HEADER HYDROLASE 28-JAN-14 4ON9
TITLE DECH BOX HELICASE DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE ATP-DEPENDENT RNA HELICASE DDX58;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 230-793;
COMPND 5 SYNONYM: DEAD BOX PROTEIN 58, RIG-I-LIKE RECEPTOR 1, RLR-1, RETINOIC
COMPND 6 ACID-INDUCIBLE GENE 1 PROTEIN, RIG-1, RETINOIC ACID-INDUCIBLE GENE I
COMPND 7 PROTEIN, RIG-I;
COMPND 8 EC: 3.6.4.13;
COMPND 9 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: DDX58;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PATTERN RECOGNITION RECEPTOR, CYTOSOL, ATPASE, DECH BOX DOMAIN, RNA,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.DEIMLING,G.WITTE,K.P.HOPFNER
REVDAT 4 08-NOV-23 4ON9 1 REMARK SEQADV
REVDAT 3 11-MAR-15 4ON9 1 JRNL
REVDAT 2 06-AUG-14 4ON9 1 JRNL
REVDAT 1 02-JUL-14 4ON9 0
JRNL AUTH T.DEIMLING,S.CUI,K.LAMMENS,K.P.HOPFNER,G.WITTE
JRNL TITL CRYSTAL AND SOLUTION STRUCTURE OF THE HUMAN RIG-I SF2 DOMAIN
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 70 1027 2014
JRNL REFN ESSN 1744-3091
JRNL PMID 25084375
JRNL DOI 10.1107/S2053230X14012230
REMARK 2
REMARK 2 RESOLUTION. 2.71 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.71
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.06
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 38264
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 1890
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.0648 - 6.5177 0.97 2713 141 0.2114 0.2099
REMARK 3 2 6.5177 - 5.1751 0.99 2660 138 0.2333 0.2645
REMARK 3 3 5.1751 - 4.5214 0.99 2617 137 0.1731 0.2361
REMARK 3 4 4.5214 - 4.1083 0.99 2609 137 0.1724 0.2183
REMARK 3 5 4.1083 - 3.8139 0.99 2586 134 0.1929 0.2438
REMARK 3 6 3.8139 - 3.5891 0.99 2600 137 0.2128 0.2374
REMARK 3 7 3.5891 - 3.4094 0.99 2560 134 0.2247 0.2910
REMARK 3 8 3.4094 - 3.2611 1.00 2609 139 0.2419 0.2590
REMARK 3 9 3.2611 - 3.1355 1.00 2593 136 0.2658 0.3872
REMARK 3 10 3.1355 - 3.0274 1.00 2603 137 0.2854 0.3348
REMARK 3 11 3.0274 - 2.9327 1.00 2573 135 0.2881 0.3433
REMARK 3 12 2.9327 - 2.8489 0.99 2557 134 0.2969 0.3245
REMARK 3 13 2.8489 - 2.7739 0.99 2583 130 0.3000 0.3820
REMARK 3 14 2.7739 - 2.7100 0.98 2511 121 0.3152 0.3681
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.600
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 8286
REMARK 3 ANGLE : 0.907 11164
REMARK 3 CHIRALITY : 0.035 1259
REMARK 3 PLANARITY : 0.004 1421
REMARK 3 DIHEDRAL : 19.084 3135
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4ON9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-JAN-14.
