HEADER TRANSFERASE 05-FEB-03 1NW3
TITLE STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN DOT1L, A NON-SET
TITLE 2 DOMAIN NUCLEOSOMAL HISTONE METHYLTRANSFERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE METHYLTRANSFERASE DOT1L;
COMPND 3 CHAIN: A;
COMPND 4 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: DOT1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-KG
KEYWDS HDOT1, HISTONE LYSINE METHYLTRANSFERASE,
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.MIN,Q.FENG,Z.H.LI,Y.ZHANG,R.M.XU
REVDAT 2 24-FEB-09 1NW3 1 VERSN
REVDAT 1 25-MAR-03 1NW3 0
JRNL AUTH J.MIN,Q.FENG,Z.LI,Y.ZHANG,R.M.XU
JRNL TITL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN DOT1L,
JRNL TITL 2 A NON-SET DOMAIN NUCLEOSOMAL HISTONE
JRNL TITL 3 METHYLTRANSFERASE
JRNL REF CELL(CAMBRIDGE,MASS.) V. 112 711 2003
JRNL REFN ISSN 0092-8674
JRNL PMID 12628190
JRNL DOI 10.1016/S0092-8674(03)00114-4
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 22926
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) : 0.204
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1810
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 : 2671
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 68
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 50.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.38
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NW3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-FEB-03.
REMARK 100 THE RCSB ID CODE IS RCSB018270.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JUL-02; NULL
REMARK 200 TEMPERATURE (KELVIN) : 100; NULL
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; NULL
REMARK 200 RADIATION SOURCE : NSLS; NULL
REMARK 200 BEAMLINE : X26C; NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1; NULL
REMARK 200 MONOCHROMATOR : GRAPHITE; GRAPHITE
REMARK 200 OPTICS : SI MONOCHROMATOR; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; NULL
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4; NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22926
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : 0.05900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
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 (%): 71.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PH 4.6, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 17K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 33.87333
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 16.93667
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 25.40500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 8.46833
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 42.34167
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 1
REMARK 465 GLY A 2
REMARK 465 GLU A 3
REMARK 465 LYS A 4
REMARK 465 LYS A 333
REMARK 465 LEU A 334
REMARK 465 ARG A 335
REMARK 465 GLU A 336
REMARK 465 GLU A 337
REMARK 465 GLN A 338
REMARK 465 GLU A 339
REMARK 465 ALA A 340
REMARK 465 ALA A 341
REMARK 465 ARG A 342
REMARK 465 ARG A 343
REMARK 465 ARG A 344
REMARK 465 GLN A 345
REMARK 465 GLN A 346
REMARK 465 ARG A 347
REMARK 465 GLU A 348
REMARK 465 SER A 349
REMARK 465 LYS A 350
REMARK 465 SER A 351
