HEADER TRANSFERASE/TRANSFERASE INHIBITOR 01-MAR-16 5IJ7
TITLE STRUCTURE OF HS/ACPRC2 IN COMPLEX WITH A PYRIDONE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENHANCER OF ZESTE HOMOLOG 2 (EZH2),HISTONE-LYSINE N-
COMPND 3 METHYLTRANSFERASE EZH2;
COMPND 4 CHAIN: A, B;
COMPND 5 SYNONYM: ENX-1,ENHANCER OF ZESTE HOMOLOG 2,LYSINE N-METHYLTRANSFERASE
COMPND 6 6;
COMPND 7 EC: 2.1.1.43;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: POLYCOMB PROTEIN EED;
COMPND 11 CHAIN: E, F;
COMPND 12 SYNONYM: HEED,WD PROTEIN ASSOCIATING WITH INTEGRIN CYTOPLASMIC TAILS
COMPND 13 1,WAIT-1;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: POLYCOMB PROTEIN SUZ12;
COMPND 17 CHAIN: S, T;
COMPND 18 SYNONYM: CHROMATIN PRECIPITATED E2F TARGET 9 PROTEIN,CHET 9 PROTEIN,
COMPND 19 JOINED TO JAZF1 PROTEIN,SUPPRESSOR OF ZESTE 12 PROTEIN HOMOLOG;
COMPND 20 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ANOLIS CAROLINENSIS, HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: GREEN ANOLE, HUMAN;
SOURCE 4 ORGANISM_TAXID: 28377, 9606;
SOURCE 5 GENE: EZH2, EZH2, KMT6;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: EED;
SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 17 ORGANISM_COMMON: HUMAN;
SOURCE 18 ORGANISM_TAXID: 9606;
SOURCE 19 GENE: SUZ12, CHET9, JJAZ1, KIAA0160;
SOURCE 20 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS LYSINE METHYLTRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.S.GAJIWALA,A.BROOUN,Y.-L.DENG,W.LIU
REVDAT 4 06-MAR-24 5IJ7 1 REMARK LINK
REVDAT 3 22-NOV-17 5IJ7 1 REMARK
REVDAT 2 11-MAY-16 5IJ7 1 JRNL
REVDAT 1 04-MAY-16 5IJ7 0
JRNL AUTH A.BROOUN,K.S.GAJIWALA,Y.L.DENG,W.LIU,B.BOLANOS,P.BINGHAM,
JRNL AUTH 2 Y.A.HE,W.DIEHL,N.GRABLE,P.P.KUNG,S.SUTTON,K.A.MAEGLEY,X.YU,
JRNL AUTH 3 A.E.STEWART
JRNL TITL POLYCOMB REPRESSIVE COMPLEX 2 STRUCTURE WITH INHIBITOR
JRNL TITL 2 REVEALS A MECHANISM OF ACTIVATION AND DRUG RESISTANCE.
JRNL REF NAT COMMUN V. 7 11384 2016
JRNL REFN ESSN 2041-1723
JRNL PMID 27122193
JRNL DOI 10.1038/NCOMMS11384
REMARK 2
REMARK 2 RESOLUTION. 2.62 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.4
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.62
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 91.15
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 70532
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 + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 3591
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 : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.62
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.69
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.60
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 5242
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2347
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4977
REMARK 3 BIN R VALUE (WORKING SET) : 0.2318
REMARK 3 BIN FREE R VALUE : 0.2868
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.06
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 265
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 : 15510
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 86
REMARK 3 SOLVENT ATOMS : 36
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 73.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 68.45
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -14.67040
REMARK 3 B22 (A**2) : 18.30440
REMARK 3 B33 (A**2) : -3.63400
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.33620
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.331
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.581
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.282
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.701
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.293
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.928
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.897
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 15954 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 21519 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 5716 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 448 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 2312 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 15954 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 15 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 2018 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 17737 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.14
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.00
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 21.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5IJ7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000218785.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 98
REMARK 200 PH : 6.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : AUTOPROC, AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70687
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.620
REMARK 200 RESOLUTION RANGE LOW (A) : 149.390
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.62
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.30600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: AUTOSHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24.0 %W/V PEG MONOMETHYL ETHER 2000,
REMARK 280 0.0050 M TCEP HYDROCHLORIDE, 0.1 M BIS_TRIS (PH 6.60), VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 286K
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 57.52100
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
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E, S
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -82.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F, T
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 GLN A 3
REMARK 465 THR A 4
REMARK 465 GLY A 5
REMARK 465 LYS A 6
REMARK 465 LYS A 7
REMARK 465 SER A 8
REMARK 465 SER A 73
REMARK 465 VAL A 74
REMARK 465 SER A 75
REMARK 465 SER A 76
REMARK 465 LEU A 77
REMARK 465 ARG A 78
REMARK 465 GLY A 79
REMARK 465 THR A 80
REMARK 465 GLU A 125
REMARK 465 THR A 126
REMARK 465 VAL A 127
REMARK 465 LEU A 128
REMARK 465 HIS A 129
REMARK 465 ASN A 130
REMARK 465 ILE A 131
REMARK 465 PRO A 132
REMARK 465 TYR A 133
REMARK 465 MET A 134
REMARK 465 GLY A 135
REMARK 465 ASP A 136
REMARK 465 GLU A 137