REMARK 100 THE DEPOSITION ID IS D_1000084706.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUL-11
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.999870
REMARK 200 MONOCHROMATOR : FIXED-EXIT LN2 COOLED DOUBLE
REMARK 200 CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS, XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38281
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.710
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.71
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
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
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3TBK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1:1 RIG-I SF2 (60MG/ML) : RESERVOIR
REMARK 280 SOLUTION (100MM HEPES PH=6.8, 100MM AMMONIUM SULFATE, 6.7%(V/V)
REMARK 280 ISOPROPANOL, 9%(V/V) PEG4000), 4DAYS, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 288K, PH 6.8
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 49.45500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 62.13000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.49500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 62.13000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 49.45500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.49500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 48940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 214
REMARK 465 GLY A 215
REMARK 465 SER A 216
REMARK 465 SER A 217
REMARK 465 HIS A 218
REMARK 465 HIS A 219
REMARK 465 HIS A 220
REMARK 465 HIS A 221
REMARK 465 HIS A 222
REMARK 465 HIS A 223
REMARK 465 SER A 224
REMARK 465 GLN A 225
REMARK 465 ASP A 226
REMARK 465 PRO A 227
REMARK 465 ASN A 228
REMARK 465 SER A 229
REMARK 465 SER A 230
REMARK 465 GLU A 231
REMARK 465 VAL A 232
REMARK 465 SER A 233
REMARK 465 ASP A 234
REMARK 465 THR A 235
REMARK 465 ASN A 236
REMARK 465 LEU A 237
REMARK 465 TYR A 238
REMARK 465 SER A 239
REMARK 465 PRO A 240
REMARK 465 ASN A 495
REMARK 465 LEU A 496
REMARK 465 PHE A 523
REMARK 465 GLN A 524
REMARK 465 MET A 525
REMARK 465 PRO A 526
REMARK 465 ASP A 527
REMARK 465 THR A 662
REMARK 465 GLY A 663
REMARK 465 ARG A 664
REMARK 465 GLY A 665
REMARK 465 LYS A 666
REMARK 465 THR A 667
REMARK 465 ASN A 668
REMARK 465 GLN A 669
REMARK 465 ASN A 670
REMARK 465 THR A 671
REMARK 465 GLY A 672
REMARK 465 MET A 673
REMARK 465 THR A 674
REMARK 465 LEU A 675
REMARK 465 PRO A 676
REMARK 465 ALA A 677
REMARK 465 GLN A 678
REMARK 465 LYS A 679
REMARK 465 CYS A 680
REMARK 465 ILE A 681
REMARK 465 LEU A 682
REMARK 465 ASP A 683
REMARK 465 ALA A 684
REMARK 465 THR A 727
REMARK 465 ARG A 728
REMARK 465 GLY A 729
REMARK 465 ARG A 730
REMARK 465 GLY A 731
REMARK 465 ARG A 732
REMARK 465 ALA A 733
REMARK 465 ARG A 734
REMARK 465 SER A 793
REMARK 465 MET B 214
REMARK 465 GLY B 215
REMARK 465 SER B 216
REMARK 465 SER B 217
REMARK 465 HIS B 218
