366 1 6
HELIX 67 67 CYS G 367 TYR G 374 5 8
HELIX 68 68 ALA H 640 LEU H 649 1 10
HELIX 69 69 CYS H 662 HIS H 673 1 12
HELIX 70 70 ASP H 682 VAL H 686 5 5
HELIX 71 71 THR H 687 TRP H 694 1 8
HELIX 72 72 CYS H 706 SER H 710 5 5
HELIX 73 73 ARG H 725 ARG H 738 1 14
HELIX 74 74 GLY H 758 GLU H 770 1 13
HELIX 75 75 LYS H 779 VAL H 781 5 3
HELIX 76 76 GLU H 810 LEU H 815 5 6
HELIX 77 77 TRP H 856 GLY H 865 1 10
HELIX 78 78 SER H 877 SER H 888 1 12
HELIX 79 79 SER H 890 PHE H 898 1 9
HELIX 80 80 ALA H 899 TYR H 904 5 6
SHEET 1 A 7 ILE A 677 VAL A 680 0
SHEET 2 A 7 VAL A 653 SER A 659 1 N ALA A 658 O VAL A 680
SHEET 3 A 7 ILE A 630 LEU A 635 1 N VAL A 632 O ARG A 655
SHEET 4 A 7 LEU A 699 GLY A 702 1 O LEU A 699 N LEU A 633
SHEET 5 A 7 PHE A 748 VAL A 754 1 O LEU A 750 N VAL A 700
SHEET 6 A 7 ALA A 787 GLY A 792 -1 O TYR A 789 N ASN A 753
SHEET 7 A 7 ILE A 776 ASP A 777 -1 N ILE A 776 O ARG A 788
SHEET 1 B 3 ILE A 820 ALA A 821 0
SHEET 2 B 3 VAL A 846 MET A 848 -1 O PHE A 847 N ILE A 820
SHEET 3 B 3 LYS A 851 ASP A 853 -1 O LYS A 851 N MET A 848
SHEET 1 C 6 LEU B 218 VAL B 221 0
SHEET 2 C 6 VAL B 192 LEU B 195 1 N VAL B 192 O LYS B 219
SHEET 3 C 6 LEU B 240 ALA B 244 1 O TYR B 242 N LEU B 195
SHEET 4 C 6 PHE B 281 ASP B 286 1 O MET B 283 N VAL B 241
SHEET 5 C 6 ARG B 322 SER B 325 -1 O ARG B 322 N ASP B 286
SHEET 6 C 6 VAL B 307 THR B 308 -1 N VAL B 307 O VAL B 323
SHEET 1 D 6 LEU C 218 VAL C 221 0
SHEET 2 D 6 VAL C 192 LEU C 195 1 N VAL C 192 O LYS C 219
SHEET 3 D 6 LEU C 240 ALA C 244 1 O TYR C 242 N LEU C 195
SHEET 4 D 6 PHE C 281 ASP C 286 1 O MET C 283 N VAL C 241
SHEET 5 D 6 ARG C 322 SER C 325 -1 O ARG C 322 N ASP C 286
SHEET 6 D 6 VAL C 307 THR C 308 -1 N VAL C 307 O VAL C 323
SHEET 1 E 7 ILE D 677 VAL D 680 0
SHEET 2 E 7 VAL D 653 SER D 659 1 N ALA D 658 O VAL D 680
SHEET 3 E 7 ILE D 630 LEU D 635 1 N SER D 634 O ILE D 657
SHEET 4 E 7 LEU D 699 GLY D 702 1 O ILE D 701 N LEU D 635
SHEET 5 E 7 PHE D 748 VAL D 754 1 O LEU D 750 N VAL D 700
SHEET 6 E 7 ALA D 787 GLY D 792 -1 O TYR D 789 N ASN D 753
SHEET 7 E 7 ILE D 776 ASP D 777 -1 N ILE D 776 O ARG D 788
SHEET 1 F 3 ARG D 819 ALA D 821 0
SHEET 2 F 3 VAL D 846 MET D 848 -1 O PHE D 847 N ILE D 820
SHEET 3 F 3 LYS D 851 ASP D 853 -1 O LYS D 851 N MET D 848
SHEET 1 G 7 ILE E 677 VAL E 680 0
SHEET 2 G 7 VAL E 653 SER E 659 1 N ALA E 658 O VAL E 680
SHEET 3 G 7 ILE E 630 LEU E 635 1 N SER E 634 O ILE E 657
SHEET 4 G 7 LEU E 699 GLY E 702 1 O ILE E 701 N LEU E 633
SHEET 5 G 7 PHE E 748 VAL E 754 1 O LEU E 750 N VAL E 700
SHEET 6 G 7 ALA E 787 GLY E 792 -1 O TYR E 789 N ASN E 753