REMARK 465 VAL A 138
REMARK 465 LEU A 139
REMARK 465 ASP A 140
REMARK 465 GLN A 141
REMARK 465 ASP A 142
REMARK 465 GLY A 143
REMARK 465 THR A 144
REMARK 465 PHE A 145
REMARK 465 ILE A 146
REMARK 465 GLU A 147
REMARK 465 GLU A 148
REMARK 465 LEU A 149
REMARK 465 ILE A 150
REMARK 465 LYS A 151
REMARK 465 ASN A 152
REMARK 465 TYR A 153
REMARK 465 ASP A 154
REMARK 465 GLY A 155
REMARK 465 LYS A 156
REMARK 465 VAL A 157
REMARK 465 HIS A 158
REMARK 465 GLY A 159
REMARK 465 ASP A 160
REMARK 465 ARG A 161
REMARK 465 GLU A 162
REMARK 465 CYS A 163
REMARK 465 GLY A 164
REMARK 465 PHE A 165
REMARK 465 GLN A 200
REMARK 465 LYS A 201
REMARK 465 ASN A 202
REMARK 465 GLN A 203
REMARK 465 GLU A 204
REMARK 465 SER A 205
REMARK 465 ASN A 206
REMARK 465 GLN A 207
REMARK 465 ILE A 208
REMARK 465 ASP A 209
REMARK 465 LYS A 210
REMARK 465 GLU A 211
REMARK 465 SER A 212
REMARK 465 HIS A 213
REMARK 465 PRO A 214
REMARK 465 PRO A 215
REMARK 465 ARG A 216
REMARK 465 LYS A 217
REMARK 465 PHE A 218
REMARK 465 LEU A 247
REMARK 465 THR A 248
REMARK 465 GLU A 249
REMARK 465 GLN A 250
REMARK 465 GLN A 251
REMARK 465 LEU A 252
REMARK 465 PRO A 253
REMARK 465 GLY A 254
REMARK 465 ALA A 255
REMARK 465 LEU A 256
REMARK 465 PRO A 257
REMARK 465 PRO A 258
REMARK 465 GLU A 259
REMARK 465 LYS A 396
REMARK 465 ASN A 397
REMARK 465 THR A 398
REMARK 465 GLU A 399
REMARK 465 MET A 400
REMARK 465 ALA A 401
REMARK 465 ILE A 402
REMARK 465 ASP A 403
REMARK 465 ASN A 404
REMARK 465 LYS A 405
REMARK 465 PRO A 406
REMARK 465 CYS A 407
REMARK 465 GLY A 408
REMARK 465 PRO A 409
REMARK 465 HIS A 410
REMARK 465 CYS A 411
REMARK 465 TYR A 412
REMARK 465 GLN A 413
REMARK 465 HIS A 414
REMARK 465 LEU A 415
REMARK 465 GLU A 416
REMARK 465 GLY A 417
REMARK 465 ALA A 418
REMARK 465 LYS A 419
REMARK 465 GLU A 420
REMARK 465 PHE A 421
REMARK 465 ALA A 422
REMARK 465 ALA A 423
REMARK 465 ALA A 424
REMARK 465 LEU A 425
REMARK 465 THR A 426
REMARK 465 ALA A 427
REMARK 465 GLU A 428
REMARK 465 ASN A 429
REMARK 465 VAL A 430
REMARK 465 GLU A 431
REMARK 465 GLU A 477
REMARK 465 SER A 478
REMARK 465 SER A 479
REMARK 465 ILE A 480
REMARK 465 ILE A 481
REMARK 465 ALA A 482
REMARK 465 PRO A 483
REMARK 465 ALA A 484
REMARK 465 PRO A 485
REMARK 465 ALA A 486
REMARK 465 GLU A 487
REMARK 465 ASP A 488
REMARK 465 VAL A 489
REMARK 465 ASP A 490
REMARK 465 THR A 491
REMARK 465 LEU A 492
REMARK 465 GLY A 493
REMARK 465 GLY A 494
REMARK 465 GLY A 495
REMARK 465 GLY A 496
REMARK 465 SER A 497
REMARK 465 GLY A 498
REMARK 465 GLY A 499
REMARK 465 GLY A 500
REMARK 465 GLY A 501
REMARK 465 SER A 502
REMARK 465 GLY A 503
REMARK 465 GLY A 504
REMARK 465 GLY A 505
REMARK 465 GLY A 506
REMARK 465 SER A 507
REMARK 465 ALA A 508
REMARK 465 ALA A 509
REMARK 465 ALA A 510
REMARK 465 ASP A 511
REMARK 465 GLY A 512
REMARK 465 SER A 513
REMARK 465 SER A 514
REMARK 465 ASN A 515
REMARK 465 HIS A 516
REMARK 465 LEU A 734
REMARK 465 LYS A 735
REMARK 465 TYR A 736
REMARK 465 VAL A 737
REMARK 465 GLY A 738
REMARK 465 ILE A 739
REMARK 465 GLU A 740
REMARK 465 ARG A 741
REMARK 465 GLU A 742
REMARK 465 MET A 743
REMARK 465 GLU A 744
REMARK 465 ILE A 745
REMARK 465 PRO A 746
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 GLN B 3
REMARK 465 THR B 4
REMARK 465 GLY B 5
REMARK 465 LYS B 6
REMARK 465 LYS B 7
REMARK 465 SER B 8
REMARK 465 SER B 73
REMARK 465 VAL B 74
REMARK 465 SER B 75
REMARK 465 SER B 76
REMARK 465 LEU B 77
REMARK 465 ARG B 78
REMARK 465 GLY B 79
REMARK 465 THR B 80
REMARK 465 GLU B 125
REMARK 465 THR B 126
REMARK 465 VAL B 127
REMARK 465 LEU B 128
REMARK 465 HIS B 129
REMARK 465 ASN B 130
REMARK 465 ILE B 131
REMARK 465 PRO B 132
REMARK 465 TYR B 133
REMARK 465 MET B 134
REMARK 465 GLY B 135
REMARK 465 ASP B 136
REMARK 465 GLU B 137
REMARK 465 VAL B 138
REMARK 465 LEU B 139
REMARK 465 ASP B 140
REMARK 465 GLN B 141
REMARK 465 ASP B 142
REMARK 465 GLY B 143
REMARK 465 THR B 144
REMARK 465 PHE B 145
REMARK 465 ILE B 146
REMARK 465 GLU B 147
REMARK 465 GLU B 148
REMARK 465 LEU B 149
REMARK 465 ILE B 150
REMARK 465 LYS B 151
REMARK 465 ASN B 152
REMARK 465 TYR B 153
REMARK 465 ASP B 154
REMARK 465 GLY B 155
REMARK 465 LYS B 156
REMARK 465 VAL B 157
REMARK 465 HIS B 158
REMARK 465 GLY B 159
REMARK 465 ASP B 160
REMARK 465 ARG B 161
REMARK 465 GLU B 162
REMARK 465 CYS B 163
REMARK 465 GLY B 164
REMARK 465 PHE B 165
REMARK 465 GLN B 200
REMARK 465 LYS B 201
REMARK 465 ASN B 202
REMARK 465 GLN B 203
REMARK 465 GLU B 204
REMARK 465 SER B 205
REMARK 465 ASN B 206
REMARK 465 GLN B 207
REMARK 465 ILE B 208
REMARK 465 ASP B 209
REMARK 465 LYS B 210
REMARK 465 GLU B 211
REMARK 465 SER B 212
REMARK 465 HIS B 213
REMARK 465 PRO B 214
REMARK 465 PRO B 215
REMARK 465 ARG B 216
REMARK 465 LYS B 217
REMARK 465 PHE B 218
REMARK 465 GLU B 249
REMARK 465 GLN B 250
REMARK 465 GLN B 251
REMARK 465 LEU B 252
REMARK 465 PRO B 253
REMARK 465 GLY B 254
REMARK 465 ALA B 255
REMARK 465 LEU B 256
REMARK 465 PRO B 257
REMARK 465 PRO B 258
REMARK 465 GLU B 259
REMARK 465 LYS B 396
REMARK 465 ASN B 397
REMARK 465 THR B 398
REMARK 465 GLU B 399
REMARK 465 MET B 400
REMARK 465 ALA B 401
REMARK 465 ILE B 402
REMARK 465 ASP B 403
REMARK 465 ASN B 404
REMARK 465 LYS B 405
REMARK 465 PRO B 406
REMARK 465 CYS B 407
REMARK 465 GLY B 408
REMARK 465 PRO B 409
REMARK 465 HIS B 410
REMARK 465 CYS B 411
REMARK 465 TYR B 412
REMARK 465 GLN B 413
REMARK 465 HIS B 414
REMARK 465 LEU B 415
REMARK 465 GLU B 416
REMARK 465 GLY B 417
REMARK 465 ALA B 418
REMARK 465 LYS B 419
REMARK 465 GLU B 420
REMARK 465 PHE B 421
REMARK 465 ALA B 422
REMARK 465 ALA B 423
REMARK 465 ALA B 424
REMARK 465 LEU B 425
REMARK 465 THR B 426
REMARK 465 ALA B 427
REMARK 465 GLU B 428
REMARK 465 ASN B 429
REMARK 465 GLU B 477
REMARK 465 SER B 478
REMARK 465 SER B 479
REMARK 465 ILE B 480
REMARK 465 ILE B 481
REMARK 465 ALA B 482
REMARK 465 PRO B 483
REMARK 465 ALA B 484
REMARK 465 PRO B 485
REMARK 465 ALA B 486
REMARK 465 GLU B 487
REMARK 465 ASP B 488
REMARK 465 VAL B 489
REMARK 465 ASP B 490
REMARK 465 THR B 491
REMARK 465 LEU B 492
REMARK 465 GLY B 493
REMARK 465 GLY B 494
REMARK 465 GLY B 495
REMARK 465 GLY B 496
REMARK 465 SER B 497
REMARK 465 GLY B 498
REMARK 465 GLY B 499
REMARK 465 GLY B 500
REMARK 465 GLY B 501
REMARK 465 SER B 502
REMARK 465 GLY B 503
REMARK 465 GLY B 504