REMARK 465 HIS B 219
REMARK 465 HIS B 220
REMARK 465 HIS B 221
REMARK 465 HIS B 222
REMARK 465 HIS B 223
REMARK 465 SER B 224
REMARK 465 GLN B 225
REMARK 465 ASP B 226
REMARK 465 PRO B 227
REMARK 465 ASN B 228
REMARK 465 SER B 229
REMARK 465 SER B 230
REMARK 465 GLU B 231
REMARK 465 VAL B 232
REMARK 465 SER B 233
REMARK 465 ASP B 234
REMARK 465 THR B 235
REMARK 465 ASN B 236
REMARK 465 LEU B 237
REMARK 465 TYR B 238
REMARK 465 SER B 239
REMARK 465 PRO B 240
REMARK 465 PHE B 241
REMARK 465 GLN B 287
REMARK 465 GLY B 288
REMARK 465 GLN B 289
REMARK 465 ALA B 327
REMARK 465 THR B 328
REMARK 465 ALA B 329
REMARK 465 GLU B 330
REMARK 465 GLY B 397
REMARK 465 SER B 398
REMARK 465 LEU B 661
REMARK 465 THR B 662
REMARK 465 GLY B 663
REMARK 465 ARG B 664
REMARK 465 GLY B 665
REMARK 465 LYS B 666
REMARK 465 THR B 667
REMARK 465 ASN B 668
REMARK 465 GLN B 669
REMARK 465 ASN B 670
REMARK 465 THR B 671
REMARK 465 GLY B 672
REMARK 465 MET B 673
REMARK 465 THR B 674
REMARK 465 LEU B 675
REMARK 465 PRO B 676
REMARK 465 ALA B 677
REMARK 465 GLN B 678
REMARK 465 LYS B 679
REMARK 465 CYS B 680
REMARK 465 ILE B 681
REMARK 465 LEU B 682
REMARK 465 ASP B 683
REMARK 465 ALA B 684
REMARK 465 PHE B 685
REMARK 465 LYS B 686
REMARK 465 ALA B 687
REMARK 465 SER B 698
REMARK 465 VAL B 699
REMARK 465 ALA B 700
REMARK 465 ASP B 701
REMARK 465 GLU B 702
REMARK 465 GLY B 703
REMARK 465 ILE B 704
REMARK 465 ASP B 705
REMARK 465 ILE B 722
REMARK 465 LYS B 723
REMARK 465 MET B 724
REMARK 465 ILE B 725
REMARK 465 GLN B 726
REMARK 465 THR B 727
REMARK 465 ARG B 728
REMARK 465 GLY B 729
REMARK 465 ARG B 730
REMARK 465 GLY B 731
REMARK 465 ARG B 732
REMARK 465 ALA B 733
REMARK 465 ARG B 734
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLN A 287 CB CD
REMARK 480 GLU A 304 CD
REMARK 480 THR A 328 CB
REMARK 480 ASN A 331 C
REMARK 480 VAL A 332 N
REMARK 480 GLU A 339 CD
REMARK 480 ASN A 340 CG
REMARK 480 LYS A 379 CG
REMARK 480 GLN A 380 CB
REMARK 480 LYS A 418 CG
REMARK 480 LYS A 443 CE
REMARK 480 GLU A 447 CD
REMARK 480 GLU A 450 CD
REMARK 480 GLN A 451 CD
REMARK 480 TYR A 454 CZ
REMARK 480 GLN A 457 CD
REMARK 480 TYR A 473 CG
REMARK 480 LYS A 491 CG
REMARK 480 GLU A 494 CD
REMARK 480 GLN A 498 CD
REMARK 480 ILE A 499 N
REMARK 480 GLN A 500 CD
REMARK 480 GLU A 503 CD
REMARK 480 MET A 521 CG
REMARK 480 SER A 532 CB
REMARK 480 ARG A 533 CZ
REMARK 480 ARG A 575 CZ
REMARK 480 GLU A 581 CD
REMARK 480 GLN A 584 CD
REMARK 480 GLN A 588 CD
REMARK 480 GLU A 591 CD
REMARK 480 GLU A 627 CD
REMARK 480 ARG A 637 CZ
REMARK 480 LEU A 661 N CG
REMARK 480 PHE A 685 CE1
REMARK 480 SER A 688 C
REMARK 480 GLY A 689 N
REMARK 480 SER A 698 CB
REMARK 480 GLU A 702 CD
REMARK 480 GLN A 726 CG
REMARK 480 LYS A 750 CD
REMARK 480 GLU A 751 CD
REMARK 480 GLU A 758 CD
REMARK 480 LYS A 759 CG
REMARK 480 GLU A 773 CD
REMARK 480 ARG A 777 CZ
REMARK 480 GLU A 778 CG