SHEET 7 G 7 ILE E 776 ASP E 777 -1 N ILE E 776 O ARG E 788
SHEET 1 H 3 ILE E 820 ALA E 821 0
SHEET 2 H 3 VAL E 846 PHE E 847 -1 O PHE E 847 N ILE E 820
SHEET 3 H 3 GLU E 852 ASP E 853 -1 O ASP E 853 N VAL E 846
SHEET 1 I 6 LEU F 218 VAL F 221 0
SHEET 2 I 6 VAL F 192 LEU F 195 1 N VAL F 192 O LYS F 219
SHEET 3 I 6 LEU F 240 ALA F 244 1 O TYR F 242 N LEU F 193
SHEET 4 I 6 PHE F 281 ASP F 286 1 O MET F 283 N VAL F 241
SHEET 5 I 6 ARG F 322 SER F 325 -1 O ARG F 322 N ASP F 286
SHEET 6 I 6 VAL F 307 THR F 308 -1 N VAL F 307 O VAL F 323
SHEET 1 J 6 LEU G 218 VAL G 221 0
SHEET 2 J 6 VAL G 192 LEU G 195 1 N VAL G 192 O LYS G 219
SHEET 3 J 6 LEU G 240 ALA G 244 1 O TYR G 242 N LEU G 193
SHEET 4 J 6 PHE G 281 ASP G 286 1 O MET G 283 N VAL G 241
SHEET 5 J 6 ARG G 322 SER G 325 -1 O ARG G 322 N ASP G 286
SHEET 6 J 6 VAL G 307 THR G 308 -1 N VAL G 307 O VAL G 323
SHEET 1 K 7 ILE H 677 VAL H 680 0
SHEET 2 K 7 VAL H 653 SER H 659 1 N TYR H 656 O MET H 678
SHEET 3 K 7 ILE H 630 LEU H 635 1 N VAL H 632 O ARG H 655
SHEET 4 K 7 LEU H 699 GLY H 702 1 O ILE H 701 N LEU H 635
SHEET 5 K 7 PHE H 748 VAL H 754 1 O LEU H 750 N VAL H 700
SHEET 6 K 7 ALA H 787 GLY H 792 -1 O TYR H 789 N ASN H 753
SHEET 7 K 7 ILE H 776 ASP H 777 -1 N ILE H 776 O ARG H 788
SHEET 1 L 3 ILE H 820 ALA H 821 0
SHEET 2 L 3 VAL H 846 PHE H 847 -1 O PHE H 847 N ILE H 820
SHEET 3 L 3 GLU H 852 ASP H 853 -1 O ASP H 853 N VAL H 846
SITE 1 AC1 18 PHE A 636 ASP A 637 GLY A 638 ILE A 639
SITE 2 AC1 18 THR A 641 SER A 659 GLU A 660 VAL A 661
SITE 3 AC1 18 CYS A 662 ASP A 682 VAL A 683 ARG A 684
SITE 4 AC1 18 GLY A 703 PRO A 705 LEU A 726 ARG A 887
SITE 5 AC1 18 SER A 888 TRP A 889
SITE 1 AC2 18 PHE D 636 ASP D 637 GLY D 638 ILE D 639
SITE 2 AC2 18 THR D 641 SER D 659 GLU D 660 VAL D 661
SITE 3 AC2 18 CYS D 662 ASP D 682 VAL D 683 ARG D 684
SITE 4 AC2 18 GLY D 703 PRO D 705 LEU D 726 ARG D 887
SITE 5 AC2 18 SER D 888 TRP D 889
SITE 1 AC3 17 PHE E 636 GLY E 638 ILE E 639 THR E 641
SITE 2 AC3 17 SER E 659 GLU E 660 VAL E 661 CYS E 662
SITE 3 AC3 17 ASP E 682 VAL E 683 ARG E 684 GLY E 703
SITE 4 AC3 17 PRO E 705 LEU E 726 ARG E 887 SER E 888
SITE 5 AC3 17 TRP E 889
SITE 1 AC4 13 PHE H 636 GLY H 638 ILE H 639 THR H 641
SITE 2 AC4 13 GLU H 660 VAL H 661 CYS H 662 ASP H 682
SITE 3 AC4 13 VAL H 683 GLY H 703 ARG H 887 SER H 888
SITE 4 AC4 13 TRP H 889
CRYST1 401.881 401.881 49.689 90.00 90.00 120.00 H 3 36
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 0.002488 0.001437 0.000000 0.00000
SCALE2 0.000000 0.002873 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020125 0.00000
(ATOM LINES ARE NOT SHOWN.)
END