REMARK 465 GLY B 505
REMARK 465 GLY B 506
REMARK 465 SER B 507
REMARK 465 ALA B 508
REMARK 465 ALA B 509
REMARK 465 ALA B 510
REMARK 465 ASP B 511
REMARK 465 GLY B 512
REMARK 465 SER B 513
REMARK 465 SER B 514
REMARK 465 ASN B 515
REMARK 465 HIS B 516
REMARK 465 LEU B 734
REMARK 465 LYS B 735
REMARK 465 TYR B 736
REMARK 465 VAL B 737
REMARK 465 GLY B 738
REMARK 465 ILE B 739
REMARK 465 GLU B 740
REMARK 465 ARG B 741
REMARK 465 GLU B 742
REMARK 465 MET B 743
REMARK 465 GLU B 744
REMARK 465 ILE B 745
REMARK 465 PRO B 746
REMARK 465 MET E 66
REMARK 465 ASP E 381
REMARK 465 PRO E 382
REMARK 465 HIS E 383
REMARK 465 LYS E 384
REMARK 465 ALA E 385
REMARK 465 ARG E 427
REMARK 465 MET F 66
REMARK 465 ARG F 427
REMARK 465 MET S 535
REMARK 465 ASP S 536
REMARK 465 TYR S 537
REMARK 465 LYS S 538
REMARK 465 ASP S 539
REMARK 465 ASP S 540
REMARK 465 ASP S 541
REMARK 465 ASP S 542
REMARK 465 LYS S 543
REMARK 465 GLY S 544
REMARK 465 GLU S 545
REMARK 465 SER S 546
REMARK 465 GLU S 547
REMARK 465 ASP S 548
REMARK 465 GLY S 549
REMARK 465 GLU S 550
REMARK 465 VAL S 551
REMARK 465 GLU S 552
REMARK 465 GLN S 553
REMARK 465 GLN S 554
REMARK 465 ARG S 555
REMARK 465 THR S 556
REMARK 465 TYR S 557
REMARK 465 SER S 558
REMARK 465 SER S 559
REMARK 465 GLY S 560
REMARK 465 HIS S 561
REMARK 465 GLU S 689
REMARK 465 LYS S 690
REMARK 465 GLY S 691
REMARK 465 GLU S 692
REMARK 465 SER S 693
REMARK 465 ALA S 694
REMARK 465 SER S 695
REMARK 465 PRO S 696
REMARK 465 ALA S 697
REMARK 465 ASN S 698
REMARK 465 GLU S 699
REMARK 465 GLU S 700
REMARK 465 ILE S 701
REMARK 465 THR S 702
REMARK 465 GLU S 703
REMARK 465 GLU S 704
REMARK 465 GLN S 705
REMARK 465 ASN S 706
REMARK 465 GLY S 707
REMARK 465 THR S 708
REMARK 465 ALA S 709
REMARK 465 ASN S 710
REMARK 465 GLY S 711
REMARK 465 PHE S 712
REMARK 465 SER S 713
REMARK 465 GLU S 714
REMARK 465 ILE S 715
REMARK 465 ASN S 716
REMARK 465 SER S 717
REMARK 465 LYS S 718
REMARK 465 GLU S 719
REMARK 465 LYS S 720
REMARK 465 ALA S 721
REMARK 465 LEU S 722
REMARK 465 GLU S 723
REMARK 465 THR S 724
REMARK 465 ASP S 725
REMARK 465 MET T 535
REMARK 465 ASP T 536
REMARK 465 TYR T 537
REMARK 465 LYS T 538
REMARK 465 ASP T 539
REMARK 465 ASP T 540
REMARK 465 ASP T 541
REMARK 465 ASP T 542
REMARK 465 LYS T 543
REMARK 465 GLY T 544
REMARK 465 GLU T 545
REMARK 465 SER T 546
REMARK 465 GLU T 547
REMARK 465 ASP T 548
REMARK 465 GLY T 549
REMARK 465 GLU T 550
REMARK 465 VAL T 551
REMARK 465 GLU T 552
REMARK 465 GLN T 553
REMARK 465 GLN T 554
REMARK 465 ARG T 555
REMARK 465 THR T 556
REMARK 465 TYR T 557
REMARK 465 SER T 558
REMARK 465 SER T 559
REMARK 465 GLY T 560
REMARK 465 GLU T 689
REMARK 465 LYS T 690
REMARK 465 GLY T 691
REMARK 465 GLU T 692
REMARK 465 SER T 693
REMARK 465 ALA T 694
REMARK 465 SER T 695
REMARK 465 PRO T 696
REMARK 465 ALA T 697
REMARK 465 ASN T 698
REMARK 465 GLU T 699
REMARK 465 GLU T 700
REMARK 465 ILE T 701
REMARK 465 THR T 702
REMARK 465 GLU T 703
REMARK 465 GLU T 704
REMARK 465 GLN T 705
REMARK 465 ASN T 706
REMARK 465 GLY T 707
REMARK 465 THR T 708
REMARK 465 ALA T 709
REMARK 465 ASN T 710
REMARK 465 GLY T 711
REMARK 465 PHE T 712
REMARK 465 SER T 713
REMARK 465 GLU T 714
REMARK 465 ILE T 715
REMARK 465 ASN T 716
REMARK 465 SER T 717
REMARK 465 LYS T 718
REMARK 465 GLU T 719
REMARK 465 LYS T 720
REMARK 465 ALA T 721
REMARK 465 LEU T 722
REMARK 465 GLU T 723
REMARK 465 THR T 724
REMARK 465 ASP T 725
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 GLU A 198 99.90 -66.18
REMARK 500 ALA A 269 104.88 -51.88
REMARK 500 TYR A 306 49.49 -100.20
REMARK 500 TYR A 448 -57.42 -9.08
REMARK 500 ASP A 449 12.94 -140.20
REMARK 500 CYS A 463 -38.22 -37.33
REMARK 500 ASP A 531 -161.47 -108.42
REMARK 500 GLN A 565 -82.76 77.69
REMARK 500 HIS A 593 73.29 37.45
REMARK 500 CYS A 604 26.08 -145.98
REMARK 500 VAL A 621 -82.99 -111.00
REMARK 500 ILE A 638 -62.07 -100.50
REMARK 500 ALA B 269 105.06 -51.08
REMARK 500 TYR B 306 49.38 -99.10
REMARK 500 THR B 446 -67.58 -96.40
REMARK 500 TYR B 448 -74.38 -94.57
REMARK 500 ASP B 531 -162.19 -108.26
REMARK 500 GLN B 565 -82.79 77.60
REMARK 500 HIS B 593 73.32 38.22
REMARK 500 CYS B 604 26.75 -146.73
REMARK 500 VAL B 621 -84.66 -111.89
REMARK 500 ILE B 638 -62.28 -100.45
REMARK 500 SER E 104 -140.07 53.69
REMARK 500 LEU E 121 -63.68 -91.59
REMARK 500 ASN E 143 -74.36 -74.49
REMARK 500 HIS E 199 -5.41 93.49
REMARK 500 PHE E 285 148.85 175.40
REMARK 500 SER E 309 -157.54 -131.27
REMARK 500 CYS E 347 53.70 -144.81
REMARK 500 VAL E 379 57.77 -114.24
REMARK 500 SER F 104 -140.57 54.91
REMARK 500 LEU F 121 -63.79 -91.42
REMARK 500 ASN F 143 -75.80 -74.22
REMARK 500 HIS F 199 -7.09 94.38
REMARK 500 PHE F 285 147.27 176.85
REMARK 500 SER F 309 -157.72 -132.42
REMARK 500 CYS F 347 54.17 -144.53
REMARK 500 GLU F 378 57.48 -97.13
REMARK 500 LYS F 384 33.07 -95.29
REMARK 500 MET S 579 71.43 44.34
REMARK 500 GLU S 584 39.39 -82.32
REMARK 500 ASN S 651 72.02 53.64
REMARK 500 ASN T 562 -30.44 -144.08
REMARK 500 MET T 579 99.75 -6.03
REMARK 500 GLU T 580 37.36 -152.02
REMARK 500 ASP T 582 74.34 -118.36
REMARK 500 ASP T 583 45.55 -103.84
REMARK 500 GLU T 584 45.92 -93.06
REMARK 500 ASN T 651 72.81 53.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A9008 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 286 SG
REMARK 620 2 CYS A 289 SG 106.9
REMARK 620 3 CYS A 294 SG 110.1 104.0
REMARK 620 4 HIS A 297 ND1 102.3 122.7 110.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A9003 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 523 SG
REMARK 620 2 CYS A 536 SG 113.6
REMARK 620 3 CYS A 543 SG 108.5 112.4
REMARK 620 4 CYS A 547 SG 107.3 108.4 106.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A9004 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 523 SG
REMARK 620 2 HIS A 525 NE2 102.4
REMARK 620 3 CYS A 530 SG 107.7 105.6
REMARK 620 4 CYS A 534 SG 121.8 109.8 108.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A9002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 530 SG
REMARK 620 2 CYS A 543 SG 98.8
REMARK 620 3 CYS A 549 SG 112.7 110.2
REMARK 620 4 CYS A 553 SG 108.1 116.8 109.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A9005 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 560 SG
REMARK 620 2 CYS A 573 SG 102.0
REMARK 620 3 CYS A 580 SG 103.8 114.8