REMARK 480 ILE A 780 CD1
REMARK 480 LEU A 781 CB
REMARK 480 HIS A 782 CG
REMARK 480 GLN A 784 CD
REMARK 480 THR A 785 CG2
REMARK 480 GLU A 787 CD
REMARK 480 LYS A 788 CG
REMARK 480 PHE A 789 CG
REMARK 480 ARG A 791 CB
REMARK 480 ASP A 792 C CG
REMARK 480 LYS B 242 CA CD
REMARK 480 GLU B 249 CD
REMARK 480 ILE B 261 CD1
REMARK 480 PHE B 272 CG CZ
REMARK 480 GLU B 279 CD
REMARK 480 LYS B 284 CD
REMARK 480 PHE B 285 CG
REMARK 480 PRO B 286 CG
REMARK 480 LYS B 290 CD
REMARK 480 GLU B 304 CD
REMARK 480 TYR B 313 CD2
REMARK 480 PHE B 314 CE2
REMARK 480 HIS B 317 CG
REMARK 480 ARG B 320 CZ
REMARK 480 ASN B 331 CA C CG
REMARK 480 VAL B 332 CB
REMARK 480 PRO B 333 C
REMARK 480 GLN B 336 OE1
REMARK 480 ILE B 337 CG1
REMARK 480 GLN B 380 CD
REMARK 480 LEU B 395 CB
REMARK 480 GLY B 396 N
REMARK 480 SER B 399 C
REMARK 480 PRO B 401 C CB
REMARK 480 ILE B 406 CD1
REMARK 480 VAL B 414 CG1
REMARK 480 THR B 420 CG2
REMARK 480 SER B 433 OG
REMARK 480 VAL B 442 CG2
REMARK 480 ASN B 445 CG
REMARK 480 TYR B 454 CG CE1
REMARK 480 GLN B 500 CD
REMARK 480 GLN B 507 CD
REMARK 480 PHE B 523 C CE1
REMARK 480 LYS B 536 CG CE
REMARK 480 PHE B 579 CB
REMARK 480 GLU B 581 CD
REMARK 480 ARG B 637 CZ
REMARK 480 GLY B 689 N
REMARK 480 ASP B 690 CG
REMARK 480 LEU B 694 CD2
REMARK 480 GLN B 708 CD
REMARK 480 VAL B 718 C
REMARK 480 ASN B 720 CG
REMARK 480 VAL B 721 CB
REMARK 480 LEU B 740 CG
REMARK 480 GLU B 749 CD
REMARK 480 GLU B 758 CD
REMARK 480 ARG B 767 CZ
REMARK 480 THR B 770 CG2
REMARK 480 GLU B 773 CD
REMARK 480 PHE B 776 CB CZ
REMARK 480 ARG B 777 CD CZ
REMARK 480 GLU B 778 OE1
REMARK 480 HIS B 782 CG NE2
REMARK 480 THR B 785 CG2
REMARK 480 HIS B 786 CG
REMARK 480 GLU B 787 CD
REMARK 480 LYS B 788 CB
REMARK 480 PHE B 789 CZ
REMARK 480 ILE B 790 CB
REMARK 480 ASP B 792 CB
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 NZ LYS A 292 O ASN A 341 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 GLU A 330 -9.90 76.55
REMARK 500 ASN A 445 40.56 -107.26
REMARK 500 GLN A 498 -5.08 75.11
REMARK 500 VAL A 721 157.53 -47.72
REMARK 500 THR B 377 83.95 -67.85
REMARK 500 ALA B 558 -159.35 -143.76
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 SO4 A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 803
DBREF 4ON9 A 230 793 UNP O95786 DDX58_HUMAN 230 793
DBREF 4ON9 B 230 793 UNP O95786 DDX58_HUMAN 230 793
SEQADV 4ON9 MET A 214 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 GLY A 215 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 SER A 216 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 SER A 217 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 HIS A 218 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 HIS A 219 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 HIS A 220 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 HIS A 221 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 HIS A 222 