REMARK 465 ASN A 352
REMARK 465 ALA A 353
REMARK 465 ALA A 354
REMARK 465 THR A 355
REMARK 465 PRO A 356
REMARK 465 THR A 357
REMARK 465 LYS A 358
REMARK 465 GLY A 359
REMARK 465 PRO A 360
REMARK 465 GLU A 361
REMARK 465 GLY A 362
REMARK 465 LYS A 363
REMARK 465 VAL A 364
REMARK 465 ALA A 365
REMARK 465 GLY A 366
REMARK 465 PRO A 367
REMARK 465 ALA A 368
REMARK 465 ASP A 369
REMARK 465 ALA A 370
REMARK 465 PRO A 371
REMARK 465 MET A 372
REMARK 465 ASP A 373
REMARK 465 SER A 374
REMARK 465 GLY A 375
REMARK 465 ALA A 376
REMARK 465 GLU A 377
REMARK 465 GLU A 378
REMARK 465 GLU A 379
REMARK 465 LYS A 380
REMARK 465 ALA A 381
REMARK 465 GLY A 382
REMARK 465 ALA A 383
REMARK 465 ALA A 384
REMARK 465 THR A 385
REMARK 465 VAL A 386
REMARK 465 LYS A 387
REMARK 465 LYS A 388
REMARK 465 PRO A 389
REMARK 465 SER A 390
REMARK 465 PRO A 391
REMARK 465 SER A 392
REMARK 465 LYS A 393
REMARK 465 ALA A 394
REMARK 465 ARG A 395
REMARK 465 LYS A 396
REMARK 465 LYS A 397
REMARK 465 LYS A 398
REMARK 465 LEU A 399
REMARK 465 ASN A 400
REMARK 465 LYS A 401
REMARK 465 LYS A 402
REMARK 465 GLY A 403
REMARK 465 ARG A 404
REMARK 465 LYS A 405
REMARK 465 MET A 406
REMARK 465 ALA A 407
REMARK 465 GLY A 408
REMARK 465 ARG A 409
REMARK 465 LYS A 410
REMARK 465 ARG A 411
REMARK 465 GLY A 412
REMARK 465 ARG A 413
REMARK 465 PRO A 414
REMARK 465 LYS A 415
REMARK 465 LYS A 416
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 HOH A 1046 O HOH A 1067 0.00
REMARK 500 O HOH A 1016 O HOH A 1048 2.18
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 ASN A 57 96.74 -54.41
REMARK 500 TYR A 58 -24.87 80.54
REMARK 500 VAL A 59 76.70 -65.23
REMARK 500 LEU A 60 51.12 -90.49
REMARK 500 ILE A 61 2.64 59.29
REMARK 500 ASP A 62 41.36 -61.49
REMARK 500 THR A 65 -11.45 -48.68
REMARK 500 ASN A 178 50.43 -115.41
REMARK 500 SER A 302 89.73 -167.80
REMARK 500 ASN A 331 -159.56 -111.83
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 ACT A 600
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 601
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 602
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM A 500
DBREF 1NW3 A 1 416 UNP Q8TEK3 DOT1L_HUMAN 1 416
SEQRES 1 A 416 MET GLY GLU LYS LEU GLU LEU ARG LEU LYS SER PRO VAL
SEQRES 2 A 416 GLY ALA GLU PRO ALA VAL TYR PRO TRP PRO LEU PRO VAL
SEQRES 3 A 416 TYR ASP LYS HIS HIS ASP ALA ALA HIS GLU ILE ILE GLU
SEQRES 4 A 416 THR ILE ARG TRP VAL CYS GLU GLU ILE PRO ASP LEU LYS
SEQRES 5 A 416 LEU ALA MET GLU ASN TYR VAL LEU ILE ASP TYR ASP THR
SEQRES 6 A 416 LYS SER PHE GLU SER MET GLN ARG LEU CYS ASP LYS TYR
SEQRES 7 A 416 ASN ARG ALA ILE ASP SER ILE HIS GLN LEU TRP LYS GLY
SEQRES 8 A 416 THR THR GLN PRO MET LYS LEU ASN THR ARG PRO SER THR
SEQRES 9 A 416 GLY LEU LEU ARG HIS ILE LEU GLN GLN VAL TYR ASN HIS
SEQRES 10 A 416 SER VAL THR ASP PRO GLU LYS LEU ASN ASN TYR GLU PRO
SEQRES 11 A 416 PHE SER PRO GLU VAL TYR GLY GLU THR SER PHE ASP LEU
SEQRES 12 A 416 VAL ALA GLN MET ILE ASP GLU ILE LYS MET THR ASP ASP
SEQRES 13 A 416 ASP LEU PHE VAL ASP LEU GLY SER GLY VAL GLY GLN VAL
SEQRES 14 A 416 VAL LEU GLN VAL ALA ALA ALA THR ASN CYS LYS HIS HIS
SEQRES 15 A 416 TYR GLY VAL GLU LYS ALA ASP ILE PRO ALA LYS TYR ALA