REMARK 620 4 CYS A 585 SG 109.7 104.5 120.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A9007 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 560 SG
REMARK 620 2 CYS A 562 SG 103.4
REMARK 620 3 CYS A 566 SG 106.5 108.8
REMARK 620 4 CYS A 571 SG 109.7 110.7 116.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A9006 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 566 SG
REMARK 620 2 CYS A 580 SG 104.4
REMARK 620 3 CYS A 588 SG 104.6 110.1
REMARK 620 4 CYS A 601 SG 118.3 109.8 109.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B9008 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 286 SG
REMARK 620 2 CYS B 289 SG 103.5
REMARK 620 3 CYS B 294 SG 109.4 107.2
REMARK 620 4 HIS B 297 ND1 97.5 125.3 112.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B9002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 523 SG
REMARK 620 2 HIS B 525 NE2 98.7
REMARK 620 3 CYS B 530 SG 111.7 103.8
REMARK 620 4 CYS B 534 SG 123.5 103.5 112.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B9003 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 523 SG
REMARK 620 2 CYS B 536 SG 112.1
REMARK 620 3 CYS B 543 SG 107.7 117.7
REMARK 620 4 CYS B 547 SG 102.1 109.3 106.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B9004 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 530 SG
REMARK 620 2 CYS B 543 SG 99.0
REMARK 620 3 CYS B 549 SG 112.6 111.7
REMARK 620 4 CYS B 553 SG 106.8 116.7 109.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B9005 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 560 SG
REMARK 620 2 CYS B 562 SG 98.6
REMARK 620 3 CYS B 566 SG 105.5 106.9
REMARK 620 4 CYS B 571 SG 111.7 108.7 122.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B9007 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 560 SG
REMARK 620 2 CYS B 573 SG 103.0
REMARK 620 3 CYS B 580 SG 104.2 115.9
REMARK 620 4 CYS B 585 SG 109.0 106.8 116.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B9006 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 566 SG
REMARK 620 2 CYS B 580 SG 99.7
REMARK 620 3 CYS B 588 SG 105.8 112.9
REMARK 620 4 CYS B 601 SG 119.2 115.9 103.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6BN A 9001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 9002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 9003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 9004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 9005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 9006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 9007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 9008
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6BN B 9001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 9002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 9003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 9004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 9005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 9006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 9007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 9008
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5IJ8 RELATED DB: PDB
DBREF 5IJ7 A 1 428 UNP G1KPH4 G1KPH4_ANOCA 4 332
DBREF 5IJ7 A 429 746 UNP Q15910 EZH2_HUMAN 390 707
DBREF 5IJ7 B 1 428 UNP G1KPH4 G1KPH4_ANOCA 4 332
DBREF 5IJ7 B 429 746 UNP Q15910 EZH2_HUMAN 390 707
DBREF 5IJ7 E 67 427 UNP O75530 EED_HUMAN 81 441
DBREF 5IJ7 F 67 427 UNP O75530 EED_HUMAN 81 441
DBREF 5IJ7 S 545 725 UNP Q15022 SUZ12_HUMAN 545 725
DBREF 5IJ7 T 545 725 UNP Q15022 SUZ12_HUMAN 545 725
SEQADV 5IJ7 A UNP Q15910 PRO 449 LINKER
SEQADV 5IJ7 A UNP Q15910 PRO 450 LINKER
SEQADV 5IJ7 A UNP Q15910 ARG 451 LINKER
SEQADV 5IJ7 A UNP Q15910 LYS 452 LINKER
SEQADV 5IJ7 LEU A 492 UNP Q15910 LYS 453 LINKER
SEQADV 5IJ7 GLY A 493 UNP Q15910 LYS 454 LINKER
SEQADV 5IJ7 GLY A 494 UNP Q15910 ARG 455 LINKER
SEQADV 5IJ7 GLY A 495 UNP Q15910 LYS 456 LINKER
SEQADV 5IJ7 GLY A 496 UNP Q15910 HIS 457 LINKER
SEQADV 5IJ7 SER A 497 UNP Q15910 ARG 458 LINKER
SEQADV 5IJ7 GLY A 498 UNP Q15910 LEU 459 LINKER
SEQADV 5IJ7 GLY A 499 UNP Q15910 TRP 460 LINKER
SEQADV 5IJ7 GLY A 500 UNP Q15910 ALA 461 LINKER
SEQADV 5IJ7 GLY A 501 UNP Q15910 ALA 462 LINKER
SEQADV 5IJ7 SER A 502 UNP Q15910 HIS 463 LINKER
SEQADV 5IJ7 GLY A 503 UNP Q15910 CYS 464 LINKER
SEQADV 5IJ7 GLY A 504 UNP Q15910 ARG 465 LINKER
SEQADV 5IJ7 GLY A 505 UNP Q15910 LYS 466 LINKER
SEQADV 5IJ7 GLY A 506 UNP Q15910 ILE 467 LINKER
SEQADV 5IJ7 SER A 507 UNP Q15910 GLN 468 LINKER
SEQADV 5IJ7 ALA A 508 UNP Q15910 LEU 469 LINKER
SEQADV 5IJ7 ALA A 509 UNP Q15910 LYS 470 LINKER
SEQADV 5IJ7 ALA A 510 UNP Q15910 LYS 471 LINKER
SEQADV 5IJ7 ASN A 532 UNP Q15910 SER 493 ENGINEERED MUTATION
SEQADV 5IJ7 B UNP Q15910 PRO 449 LINKER
SEQADV 5IJ7 B UNP Q15910 PRO 450 LINKER
SEQADV 5IJ7 B UNP Q15910 ARG 451 LINKER
SEQADV 5IJ7 B UNP Q15910 LYS 452 LINKER
SEQADV 5IJ7 LEU B 492 UNP Q15910 LYS 453 LINKER
SEQADV 5IJ7 GLY B 493 UNP Q15910 LYS 454 LINKER
SEQADV 5IJ7 GLY B 494 UNP Q15910 ARG 455 LINKER
SEQADV 5IJ7 GLY B 495 UNP Q15910 LYS 456 LINKER
SEQADV 5IJ7 GLY B 496 UNP Q15910 HIS 457 LINKER
SEQADV 5IJ7 SER B 497 UNP Q15910 ARG 458 LINKER
SEQADV 5IJ7 GLY B 498 UNP Q15910 LEU 459 LINKER
SEQADV 5IJ7 GLY B 499 UNP Q15910 TRP 460 LINKER
SEQADV 5IJ7 GLY B 500 UNP Q15910 ALA 461 LINKER
SEQADV 5IJ7 GLY B 501 UNP Q15910 ALA 462 LINKER
SEQADV 5IJ7 SER B 502 UNP Q15910 HIS 463 LINKER
SEQADV 5IJ7 GLY B 503 UNP Q15910 CYS 464 LINKER
SEQADV 5IJ7 GLY B 504 UNP Q15910 ARG 465 LINKER
SEQADV 5IJ7 GLY B 505 UNP Q15910 LYS 466 LINKER
SEQADV 5IJ7 GLY B 506 UNP Q15910 ILE 467 LINKER
SEQADV 5IJ7 SER B 507 UNP Q15910 GLN 468 LINKER
SEQADV 5IJ7 ALA B 508 UNP Q15910 LEU 469 LINKER
SEQADV 5IJ7 ALA B 509 UNP Q15910 LYS 470 LINKER
SEQADV 5IJ7 ALA B 510 UNP Q15910 LYS 471 LINKER
SEQADV 5IJ7 ASN B 532 UNP Q15910 SER 493 ENGINEERED MUTATION
SEQADV 5IJ7 MET E 66 UNP O75530 INITIATING METHIONINE
SEQADV 5IJ7 MET F 66 UNP O75530 INITIATING METHIONINE
SEQADV 5IJ7 MET S 535 UNP Q15022 INITIATING METHIONINE
SEQADV 5IJ7 ASP S 536 UNP Q15022 EXPRESSION TAG
SEQADV 5IJ7 TYR S 537 UNP Q15022 EXPRESSION TAG
SEQADV 5IJ7 LYS S 538 UNP Q15022 EXPRESSION TAG
SEQADV 5IJ7 ASP S 539 UNP Q15022 EXPRESSION TAG
SEQADV 5IJ7 ASP S 540 UNP Q15022 EXPRESSION TAG