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 HIS A 223 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 SER A 224 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 GLN A 225 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 ASP A 226 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 PRO A 227 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 ASN A 228 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 SER A 229 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 MET B 214 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 GLY B 215 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 SER B 216 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 SER B 217 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 HIS B 218 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 HIS B 219 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 HIS B 220 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 HIS B 221 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 HIS B 222 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 HIS B 223 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 SER B 224 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 GLN B 225 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 ASP B 226 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 PRO B 227 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 ASN B 228 UNP O95786 EXPRESSION TAG
SEQADV 4ON9 SER B 229 UNP O95786 EXPRESSION TAG
SEQRES 1 A 580 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 A 580 PRO ASN SER SER GLU VAL SER ASP THR ASN LEU TYR SER
SEQRES 3 A 580 PRO PHE LYS PRO ARG ASN TYR GLN LEU GLU LEU ALA LEU
SEQRES 4 A 580 PRO ALA MET LYS GLY LYS ASN THR ILE ILE CYS ALA PRO
SEQRES 5 A 580 THR GLY CYS GLY LYS THR PHE VAL SER LEU LEU ILE CYS
SEQRES 6 A 580 GLU HIS HIS LEU LYS LYS PHE PRO GLN GLY GLN LYS GLY
SEQRES 7 A 580 LYS VAL VAL PHE PHE ALA ASN GLN ILE PRO VAL TYR GLU
SEQRES 8 A 580 GLN GLN LYS SER VAL PHE SER LYS TYR PHE GLU ARG HIS
SEQRES 9 A 580 GLY TYR ARG VAL THR GLY ILE SER GLY ALA THR ALA GLU
SEQRES 10 A 580 ASN VAL PRO VAL GLU GLN ILE VAL GLU ASN ASN ASP ILE
SEQRES 11 A 580 ILE ILE LEU THR PRO GLN ILE LEU VAL ASN ASN LEU LYS
SEQRES 12 A 580 LYS GLY THR ILE PRO SER LEU SER ILE PHE THR LEU MET
SEQRES 13 A 580 ILE PHE ASP GLU CYS HIS ASN THR SER LYS GLN HIS PRO
SEQRES 14 A 580 TYR ASN MET ILE MET PHE ASN TYR LEU ASP GLN LYS LEU
SEQRES 15 A 580 GLY GLY SER SER GLY PRO LEU PRO GLN VAL ILE GLY LEU
SEQRES 16 A 580 THR ALA SER VAL GLY VAL GLY ASP ALA LYS ASN THR ASP
SEQRES 17 A 580 GLU ALA LEU ASP TYR ILE CYS LYS LEU CYS ALA SER LEU
SEQRES 18 A 580 ASP ALA SER VAL ILE ALA THR VAL LYS HIS ASN LEU GLU
SEQRES 19 A 580 GLU LEU GLU GLN VAL VAL TYR LYS PRO GLN LYS PHE PHE
SEQRES 20 A 580 ARG LYS VAL GLU SER ARG ILE SER ASP LYS PHE LYS TYR
SEQRES 21 A 580 ILE ILE ALA GLN LEU MET ARG ASP THR GLU SER LEU ALA