SEQRES 16 A 416 GLU THR MET ASP ARG GLU PHE ARG LYS TRP MET LYS TRP
SEQRES 17 A 416 TYR GLY LYS LYS HIS ALA GLU TYR THR LEU GLU ARG GLY
SEQRES 18 A 416 ASP PHE LEU SER GLU GLU TRP ARG GLU ARG ILE ALA ASN
SEQRES 19 A 416 THR SER VAL ILE PHE VAL ASN ASN PHE ALA PHE GLY PRO
SEQRES 20 A 416 GLU VAL ASP HIS GLN LEU LYS GLU ARG PHE ALA ASN MET
SEQRES 21 A 416 LYS GLU GLY GLY ARG ILE VAL SER SER LYS PRO PHE ALA
SEQRES 22 A 416 PRO LEU ASN PHE ARG ILE ASN SER ARG ASN LEU SER ASP
SEQRES 23 A 416 ILE GLY THR ILE MET ARG VAL VAL GLU LEU SER PRO LEU
SEQRES 24 A 416 LYS GLY SER VAL SER TRP THR GLY LYS PRO VAL SER TYR
SEQRES 25 A 416 TYR LEU HIS THR ILE ASP ARG THR ILE LEU GLU ASN TYR
SEQRES 26 A 416 PHE SER SER LEU LYS ASN PRO LYS LEU ARG GLU GLU GLN
SEQRES 27 A 416 GLU ALA ALA ARG ARG ARG GLN GLN ARG GLU SER LYS SER
SEQRES 28 A 416 ASN ALA ALA THR PRO THR LYS GLY PRO GLU GLY LYS VAL
SEQRES 29 A 416 ALA GLY PRO ALA ASP ALA PRO MET ASP SER GLY ALA GLU
SEQRES 30 A 416 GLU GLU LYS ALA GLY ALA ALA THR VAL LYS LYS PRO SER
SEQRES 31 A 416 PRO SER LYS ALA ARG LYS LYS LYS LEU ASN LYS LYS GLY
SEQRES 32 A 416 ARG LYS MET ALA GLY ARG LYS ARG GLY ARG PRO LYS LYS
HET ACT A 600 4
HET SO4 A 601 5
HET SO4 A 602 5
HET SAM A 500 27
HETNAM ACT ACETATE ION
HETNAM SO4 SULFATE ION
HETNAM SAM S-ADENOSYLMETHIONINE
FORMUL 2 ACT C2 H3 O2 1-
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 SAM C15 H22 N6 O5 S
FORMUL 6 HOH *68(H2 O)
HELIX 1 1 ALA A 33 ILE A 48 1 16
HELIX 2 2 ILE A 48 GLU A 56 1 9
HELIX 3 3 SER A 67 GLY A 91 1 25
HELIX 4 4 SER A 103 VAL A 119 1 17
HELIX 5 5 ASP A 121 ASN A 127 5 7
HELIX 6 6 SER A 140 ILE A 151 1 12
HELIX 7 7 GLY A 167 THR A 177 1 11
HELIX 8 8 ALA A 188 GLY A 210 1 23
HELIX 9 9 SER A 225 THR A 235 1 11
HELIX 10 10 GLY A 246 ALA A 258 1 13
HELIX 11 11 ASP A 286 THR A 289 5 4
HELIX 12 12 ARG A 319 ASN A 331 1 13
SHEET 1 A 2 GLU A 6 LEU A 9 0
SHEET 2 A 2 ALA A 18 PRO A 21 -1 O TYR A 20 N LEU A 7
SHEET 1 B 2 VAL A 26 ASP A 28 0
SHEET 2 B 2 HIS A 31 ASP A 32 -1 O HIS A 31 N ASP A 28
SHEET 1 C 7 TYR A 216 ARG A 220 0
SHEET 2 C 7 HIS A 181 GLU A 186 1 N GLY A 184 O GLU A 219
SHEET 3 C 7 LEU A 158 LEU A 162 1 N PHE A 159 O TYR A 183
SHEET 4 C 7 VAL A 237 VAL A 240 1 O PHE A 239 N VAL A 160
SHEET 5 C 7 ARG A 265 SER A 268 1 O VAL A 267 N ILE A 238
SHEET 6 C 7 TYR A 313 ILE A 317 -1 O HIS A 315 N ILE A 266
SHEET 7 C 7 MET A 291 GLU A 295 -1 N ARG A 292 O THR A 316
CISPEP 1 TRP A 22 PRO A 23 0 0.16
CISPEP 2 ASN A 331 PRO A 332 0 0.21
SITE 1 AC1 4 TYR A 183 ARG A 231 THR A 235 HOH A1047
SITE 1 AC2 2 ARG A 203 HIS A 213
SITE 1 AC3 4 ARG A 229 GLN A 252 GLU A 255 ARG A 256
SITE 1 AC4 17 PRO A 133 GLY A 137 GLU A 138 THR A 139
SITE 2 AC4 17 ASP A 161 GLY A 163 GLN A 168 VAL A 169
SITE 3 AC4 17 GLU A 186 LYS A 187 GLY A 221 ASP A 222
SITE 4 AC4 17 PHE A 223 PHE A 239 ASN A 241 PHE A 245
SITE 5 AC4 17 HOH A1032
CRYST1 152.800 152.800 50.810 90.00 90.00 120.00 P 65 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 0.006545 0.003778 0.000000 0.00000
SCALE2 0.000000 0.007557 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019681 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