SEQADV 5IJ7 ASP S 541 UNP Q15022 EXPRESSION TAG
SEQADV 5IJ7 ASP S 542 UNP Q15022 EXPRESSION TAG
SEQADV 5IJ7 LYS S 543 UNP Q15022 EXPRESSION TAG
SEQADV 5IJ7 GLY S 544 UNP Q15022 EXPRESSION TAG
SEQADV 5IJ7 ASP S 583 UNP Q15022 SER 583 ENGINEERED MUTATION
SEQADV 5IJ7 MET T 535 UNP Q15022 INITIATING METHIONINE
SEQADV 5IJ7 ASP T 536 UNP Q15022 EXPRESSION TAG
SEQADV 5IJ7 TYR T 537 UNP Q15022 EXPRESSION TAG
SEQADV 5IJ7 LYS T 538 UNP Q15022 EXPRESSION TAG
SEQADV 5IJ7 ASP T 539 UNP Q15022 EXPRESSION TAG
SEQADV 5IJ7 ASP T 540 UNP Q15022 EXPRESSION TAG
SEQADV 5IJ7 ASP T 541 UNP Q15022 EXPRESSION TAG
SEQADV 5IJ7 ASP T 542 UNP Q15022 EXPRESSION TAG
SEQADV 5IJ7 LYS T 543 UNP Q15022 EXPRESSION TAG
SEQADV 5IJ7 GLY T 544 UNP Q15022 EXPRESSION TAG
SEQADV 5IJ7 ASP T 583 UNP Q15022 SER 583 ENGINEERED MUTATION
SEQRES 1 A 643 MET GLY GLN THR GLY LYS LYS SER GLU LYS GLY PRO ILE
SEQRES 2 A 643 CYS TRP ARG LYS ARG VAL LYS SER GLU TYR MET ARG LEU
SEQRES 3 A 643 ARG GLN LEU LYS ARG PHE ARG ARG ALA ASP GLU VAL LYS
SEQRES 4 A 643 SER MET PHE ASN SER ASN ARG GLN LYS ILE GLN GLU ARG
SEQRES 5 A 643 THR GLU ILE LEU ASN GLN GLU TRP LYS GLN ARG ARG ILE
SEQRES 6 A 643 GLN PRO VAL HIS ILE MET THR SER VAL SER SER LEU ARG
SEQRES 7 A 643 GLY THR ARG GLU CYS SER VAL THR SER ASP LEU ASP PHE
SEQRES 8 A 643 PRO LYS GLN VAL ILE PRO LEU LYS THR LEU ASN ALA VAL
SEQRES 9 A 643 ALA SER VAL PRO ILE MET TYR SER TRP SER PRO LEU GLN
SEQRES 10 A 643 GLN ASN PHE MET VAL GLU ASP GLU THR VAL LEU HIS ASN
SEQRES 11 A 643 ILE PRO TYR MET GLY ASP GLU VAL LEU ASP GLN ASP GLY
SEQRES 12 A 643 THR PHE ILE GLU GLU LEU ILE LYS ASN TYR ASP GLY LYS
SEQRES 13 A 643 VAL HIS GLY ASP ARG GLU CYS GLY PHE ILE ASN ASP GLU
SEQRES 14 A 643 ILE PHE VAL GLU LEU VAL ASN ALA LEU GLY GLN LEU ASP
SEQRES 15 A 643 ARG ARG ASP GLU LYS GLN LYS ASN GLN GLU SER ASN GLN
SEQRES 16 A 643 ILE ASP LYS GLU SER HIS PRO PRO ARG LYS PHE PRO SER
SEQRES 17 A 643 ASP LYS ILE PHE GLU ALA ILE SER SER MET PHE PRO ASP
SEQRES 18 A 643 LYS GLY THR ALA GLU GLU LEU LYS GLU LYS TYR LYS GLU
SEQRES 19 A 643 LEU THR GLU GLN GLN LEU PRO GLY ALA LEU PRO PRO GLU
SEQRES 20 A 643 CYS THR PRO ASN ILE ASP GLY PRO ASN ALA LYS SER VAL
SEQRES 21 A 643 GLN ARG GLU GLN SER LEU HIS SER PHE HIS THR LEU PHE
SEQRES 22 A 643 CYS ARG ARG CYS PHE LYS TYR ASP CYS PHE LEU HIS PRO
SEQRES 23 A 643 PHE HIS ALA THR PRO ASN THR TYR LYS ARG LYS ASN THR
SEQRES 24 A 643 GLU MET ALA ILE ASP ASN LYS PRO CYS GLY PRO HIS CYS
SEQRES 25 A 643 TYR GLN HIS LEU GLU GLY ALA LYS GLU PHE ALA ALA ALA
SEQRES 26 A 643 LEU THR ALA GLU ASN VAL GLU TRP SER GLY ALA GLU ALA
SEQRES 27 A 643 SER MET PHE ARG VAL LEU ILE GLY THR TYR TYR ASP ASN
SEQRES 28 A 643 PHE CYS ALA ILE ALA ARG LEU ILE GLY THR LYS THR CYS
SEQRES 29 A 643 ARG GLN VAL TYR GLU PHE ARG VAL LYS GLU SER SER ILE
SEQRES 30 A 643 ILE ALA PRO ALA PRO ALA GLU ASP VAL ASP THR LEU GLY
SEQRES 31 A 643 GLY GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY GLY
SEQRES 32 A 643 SER ALA ALA ALA ASP GLY SER SER ASN HIS VAL TYR ASN
SEQRES 33 A 643 TYR GLN PRO CYS ASP HIS PRO ARG GLN PRO CYS ASP ASN
SEQRES 34 A 643 SER CYS PRO CYS VAL ILE ALA GLN ASN PHE CYS GLU LYS
SEQRES 35 A 643 PHE CYS GLN CYS SER SER GLU CYS GLN ASN ARG PHE PRO
SEQRES 36 A 643 GLY CYS ARG CYS LYS ALA GLN CYS ASN THR LYS GLN CYS
SEQRES 37 A 643 PRO CYS TYR LEU ALA VAL ARG GLU CYS ASP PRO ASP LEU
SEQRES 38 A 643 CYS LEU THR CYS GLY ALA ALA ASP HIS TRP ASP SER LYS
SEQRES 39 A 643 ASN VAL SER CYS LYS ASN CYS SER ILE GLN ARG GLY SER
SEQRES 40 A 643 LYS LYS HIS LEU LEU LEU ALA PRO SER ASP VAL ALA GLY
SEQRES 41 A 643 TRP GLY ILE PHE ILE LYS ASP PRO VAL GLN LYS ASN GLU
SEQRES 42 A 643 PHE ILE SER GLU TYR CYS GLY GLU ILE ILE SER GLN ASP
SEQRES 43 A 643 GLU ALA ASP ARG ARG GLY LYS VAL TYR ASP LYS TYR MET
SEQRES 44 A 643 CYS SER PHE LEU PHE ASN LEU ASN ASN ASP PHE VAL VAL
SEQRES 45 A 643 ASP ALA THR ARG LYS GLY ASN LYS ILE ARG PHE ALA ASN
SEQRES 46 A 643 HIS SER VAL ASN PRO ASN CYS TYR ALA LYS VAL MET MET
SEQRES 47 A 643 VAL ASN GLY ASP HIS ARG ILE GLY ILE PHE ALA LYS ARG
SEQRES 48 A 643 ALA ILE GLN THR GLY GLU GLU LEU PHE PHE ASP TYR ARG
SEQRES 49 A 643 TYR SER GLN ALA ASP ALA LEU LYS TYR VAL GLY ILE GLU
SEQRES 50 A 643 ARG GLU MET GLU ILE PRO
SEQRES 1 B 643 MET GLY GLN THR GLY LYS LYS SER GLU LYS GLY PRO ILE
SEQRES 2 B 643 CYS TRP ARG LYS ARG VAL LYS SER GLU TYR MET ARG LEU
SEQRES 3 B 643 ARG GLN LEU LYS ARG PHE ARG ARG ALA ASP GLU VAL LYS
SEQRES 4 B 643 SER MET PHE ASN SER ASN ARG GLN LYS ILE GLN GLU ARG
SEQRES 5 B 643 THR GLU ILE LEU ASN GLN GLU TRP LYS GLN ARG ARG ILE
SEQRES 6 B 643 GLN PRO VAL HIS ILE MET THR SER VAL SER SER LEU ARG
SEQRES 7 B 643 GLY THR ARG GLU CYS SER VAL THR SER ASP LEU ASP PHE
SEQRES 8 B 643 PRO LYS GLN VAL ILE PRO LEU LYS THR LEU ASN ALA VAL
SEQRES 9 B 643 ALA SER VAL PRO ILE MET TYR SER TRP SER PRO LEU GLN
SEQRES 10 B 643 GLN ASN PHE MET VAL GLU ASP GLU THR VAL LEU HIS ASN
SEQRES 11 B 643 ILE PRO TYR MET GLY ASP GLU VAL LEU ASP GLN ASP GLY
SEQRES 12 B 643 THR PHE ILE GLU GLU LEU ILE LYS ASN TYR ASP GLY LYS
SEQRES 13 B 643 VAL HIS GLY ASP ARG GLU CYS GLY PHE ILE ASN ASP GLU
SEQRES 14 B 643 ILE PHE VAL GLU LEU VAL ASN ALA LEU GLY GLN LEU ASP
SEQRES 15 B 643 ARG ARG ASP GLU LYS GLN LYS ASN GLN GLU SER ASN GLN
SEQRES 16 B 643 ILE ASP LYS GLU SER HIS PRO PRO ARG LYS PHE PRO SER
SEQRES 17 B 643 ASP LYS ILE PHE GLU ALA ILE SER SER MET PHE PRO ASP
SEQRES 18 B 643 LYS GLY THR ALA GLU GLU LEU LYS GLU LYS TYR LYS GLU
SEQRES 19 B 643 LEU THR GLU GLN GLN LEU PRO GLY ALA LEU PRO PRO GLU
SEQRES 20 B 643 CYS THR PRO ASN ILE ASP GLY PRO ASN ALA LYS SER VAL
SEQRES 21 B 643 GLN ARG GLU GLN SER LEU HIS SER PHE HIS THR LEU PHE
SEQRES 22 B 643 CYS ARG ARG CYS PHE LYS TYR ASP CYS PHE LEU HIS PRO
SEQRES 23 B 643 PHE HIS ALA THR PRO ASN THR TYR LYS ARG LYS ASN THR
SEQRES 24 B 643 GLU MET ALA ILE ASP ASN LYS PRO CYS GLY PRO HIS CYS
SEQRES 25 B 643 TYR GLN HIS LEU GLU GLY ALA LYS GLU PHE ALA ALA ALA
SEQRES 26 B 643 LEU THR ALA GLU ASN VAL GLU TRP SER GLY ALA GLU ALA
SEQRES 27 B 643 SER MET PHE ARG VAL LEU ILE GLY THR TYR TYR ASP ASN
SEQRES 28 B 643 PHE CYS ALA ILE ALA ARG LEU ILE GLY THR LYS THR CYS
SEQRES 29 B 643 ARG GLN VAL TYR GLU PHE ARG VAL LYS GLU SER SER ILE
SEQRES 30 B 643 ILE ALA PRO ALA PRO ALA GLU ASP VAL ASP THR LEU GLY
SEQRES 31 B 643 GLY GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY GLY