SEQRES 22 A 580 LYS ARG ILE CYS LYS ASP LEU GLU ASN LEU SER GLN ILE
SEQRES 23 A 580 GLN ASN ARG GLU PHE GLY THR GLN LYS TYR GLU GLN TRP
SEQRES 24 A 580 ILE VAL THR VAL GLN LYS ALA CYS MET VAL PHE GLN MET
SEQRES 25 A 580 PRO ASP LYS ASP GLU GLU SER ARG ILE CYS LYS ALA LEU
SEQRES 26 A 580 PHE LEU TYR THR SER HIS LEU ARG LYS TYR ASN ASP ALA
SEQRES 27 A 580 LEU ILE ILE SER GLU HIS ALA ARG MET LYS ASP ALA LEU
SEQRES 28 A 580 ASP TYR LEU LYS ASP PHE PHE SER ASN VAL ARG ALA ALA
SEQRES 29 A 580 GLY PHE ASP GLU ILE GLU GLN ASP LEU THR GLN ARG PHE
SEQRES 30 A 580 GLU GLU LYS LEU GLN GLU LEU GLU SER VAL SER ARG ASP
SEQRES 31 A 580 PRO SER ASN GLU ASN PRO LYS LEU GLU ASP LEU CYS PHE
SEQRES 32 A 580 ILE LEU GLN GLU GLU TYR HIS LEU ASN PRO GLU THR ILE
SEQRES 33 A 580 THR ILE LEU PHE VAL LYS THR ARG ALA LEU VAL ASP ALA
SEQRES 34 A 580 LEU LYS ASN TRP ILE GLU GLY ASN PRO LYS LEU SER PHE
SEQRES 35 A 580 LEU LYS PRO GLY ILE LEU THR GLY ARG GLY LYS THR ASN
SEQRES 36 A 580 GLN ASN THR GLY MET THR LEU PRO ALA GLN LYS CYS ILE
SEQRES 37 A 580 LEU ASP ALA PHE LYS ALA SER GLY ASP HIS ASN ILE LEU
SEQRES 38 A 580 ILE ALA THR SER VAL ALA ASP GLU GLY ILE ASP ILE ALA
SEQRES 39 A 580 GLN CYS ASN LEU VAL ILE LEU TYR GLU TYR VAL GLY ASN
SEQRES 40 A 580 VAL ILE LYS MET ILE GLN THR ARG GLY ARG GLY ARG ALA
SEQRES 41 A 580 ARG GLY SER LYS CYS PHE LEU LEU THR SER ASN ALA GLY
SEQRES 42 A 580 VAL ILE GLU LYS GLU GLN ILE ASN MET TYR LYS GLU LYS
SEQRES 43 A 580 MET MET ASN ASP SER ILE LEU ARG LEU GLN THR TRP ASP
SEQRES 44 A 580 GLU ALA VAL PHE ARG GLU LYS ILE LEU HIS ILE GLN THR
SEQRES 45 A 580 HIS GLU LYS PHE ILE ARG ASP SER
SEQRES 1 B 580 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 B 580 PRO ASN SER SER GLU VAL SER ASP THR ASN LEU TYR SER
SEQRES 3 B 580 PRO PHE LYS PRO ARG ASN TYR GLN LEU GLU LEU ALA LEU
SEQRES 4 B 580 PRO ALA MET LYS GLY LYS ASN THR ILE ILE CYS ALA PRO
SEQRES 5 B 580 THR GLY CYS GLY LYS THR PHE VAL SER LEU LEU ILE CYS
SEQRES 6 B 580 GLU HIS HIS LEU LYS LYS PHE PRO GLN GLY GLN LYS GLY
SEQRES 7 B 580 LYS VAL VAL PHE PHE ALA ASN GLN ILE PRO VAL TYR GLU
SEQRES 8 B 580 GLN GLN LYS SER VAL PHE SER LYS TYR PHE GLU ARG HIS
SEQRES 9 B 580 GLY TYR ARG VAL THR GLY ILE SER GLY ALA THR ALA GLU
SEQRES 10 B 580 ASN VAL PRO VAL GLU GLN ILE VAL GLU ASN ASN ASP ILE
SEQRES 11 B 580 ILE ILE LEU THR PRO GLN ILE LEU VAL ASN ASN LEU LYS
SEQRES 12 B 580 LYS GLY THR ILE PRO SER LEU SER ILE PHE THR LEU MET
SEQRES 13 B 580 ILE PHE ASP GLU CYS HIS ASN THR SER LYS GLN HIS PRO
SEQRES 14 B 580 TYR ASN MET ILE MET PHE ASN TYR LEU ASP GLN LYS LEU
SEQRES 15 B 580 GLY GLY SER SER GLY PRO LEU PRO GLN VAL ILE GLY LEU
SEQRES 16 B 580 THR ALA SER VAL GLY VAL GLY ASP ALA LYS ASN THR ASP
SEQRES 17 B 580 GLU ALA LEU ASP TYR ILE CYS LYS LEU CYS ALA SER LEU
SEQRES 18 B 580 ASP ALA SER VAL ILE ALA THR VAL LYS HIS ASN LEU GLU