SEQRES 32 B 643 SER ALA ALA ALA ASP GLY SER SER ASN HIS VAL TYR ASN
SEQRES 33 B 643 TYR GLN PRO CYS ASP HIS PRO ARG GLN PRO CYS ASP ASN
SEQRES 34 B 643 SER CYS PRO CYS VAL ILE ALA GLN ASN PHE CYS GLU LYS
SEQRES 35 B 643 PHE CYS GLN CYS SER SER GLU CYS GLN ASN ARG PHE PRO
SEQRES 36 B 643 GLY CYS ARG CYS LYS ALA GLN CYS ASN THR LYS GLN CYS
SEQRES 37 B 643 PRO CYS TYR LEU ALA VAL ARG GLU CYS ASP PRO ASP LEU
SEQRES 38 B 643 CYS LEU THR CYS GLY ALA ALA ASP HIS TRP ASP SER LYS
SEQRES 39 B 643 ASN VAL SER CYS LYS ASN CYS SER ILE GLN ARG GLY SER
SEQRES 40 B 643 LYS LYS HIS LEU LEU LEU ALA PRO SER ASP VAL ALA GLY
SEQRES 41 B 643 TRP GLY ILE PHE ILE LYS ASP PRO VAL GLN LYS ASN GLU
SEQRES 42 B 643 PHE ILE SER GLU TYR CYS GLY GLU ILE ILE SER GLN ASP
SEQRES 43 B 643 GLU ALA ASP ARG ARG GLY LYS VAL TYR ASP LYS TYR MET
SEQRES 44 B 643 CYS SER PHE LEU PHE ASN LEU ASN ASN ASP PHE VAL VAL
SEQRES 45 B 643 ASP ALA THR ARG LYS GLY ASN LYS ILE ARG PHE ALA ASN
SEQRES 46 B 643 HIS SER VAL ASN PRO ASN CYS TYR ALA LYS VAL MET MET
SEQRES 47 B 643 VAL ASN GLY ASP HIS ARG ILE GLY ILE PHE ALA LYS ARG
SEQRES 48 B 643 ALA ILE GLN THR GLY GLU GLU LEU PHE PHE ASP TYR ARG
SEQRES 49 B 643 TYR SER GLN ALA ASP ALA LEU LYS TYR VAL GLY ILE GLU
SEQRES 50 B 643 ARG GLU MET GLU ILE PRO
SEQRES 1 E 362 MET SER PHE LYS CYS VAL ASN SER LEU LYS GLU ASP HIS
SEQRES 2 E 362 ASN GLN PRO LEU PHE GLY VAL GLN PHE ASN TRP HIS SER
SEQRES 3 E 362 LYS GLU GLY ASP PRO LEU VAL PHE ALA THR VAL GLY SER
SEQRES 4 E 362 ASN ARG VAL THR LEU TYR GLU CYS HIS SER GLN GLY GLU
SEQRES 5 E 362 ILE ARG LEU LEU GLN SER TYR VAL ASP ALA ASP ALA ASP
SEQRES 6 E 362 GLU ASN PHE TYR THR CYS ALA TRP THR TYR ASP SER ASN
SEQRES 7 E 362 THR SER HIS PRO LEU LEU ALA VAL ALA GLY SER ARG GLY
SEQRES 8 E 362 ILE ILE ARG ILE ILE ASN PRO ILE THR MET GLN CYS ILE
SEQRES 9 E 362 LYS HIS TYR VAL GLY HIS GLY ASN ALA ILE ASN GLU LEU
SEQRES 10 E 362 LYS PHE HIS PRO ARG ASP PRO ASN LEU LEU LEU SER VAL
SEQRES 11 E 362 SER LYS ASP HIS ALA LEU ARG LEU TRP ASN ILE GLN THR
SEQRES 12 E 362 ASP THR LEU VAL ALA ILE PHE GLY GLY VAL GLU GLY HIS
SEQRES 13 E 362 ARG ASP GLU VAL LEU SER ALA ASP TYR ASP LEU LEU GLY
SEQRES 14 E 362 GLU LYS ILE MET SER CYS GLY MET ASP HIS SER LEU LYS
SEQRES 15 E 362 LEU TRP ARG ILE ASN SER LYS ARG MET MET ASN ALA ILE
SEQRES 16 E 362 LYS GLU SER TYR ASP TYR ASN PRO ASN LYS THR ASN ARG
SEQRES 17 E 362 PRO PHE ILE SER GLN LYS ILE HIS PHE PRO ASP PHE SER
SEQRES 18 E 362 THR ARG ASP ILE HIS ARG ASN TYR VAL ASP CYS VAL ARG
SEQRES 19 E 362 TRP LEU GLY ASP LEU ILE LEU SER LYS SER CYS GLU ASN
SEQRES 20 E 362 ALA ILE VAL CYS TRP LYS PRO GLY LYS MET GLU ASP ASP
SEQRES 21 E 362 ILE ASP LYS ILE LYS PRO SER GLU SER ASN VAL THR ILE
SEQRES 22 E 362 LEU GLY ARG PHE ASP TYR SER GLN CYS ASP ILE TRP TYR
SEQRES 23 E 362 MET ARG PHE SER MET ASP PHE TRP GLN LYS MET LEU ALA
SEQRES 24 E 362 LEU GLY ASN GLN VAL GLY LYS LEU TYR VAL TRP ASP LEU
SEQRES 25 E 362 GLU VAL GLU ASP PRO HIS LYS ALA LYS CYS THR THR LEU
SEQRES 26 E 362 THR HIS HIS LYS CYS GLY ALA ALA ILE ARG GLN THR SER
SEQRES 27 E 362 PHE SER ARG ASP SER SER ILE LEU ILE ALA VAL CYS ASP
SEQRES 28 E 362 ASP ALA SER ILE TRP ARG TRP ASP ARG LEU ARG
SEQRES 1 F 362 MET SER PHE LYS CYS VAL ASN SER LEU LYS GLU ASP HIS
SEQRES 2 F 362 ASN GLN PRO LEU PHE GLY VAL GLN PHE ASN TRP HIS SER
SEQRES 3 F 362 LYS GLU GLY ASP PRO LEU VAL PHE ALA THR VAL GLY SER
SEQRES 4 F 362 ASN ARG VAL THR LEU TYR GLU CYS HIS SER GLN GLY GLU
SEQRES 5 F 362 ILE ARG LEU LEU GLN SER TYR VAL ASP ALA ASP ALA ASP
SEQRES 6 F 362 GLU ASN PHE TYR THR CYS ALA TRP THR TYR ASP SER ASN
SEQRES 7 F 362 THR SER HIS PRO LEU LEU ALA VAL ALA GLY SER ARG GLY
SEQRES 8 F 362 ILE ILE ARG ILE ILE ASN PRO ILE THR MET GLN CYS ILE
SEQRES 9 F 362 LYS HIS TYR VAL GLY HIS GLY ASN ALA ILE ASN GLU LEU
SEQRES 10 F 362 LYS PHE HIS PRO ARG ASP PRO ASN LEU LEU LEU SER VAL
SEQRES 11 F 362 SER LYS ASP HIS ALA LEU ARG LEU TRP ASN ILE GLN THR
SEQRES 12 F 362 ASP THR LEU VAL ALA ILE PHE GLY GLY VAL GLU GLY HIS
SEQRES 13 F 362 ARG ASP GLU VAL LEU SER ALA ASP TYR ASP LEU LEU GLY
SEQRES 14 F 362 GLU LYS ILE MET SER CYS GLY MET ASP HIS SER LEU LYS
SEQRES 15 F 362 LEU TRP ARG ILE ASN SER LYS ARG MET MET ASN ALA ILE
SEQRES 16 F 362 LYS GLU SER TYR ASP TYR ASN PRO ASN LYS THR ASN ARG
SEQRES 17 F 362 PRO PHE ILE SER GLN LYS ILE HIS PHE PRO ASP PHE SER
SEQRES 18 F 362 THR ARG ASP ILE HIS ARG ASN TYR VAL ASP CYS VAL ARG
SEQRES 19 F 362 TRP LEU GLY ASP LEU ILE LEU SER LYS SER CYS GLU ASN
SEQRES 20 F 362 ALA ILE VAL CYS TRP LYS PRO GLY LYS MET GLU ASP ASP
SEQRES 21 F 362 ILE ASP LYS ILE LYS PRO SER GLU SER ASN VAL THR ILE
SEQRES 22 F 362 LEU GLY ARG PHE ASP TYR SER GLN CYS ASP ILE TRP TYR
SEQRES 23 F 362 MET ARG PHE SER MET ASP PHE TRP GLN LYS MET LEU ALA
SEQRES 24 F 362 LEU GLY ASN GLN VAL GLY LYS LEU TYR VAL TRP ASP LEU
SEQRES 25 F 362 GLU VAL GLU ASP PRO HIS LYS ALA LYS CYS THR THR LEU
SEQRES 26 F 362 THR HIS HIS LYS CYS GLY ALA ALA ILE ARG GLN THR SER
SEQRES 27 F 362 PHE SER ARG ASP SER SER ILE LEU ILE ALA VAL CYS ASP
SEQRES 28 F 362 ASP ALA SER ILE TRP ARG TRP ASP ARG LEU ARG
SEQRES 1 S 191 MET ASP TYR LYS ASP ASP ASP ASP LYS GLY GLU SER GLU
SEQRES 2 S 191 ASP GLY GLU VAL GLU GLN GLN ARG THR TYR SER SER GLY
SEQRES 3 S 191 HIS ASN ARG LEU TYR PHE HIS SER ASP THR CYS LEU PRO
SEQRES 4 S 191 LEU ARG PRO GLN GLU MET GLU VAL ASP ASP GLU ASP GLU
SEQRES 5 S 191 LYS ASP PRO GLU TRP LEU ARG GLU LYS THR ILE THR GLN
SEQRES 6 S 191 ILE GLU GLU PHE SER ASP VAL ASN GLU GLY GLU LYS GLU
SEQRES 7 S 191 VAL MET LYS LEU TRP ASN LEU HIS VAL MET LYS HIS GLY
SEQRES 8 S 191 PHE ILE ALA ASP ASN GLN MET ASN HIS ALA CYS MET LEU
SEQRES 9 S 191 PHE VAL GLU ASN TYR GLY GLN LYS ILE ILE LYS LYS ASN
SEQRES 10 S 191 LEU CYS ARG ASN PHE MET LEU HIS LEU VAL SER MET HIS
SEQRES 11 S 191 ASP PHE ASN LEU ILE SER ILE MET SER ILE ASP LYS ALA
SEQRES 12 S 191 VAL THR LYS LEU ARG GLU MET GLN GLN LYS LEU GLU LYS
SEQRES 13 S 191 GLY GLU SER ALA SER PRO ALA ASN GLU GLU ILE THR GLU
SEQRES 14 S 191 GLU GLN ASN GLY THR ALA ASN GLY PHE SER GLU ILE ASN
SEQRES 15 S 191 SER LYS GLU LYS ALA LEU GLU THR ASP
SEQRES 1 T 191 MET ASP TYR LYS ASP ASP ASP ASP LYS GLY GLU SER GLU
SEQRES 2 T 191 ASP GLY GLU VAL GLU GLN GLN ARG THR TYR SER SER GLY
SEQRES 3 T 191 HIS ASN ARG LEU TYR PHE HIS SER ASP THR CYS LEU PRO
SEQRES 4 T 191 LEU ARG PRO GLN GLU MET GLU VAL ASP ASP GLU ASP GLU
SEQRES 5 T 191 LYS ASP PRO GLU TRP LEU ARG GLU LYS THR ILE THR GLN
SEQRES 6 T 191 ILE GLU GLU PHE SER ASP VAL ASN GLU GLY GLU LYS GLU
SEQRES 7 T 191 VAL MET LYS LEU TRP ASN LEU HIS VAL MET LYS HIS GLY
SEQRES 8 T 191 PHE ILE ALA ASP ASN GLN MET ASN HIS ALA CYS MET LEU
SEQRES 9 T 191 PHE VAL GLU ASN TYR GLY GLN LYS ILE ILE LYS LYS ASN
SEQRES 10 T 191 LEU CYS ARG ASN PHE MET LEU HIS LEU VAL SER MET HIS
SEQRES 11 T 191 ASP PHE ASN LEU ILE SER ILE MET SER ILE ASP LYS ALA
SEQRES 12 T 191 VAL THR LYS LEU ARG GLU MET GLN GLN LYS LEU GLU LYS
SEQRES 13 T 191 GLY GLU SER ALA SER PRO ALA ASN GLU GLU ILE THR GLU
SEQRES 14 T 191 GLU GLN ASN GLY THR ALA ASN GLY PHE SER GLU ILE ASN
SEQRES 15 T 191 SER LYS GLU LYS ALA LEU GLU THR ASP
HET 6BN A9001 36
HET ZN A9002 1
HET ZN A9003 1
HET ZN A9004 1
HET ZN A9005 1
HET ZN A9006 1
HET ZN A9007 1
HET ZN A9008 1
HET 6BN B9001 36
HET ZN B9002 1
HET ZN B9003 1
HET ZN B9004 1
HET ZN B9005 1
HET ZN B9006 1
HET ZN B9007 1
HET ZN B9008 1
HETNAM 6BN 5,8-DICHLORO-2-[(4-ETHYL-6-METHYL-2-OXO-1,2-
HETNAM 2 6BN DIHYDROPYRIDIN-3-YL)METHYL]-7-({1-[(2R)-2-
HETNAM 3 6BN HYDROXYPROPANOYL]PIPERIDIN-4-YL}OXY)-3,4-
HETNAM 4 6BN DIHYDROISOQUINOLIN-1(2H)-ONE
HETNAM ZN ZINC ION
FORMUL 7 6BN 2(C26 H31 CL2 N3 O5)
FORMUL 8 ZN 14(ZN 2+)
FORMUL 23 HOH *36(H2 O)
HELIX 1 AA1 GLY A 11 GLN A 62 1 52
HELIX 2 AA2 ASN A 167 GLU A 198 1 20
HELIX 3 AA3 SER A 220 PHE A 231 1 12
HELIX 4 AA4 PRO A 232 GLY A 235 5 4
HELIX 5 AA5 THR A 236 LYS A 245 1 10
HELIX 6 AA6 GLN A 273 LEU A 284 1 12
HELIX 7 AA7 THR A 302 LYS A 307 5 6
HELIX 8 AA8 SER A 433 ILE A 444 1 12
HELIX 9 AA9 ASN A 450 GLY A 459 1 10
HELIX 10 AB1 THR A 462 LYS A 472 1 11
HELIX 11 AB2 CYS A 534 ALA A 539 1 6
HELIX 12 AB3 CYS A 571 ALA A 576 1 6
HELIX 13 AB4 CYS A 604 GLY A 609 1 6
HELIX 14 AB5 GLN A 648 TYR A 661 1 14
HELIX 15 AB6 LYS A 683 ALA A 687 5 5
HELIX 16 AB7 ASP A 725 ALA A 731 1 7
HELIX 17 AB8 GLY B 11 GLN B 62 1 52
HELIX 18 AB9 ASN B 167 ASP B 197 1 19
HELIX 19 AC1 SER B 220 PHE B 231 1 12
HELIX 20 AC2 THR B 236 THR B 248 1 13
HELIX 21 AC3 GLN B 273 LEU B 284 1 12
HELIX 22 AC4 THR B 302 LYS B 307 5 6
HELIX 23 AC5 SER B 433 TYR B 447 1 15
HELIX 24 AC6 ASN B 450 GLY B 459 1 10
HELIX 25 AC7 THR B 462 LYS B 472 1 11
HELIX 26 AC8 CYS B 534 ALA B 539 1 6
HELIX 27 AC9 CYS B 571 ALA B 576 1 6
HELIX 28 AD1 CYS B 604 GLY B 609 1 6
HELIX 29 AD2 GLN B 648 TYR B 661 1 14
HELIX 30 AD3 LYS B 683 ALA B 687 5 5
HELIX 31 AD4 ASP B 725 ALA B 731 1 7
HELIX 32 AD5 SER E 253 TYR E 266 1 14
HELIX 33 AD6 ASP E 325 ILE E 329 5 5
HELIX 34 AD7 SER F 253 TYR F 266 1 14
HELIX 35 AD8 ASP F 325 ILE F 329 5 5
HELIX 36 AD9 ARG S 575 MET S 579 5 5
HELIX 37 AE1 PRO S 589 GLU S 602 1 14
HELIX 38 AE2 ASN S 607 GLY S 625 1 19
HELIX 39 AE3 ALA S 628 ASN S 630 5 3
HELIX 40 AE4 GLN S 631 LYS S 650 1 20
HELIX 41 AE5 LEU S 652 PHE S 666 1 15
HELIX 42 AE6 SER S 670 LYS S 687 1 18
HELIX 43 AE7 ARG T 575 MET T 579 5 5
HELIX 44 AE8 PRO T 589 GLU T 602 1 14
HELIX 45 AE9 ASN T 607 GLY T 625 1 19
HELIX 46 AF1 ALA T 628 ASN T 630 5 3
HELIX 47 AF2 GLN T 631 LYS T 650 1 20
HELIX 48 AF3 LEU T 652 PHE T 666 1 15
HELIX 49 AF4 SER T 670 LYS T 687 1 18
SHEET 1 AA1 6 GLN A 94 PRO A 97 0
SHEET 2 AA1 6 GLU A 82 SER A 87 -1 N CYS A 83 O ILE A 96
SHEET 3 AA1 6 PHE E 68 GLU E 76 -1 O LYS E 75 N THR A 86
SHEET 4 AA1 6 SER E 419 ARG E 425 -1 O ARG E 422 N ASN E 72
SHEET 5 AA1 6 ILE E 410 CYS E 415 -1 N ALA E 413 O TRP E 421
SHEET 6 AA1 6 ILE E 399 PHE E 404 -1 N SER E 403 O ILE E 412
SHEET 1 AA2 5 LYS A 99 LEU A 101 0
SHEET 2 AA2 5 ILE E 118 ASP E 126 1 O VAL E 125 N LEU A 101
SHEET 3 AA2 5 ARG E 106 CYS E 112 -1 N GLU E 111 O ARG E 119
SHEET 4 AA2 5 VAL E 98 GLY E 103 -1 N GLY E 103 O ARG E 106
SHEET 5 AA2 5 LEU E 82 PHE E 87 -1 N GLN E 86 O ALA E 100
SHEET 1 AA3 4 SER A 114 PRO A 115 0
SHEET 2 AA3 4 PHE A 673 GLY A 681 1 O GLY A 681 N SER A 114
SHEET 3 AA3 4 GLY A 643 SER A 647 -1 N ILE A 646 O VAL A 674
SHEET 4 AA3 4 PHE A 120 MET A 121 1 N PHE A 120 O GLY A 643
SHEET 1 AA4 3 SER A 114 PRO A 115 0
SHEET 2 AA4 3 PHE A 673 GLY A 681 1 O GLY A 681 N SER A 114
SHEET 3 AA4 3 LEU A 666 ASN A 668 -1 N PHE A 667 O VAL A 675
SHEET 1 AA5 2 PHE A 285 CYS A 286 0
SHEET 2 AA5 2 LYS A 291 TYR A 292 -1 O LYS A 291 N CYS A 286
SHEET 1 AA6 2 LEU A 614 PRO A 618 0
SHEET 2 AA6 2 TRP A 624 ILE A 628 -1 O PHE A 627 N LEU A 615
SHEET 1 AA7 3 PHE A 637 GLU A 640 0
SHEET 2 AA7 3 ASP A 705 ALA A 712 -1 O ILE A 710 N ILE A 638
SHEET 3 AA7 3 CYS A 695 VAL A 702 -1 N VAL A 702 O ASP A 705
SHEET 1 AA8 2 ASN A 688 HIS A 689 0
SHEET 2 AA8 2 PHE A 723 PHE A 724 1 O PHE A 724 N ASN A 688
SHEET 1 AA9 6 GLN B 94 PRO B 97 0
SHEET 2 AA9 6 GLU B 82 SER B 87 -1 N CYS B 83 O ILE B 96
SHEET 3 AA9 6 PHE F 68 GLU F 76 -1 O LYS F 75 N THR B 86
SHEET 4 AA9 6 SER F 419 ARG F 425 -1 O ARG F 422 N ASN F 72
SHEET 5 AA9 6 ILE F 410 CYS F 415 -1 N ALA F 413 O TRP F 421
SHEET 6 AA9 6 ILE F 399 PHE F 404 -1 N SER F 403 O ILE F 412
SHEET 1 AB1 5 LYS B 99 LEU B 101 0
SHEET 2 AB1 5 ILE F 118 ASP F 126 1 O VAL F 125 N LEU B 101
SHEET 3 AB1 5 ARG F 106 CYS F 112 -1 N GLU F 111 O ARG F 119
SHEET 4 AB1 5 VAL F 98 GLY F 103 -1 N PHE F 99 O TYR F 110
SHEET 5 AB1 5 LEU F 82 PHE F 87 -1 N GLN F 86 O ALA F 100
SHEET 1 AB2 4 SER B 114 PRO B 115 0
SHEET 2 AB2 4 PHE B 673 GLY B 681 1 O GLY B 681 N SER B 114
SHEET 3 AB2 4 GLY B 643 SER B 647 -1 N ILE B 646 O VAL B 674
SHEET 4 AB2 4 PHE B 120 MET B 121 1 N PHE B 120 O GLY B 643
SHEET 1 AB3 3 SER B 114 PRO B 115 0
SHEET 2 AB3 3 PHE B 673 GLY B 681 1 O GLY B 681 N SER B 114
SHEET 3 AB3 3 LEU B 666 ASN B 668 -1 N PHE B 667 O VAL B 675
SHEET 1 AB4 2 PHE B 285 CYS B 286 0
SHEET 2 AB4 2 LYS B 291 TYR B 292 -1 O LYS B 291 N CYS B 286
SHEET 1 AB5 2 LEU B 614 PRO B 618 0
SHEET 2 AB5 2 TRP B 624 ILE B 628 -1 O PHE B 627 N LEU B 615
SHEET 1 AB6 3 PHE B 637 GLU B 640 0
SHEET 2 AB6 3 ASP B 705 ALA B 712 -1 O ILE B 710 N ILE B 638
SHEET 3 AB6 3 CYS B 695 VAL B 702 -1 N VAL B 702 O ASP B 705
SHEET 1 AB7 2 ASN B 688 HIS B 689 0
SHEET 2 AB7 2 PHE B 723 PHE B 724 1 O PHE B 724 N ASN B 688
SHEET 1 AB8 4 PHE E 133 TYR E 140 0
SHEET 2 AB8 4 PRO E 147 GLY E 153 -1 O ALA E 150 N ALA E 137
SHEET 3 AB8 4 ILE E 158 ASN E 162 -1 O ILE E 161 N LEU E 149