SEQRES 19 B 580 GLU LEU GLU GLN VAL VAL TYR LYS PRO GLN LYS PHE PHE
SEQRES 20 B 580 ARG LYS VAL GLU SER ARG ILE SER ASP LYS PHE LYS TYR
SEQRES 21 B 580 ILE ILE ALA GLN LEU MET ARG ASP THR GLU SER LEU ALA
SEQRES 22 B 580 LYS ARG ILE CYS LYS ASP LEU GLU ASN LEU SER GLN ILE
SEQRES 23 B 580 GLN ASN ARG GLU PHE GLY THR GLN LYS TYR GLU GLN TRP
SEQRES 24 B 580 ILE VAL THR VAL GLN LYS ALA CYS MET VAL PHE GLN MET
SEQRES 25 B 580 PRO ASP LYS ASP GLU GLU SER ARG ILE CYS LYS ALA LEU
SEQRES 26 B 580 PHE LEU TYR THR SER HIS LEU ARG LYS TYR ASN ASP ALA
SEQRES 27 B 580 LEU ILE ILE SER GLU HIS ALA ARG MET LYS ASP ALA LEU
SEQRES 28 B 580 ASP TYR LEU LYS ASP PHE PHE SER ASN VAL ARG ALA ALA
SEQRES 29 B 580 GLY PHE ASP GLU ILE GLU GLN ASP LEU THR GLN ARG PHE
SEQRES 30 B 580 GLU GLU LYS LEU GLN GLU LEU GLU SER VAL SER ARG ASP
SEQRES 31 B 580 PRO SER ASN GLU ASN PRO LYS LEU GLU ASP LEU CYS PHE
SEQRES 32 B 580 ILE LEU GLN GLU GLU TYR HIS LEU ASN PRO GLU THR ILE
SEQRES 33 B 580 THR ILE LEU PHE VAL LYS THR ARG ALA LEU VAL ASP ALA
SEQRES 34 B 580 LEU LYS ASN TRP ILE GLU GLY ASN PRO LYS LEU SER PHE
SEQRES 35 B 580 LEU LYS PRO GLY ILE LEU THR GLY ARG GLY LYS THR ASN
SEQRES 36 B 580 GLN ASN THR GLY MET THR LEU PRO ALA GLN LYS CYS ILE
SEQRES 37 B 580 LEU ASP ALA PHE LYS ALA SER GLY ASP HIS ASN ILE LEU
SEQRES 38 B 580 ILE ALA THR SER VAL ALA ASP GLU GLY ILE ASP ILE ALA
SEQRES 39 B 580 GLN CYS ASN LEU VAL ILE LEU TYR GLU TYR VAL GLY ASN
SEQRES 40 B 580 VAL ILE LYS MET ILE GLN THR ARG GLY ARG GLY ARG ALA
SEQRES 41 B 580 ARG GLY SER LYS CYS PHE LEU LEU THR SER ASN ALA GLY
SEQRES 42 B 580 VAL ILE GLU LYS GLU GLN ILE ASN MET TYR LYS GLU LYS
SEQRES 43 B 580 MET MET ASN ASP SER ILE LEU ARG LEU GLN THR TRP ASP
SEQRES 44 B 580 GLU ALA VAL PHE ARG GLU LYS ILE LEU HIS ILE GLN THR
SEQRES 45 B 580 HIS GLU LYS PHE ILE ARG ASP SER
HET SO4 A 801 5
HET SO4 A 802 5
HET SO4 B 801 5
HET SO4 B 802 5
HET CL B 803 1
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
FORMUL 3 SO4 4(O4 S 2-)
FORMUL 7 CL CL 1-
FORMUL 8 HOH *36(H2 O)
HELIX 1 1 ARG A 244 LYS A 256 1 13
HELIX 2 2 GLY A 269 LYS A 284 1 16
HELIX 3 3 GLN A 299 ARG A 316 1 18
HELIX 4 4 PRO A 333 ASN A 341 1 9
HELIX 5 5 THR A 347 GLY A 358 1 12
HELIX 6 6 GLU A 373 THR A 377 5 5
HELIX 7 7 HIS A 381 GLY A 396 1 16
HELIX 8 8 ASN A 419 LEU A 434 1 16
HELIX 9 9 ASN A 445 VAL A 453 1 9
HELIX 10 10 ASP A 469 CYS A 490 1 22
HELIX 11 11 THR A 506 VAL A 522 1 17
HELIX 12 12 ASP A 529 ALA A 558 1 30
HELIX 13 13 ARG A 559 ALA A 577 1 19
HELIX 14 14 ASP A 580 ASP A 603 1 24
HELIX 15 15 PRO A 604 GLU A 607 5 4
HELIX 16 16 ASN A 608 ASN A 625 1 18
HELIX 17 17 THR A 636 ASN A 650 1 15
HELIX 18 18 PRO A 651 SER A 654 5 4
HELIX 19 19 ASN A 744 TRP A 771 1 28
HELIX 20 20 ASP A 772 ASP A 792 1 21
HELIX 21 21 ARG B 244 LYS B 256 1 13
HELIX 22 22 GLY B 269 LYS B 283 1 15
HELIX 23 23 GLN B 299 ARG B 316 1 18
HELIX 24 24 PRO B 333 ASN B 341 1 9