SHEET 4 AB8 4 GLN E 167 TYR E 172 -1 O GLN E 167 N ASN E 162
SHEET 1 AB9 5 ILE E 179 PHE E 184 0
SHEET 2 AB9 5 LEU E 191 SER E 196 -1 O LEU E 193 N LYS E 183
SHEET 3 AB9 5 LEU E 201 ASN E 205 -1 O TRP E 204 N LEU E 192
SHEET 4 AB9 5 THR E 210 PHE E 215 -1 O THR E 210 N ASN E 205
SHEET 5 AB9 5 GLN E 278 ILE E 280 1 O GLN E 278 N ILE E 214
SHEET 1 AC1 4 VAL E 225 TYR E 230 0
SHEET 2 AC1 4 LYS E 236 GLY E 241 -1 O CYS E 240 N SER E 227
SHEET 3 AC1 4 LEU E 246 ARG E 250 -1 O LYS E 247 N SER E 239
SHEET 4 AC1 4 PHE E 285 THR E 287 -1 O PHE E 285 N LEU E 248
SHEET 1 AC2 4 CYS E 297 LEU E 301 0
SHEET 2 AC2 4 LEU E 304 LYS E 308 -1 O LEU E 306 N ARG E 299
SHEET 3 AC2 4 ALA E 313 PRO E 319 -1 O VAL E 315 N SER E 307
SHEET 4 AC2 4 VAL E 336 ASP E 343 -1 O GLY E 340 N CYS E 316
SHEET 1 AC3 4 SER E 355 MET E 356 0
SHEET 2 AC3 4 MET E 362 GLY E 366 -1 O ALA E 364 N SER E 355
SHEET 3 AC3 4 LEU E 372 ASP E 376 -1 O TYR E 373 N LEU E 365
SHEET 4 AC3 4 CYS E 387 LEU E 390 -1 O LEU E 390 N LEU E 372
SHEET 1 AC4 4 PHE F 133 TYR F 140 0
SHEET 2 AC4 4 PRO F 147 GLY F 153 -1 O ALA F 150 N ALA F 137
SHEET 3 AC4 4 ILE F 158 ASN F 162 -1 O ILE F 161 N LEU F 149
SHEET 4 AC4 4 GLN F 167 TYR F 172 -1 O LYS F 170 N ILE F 160
SHEET 1 AC5 5 ILE F 179 PHE F 184 0
SHEET 2 AC5 5 LEU F 191 SER F 196 -1 O LEU F 193 N LYS F 183
SHEET 3 AC5 5 LEU F 201 ASN F 205 -1 O TRP F 204 N LEU F 192
SHEET 4 AC5 5 THR F 210 PHE F 215 -1 O THR F 210 N ASN F 205
SHEET 5 AC5 5 GLN F 278 ILE F 280 1 O GLN F 278 N ILE F 214
SHEET 1 AC6 4 VAL F 225 TYR F 230 0
SHEET 2 AC6 4 LYS F 236 GLY F 241 -1 O CYS F 240 N SER F 227
SHEET 3 AC6 4 LEU F 246 ARG F 250 -1 O LYS F 247 N SER F 239
SHEET 4 AC6 4 PHE F 285 THR F 287 -1 O PHE F 285 N LEU F 248
SHEET 1 AC7 4 CYS F 297 LEU F 301 0
SHEET 2 AC7 4 LEU F 304 LYS F 308 -1 O LEU F 306 N ARG F 299
SHEET 3 AC7 4 ALA F 313 PRO F 319 -1 O VAL F 315 N SER F 307
SHEET 4 AC7 4 VAL F 336 ASP F 343 -1 O GLY F 340 N CYS F 316
SHEET 1 AC8 4 SER F 355 MET F 356 0
SHEET 2 AC8 4 MET F 362 GLY F 366 -1 O ALA F 364 N SER F 355
SHEET 3 AC8 4 LEU F 372 ASP F 376 -1 O TYR F 373 N LEU F 365
SHEET 4 AC8 4 CYS F 387 LEU F 390 -1 O LEU F 390 N LEU F 372
SSBOND 1 CYS B 452 CYS B 463 1555 1555 2.71
LINK SG CYS A 286 ZN ZN A9008 1555 1555 2.15
LINK SG CYS A 289 ZN ZN A9008 1555 1555 2.33
LINK SG CYS A 294 ZN ZN A9008 1555 1555 2.27
LINK ND1 HIS A 297 ZN ZN A9008 1555 1555 1.92
LINK SG CYS A 523 ZN ZN A9003 1555 1555 2.48
LINK SG CYS A 523 ZN ZN A9004 1555 1555 2.20
LINK NE2 HIS A 525 ZN ZN A9004 1555 1555 1.94
LINK SG CYS A 530 ZN ZN A9002 1555 1555 2.28
LINK SG CYS A 530 ZN ZN A9004 1555 1555 2.25
LINK SG CYS A 534 ZN ZN A9004 1555 1555 2.14
LINK SG CYS A 536 ZN ZN A9003 1555 1555 2.34
LINK SG CYS A 543 ZN ZN A9002 1555 1555 2.43
LINK SG CYS A 543 ZN ZN A9003 1555 1555 2.35
LINK SG CYS A 547 ZN ZN A9003 1555 1555 2.26
LINK SG CYS A 549 ZN ZN A9002 1555 1555 2.17
LINK SG CYS A 553 ZN ZN A9002 1555 1555 2.22
LINK SG CYS A 560 ZN ZN A9005 1555 1555 2.49
LINK SG CYS A 560 ZN ZN A9007 1555 1555 2.30
LINK SG CYS A 562 ZN ZN A9007 1555 1555 2.47
LINK SG CYS A 566 ZN ZN A9006 1555 1555 2.28
LINK SG CYS A 566 ZN ZN A9007 1555 1555 2.23
LINK SG CYS A 571 ZN ZN A9007 1555 1555 2.22
LINK SG CYS A 573 ZN ZN A9005 1555 1555 2.26
LINK SG CYS A 580 ZN ZN A9005 1555 1555 2.11
LINK SG CYS A 580 ZN ZN A9006 1555 1555 2.42
LINK SG CYS A 585 ZN ZN A9005 1555 1555 2.15
LINK SG CYS A 588 ZN ZN A9006 1555 1555 2.40
LINK SG CYS A 601 ZN ZN A9006 1555 1555 2.17
LINK SG CYS B 286 ZN ZN B9008 1555 1555 2.22
LINK SG CYS B 289 ZN ZN B9008 1555 1555 2.31
LINK SG CYS B 294 ZN ZN B9008 1555 1555 2.23
LINK ND1 HIS B 297 ZN ZN B9008 1555 1555 1.95
LINK SG CYS B 523 ZN ZN B9002 1555 1555 2.17
LINK SG CYS B 523 ZN ZN B9003 1555 1555 2.57
LINK NE2 HIS B 525 ZN ZN B9002 1555 1555 2.10
LINK SG CYS B 530 ZN ZN B9002 1555 1555 2.18
LINK SG CYS B 530 ZN ZN B9004 1555 1555 2.30
LINK SG CYS B 534 ZN ZN B9002 1555 1555 2.16
LINK SG CYS B 536 ZN ZN B9003 1555 1555 2.25
LINK SG CYS B 543 ZN ZN B9003 1555 1555 2.31
LINK SG CYS B 543 ZN ZN B9004 1555 1555 2.39
LINK SG CYS B 547 ZN ZN B9003 1555 1555 2.31
LINK SG CYS B 549 ZN ZN B9004 1555 1555 2.18
LINK SG CYS B 553 ZN ZN B9004 1555 1555 2.25
LINK SG CYS B 560 ZN ZN B9005 1555 1555 2.30
LINK SG CYS B 560 ZN ZN B9007 1555 1555 2.50
LINK SG CYS B 562 ZN ZN B9005 1555 1555 2.60
LINK SG CYS B 566 ZN ZN B9005 1555 1555 2.19
LINK SG CYS B 566 ZN ZN B9006 1555 1555 2.40
LINK SG CYS B 571 ZN ZN B9005 1555 1555 2.13
LINK SG CYS B 573 ZN ZN B9007 1555 1555 2.17
LINK SG CYS B 580 ZN ZN B9006 1555 1555 2.40
LINK SG CYS B 580 ZN ZN B9007 1555 1555 2.16
LINK SG CYS B 585 ZN ZN B9007 1555 1555 2.14
LINK SG CYS B 588 ZN ZN B9006 1555 1555 2.27
LINK SG CYS B 601 ZN ZN B9006 1555 1555 2.09
CISPEP 1 MET T 579 GLU T 580 0 -1.57
SITE 1 AC1 15 ILE A 109 MET A 110 TYR A 111 GLY A 623
SITE 2 AC1 15 TRP A 624 VAL A 657 TYR A 658 TYR A 661
SITE 3 AC1 15 PHE A 665 ARG A 685 PHE A 686 ASN A 688
SITE 4 AC1 15 HOH A9101 ARG E 222 ASP E 223
SITE 1 AC2 4 CYS A 530 CYS A 543 CYS A 549 CYS A 553
SITE 1 AC3 5 CYS A 523 CYS A 536 CYS A 543 CYS A 547
SITE 2 AC3 5 ZN A9004
SITE 1 AC4 5 CYS A 523 HIS A 525 CYS A 530 CYS A 534
SITE 2 AC4 5 ZN A9003
SITE 1 AC5 4 CYS A 560 CYS A 573 CYS A 580 CYS A 585
SITE 1 AC6 4 CYS A 566 CYS A 580 CYS A 588 CYS A 601
SITE 1 AC7 4 CYS A 560 CYS A 562 CYS A 566 CYS A 571
SITE 1 AC8 4 CYS A 286 CYS A 289 CYS A 294 HIS A 297
SITE 1 AC9 14 ILE B 109 MET B 110 TYR B 111 GLY B 623
SITE 2 AC9 14 TRP B 624 VAL B 657 TYR B 658 TYR B 661
SITE 3 AC9 14 PHE B 665 ARG B 685 PHE B 686 ASN B 688
SITE 4 AC9 14 ARG F 222 ASP F 223
SITE 1 AD1 5 CYS B 523 HIS B 525 CYS B 530 CYS B 534
SITE 2 AD1 5 ZN B9003
SITE 1 AD2 5 CYS B 523 CYS B 536 CYS B 543 CYS B 547
SITE 2 AD2 5 ZN B9002
SITE 1 AD3 4 CYS B 530 CYS B 543 CYS B 549 CYS B 553
SITE 1 AD4 4 CYS B 560 CYS B 562 CYS B 566 CYS B 571
SITE 1 AD5 4 CYS B 566 CYS B 580 CYS B 588 CYS B 601
SITE 1 AD6 4 CYS B 560 CYS B 573 CYS B 580 CYS B 585
SITE 1 AD7 4 CYS B 286 CYS B 289 CYS B 294 HIS B 297
CRYST1 69.575 115.042 153.033 90.00 102.53 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014373 0.000000 0.003194 0.00000
SCALE2 0.000000 0.008692 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006694 0.00000
(ATOM LINES ARE NOT SHOWN.)
END