HELIX 25 25 THR B 347 GLY B 358 1 12
HELIX 26 26 SER B 362 PHE B 366 5 5
HELIX 27 27 CYS B 374 THR B 377 5 4
HELIX 28 28 HIS B 381 LEU B 395 1 15
HELIX 29 29 ASN B 419 LEU B 434 1 16
HELIX 30 30 ASN B 445 VAL B 453 1 9
HELIX 31 31 ASP B 469 ILE B 489 1 21
HELIX 32 32 CYS B 490 LEU B 496 1 7
HELIX 33 33 THR B 506 PHE B 523 1 18
HELIX 34 34 ASP B 527 ALA B 558 1 32
HELIX 35 35 ARG B 559 ALA B 577 1 19
HELIX 36 36 ASP B 580 ASP B 603 1 24
HELIX 37 37 PRO B 604 GLU B 607 5 4
HELIX 38 38 ASN B 608 ASN B 625 1 18
HELIX 39 39 THR B 636 ASN B 650 1 15
HELIX 40 40 PRO B 651 SER B 654 5 4
HELIX 41 41 ASN B 744 TRP B 771 1 28
HELIX 42 42 ASP B 772 SER B 793 1 22
SHEET 1 A 7 VAL A 321 ILE A 324 0
SHEET 2 A 7 ILE A 343 LEU A 346 1 O ILE A 345 N ILE A 324
SHEET 3 A 7 VAL A 293 PHE A 296 1 N PHE A 295 O LEU A 346
SHEET 4 A 7 LEU A 368 PHE A 371 1 O ILE A 370 N PHE A 296
SHEET 5 A 7 GLN A 404 THR A 409 1 O ILE A 406 N PHE A 371
SHEET 6 A 7 THR A 260 CYS A 263 1 N ILE A 262 O GLY A 407
SHEET 7 A 7 VAL A 438 ALA A 440 1 O ALA A 440 N ILE A 261
SHEET 1 B 6 GLN A 457 LYS A 462 0
SHEET 2 B 6 LYS A 737 THR A 742 1 O LEU A 740 N PHE A 459
SHEET 3 B 6 LEU A 711 TYR A 715 1 N VAL A 712 O PHE A 739
SHEET 4 B 6 THR A 630 PHE A 633 1 N PHE A 633 O ILE A 713
SHEET 5 B 6 ILE A 693 ALA A 696 1 O LEU A 694 N LEU A 632
SHEET 6 B 6 PRO A 658 ILE A 660 1 N GLY A 659 O ILE A 695
SHEET 1 C 2 ASP A 705 GLN A 708 0
SHEET 2 C 2 ILE A 722 ILE A 725 1 O LYS A 723 N ALA A 707
SHEET 1 D 7 VAL B 321 ILE B 324 0
SHEET 2 D 7 ILE B 343 LEU B 346 1 O ILE B 343 N THR B 322
SHEET 3 D 7 VAL B 293 PHE B 296 1 N PHE B 295 O LEU B 346
SHEET 4 D 7 LEU B 368 ASP B 372 1 O ILE B 370 N PHE B 296
SHEET 5 D 7 GLN B 404 THR B 409 1 O ILE B 406 N PHE B 371
SHEET 6 D 7 THR B 260 CYS B 263 1 N ILE B 262 O GLY B 407
SHEET 7 D 7 VAL B 438 ALA B 440 1 O ALA B 440 N ILE B 261
SHEET 1 E 6 GLN B 457 LYS B 462 0
SHEET 2 E 6 LYS B 737 THR B 742 1 O LEU B 740 N PHE B 459
SHEET 3 E 6 LEU B 711 TYR B 715 1 N LEU B 714 O PHE B 739
SHEET 4 E 6 THR B 630 PHE B 633 1 N PHE B 633 O ILE B 713
SHEET 5 E 6 ILE B 693 ALA B 696 1 O LEU B 694 N LEU B 632
SHEET 6 E 6 PRO B 658 GLY B 659 1 N GLY B 659 O ILE B 693
CISPEP 1 GLY A 397 SER A 398 0 -9.71
CISPEP 2 PHE A 685 LYS A 686 0 1.23
SITE 1 AC1 8 PRO A 265 THR A 266 GLY A 267 CYS A 268
SITE 2 AC1 8 GLY A 269 LYS A 270 THR A 271 ARG B 488
SITE 1 AC2 4 THR A 506 GLN A 507 LYS A 508 LYS A 635
SITE 1 AC3 6 ARG A 488 THR B 266 GLY B 267 CYS B 268
SITE 2 AC3 6 GLY B 269 LYS B 270
SITE 1 AC4 3 THR B 506 GLN B 507 LYS B 508
SITE 1 AC5 3 ASN B 744 HOH B 914 HOH B 918
CRYST1 98.910 112.990 124.260 90.00 90.00 90.00 P 21 21 21 8
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 0.010110 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008850 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008048 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
