HEADER TRANSFERASE/TRANSFERASE INHIBITOR 09-MAY-16 5JT2
TITLE BRAFV600E KINASE DOMAIN IN COMPLEX WITH CHEMICALLY LINKED VEMURAFENIB
TITLE 2 INHIBITOR VEM-BISAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE B-RAF;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: KINASE DOMAIN (UNP RESIDUES 448-723);
COMPND 5 SYNONYM: PROTO-ONCOGENE B-RAF,P94,V-RAF MURINE SARCOMA VIRAL ONCOGENE
COMPND 6 HOMOLOG B1;
COMPND 7 EC: 2.7.11.1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BRAF, BRAF1, RAFB1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS KINASE, DIMER, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.J.GRASSO,R.MARMORSTEIN
REVDAT 7 18-OCT-23 5JT2 1 REMARK
REVDAT 6 02-NOV-22 5JT2 1 COMPND HETNAM FORMUL ATOM
REVDAT 5 04-DEC-19 5JT2 1 REMARK
REVDAT 4 27-SEP-17 5JT2 1 REMARK
REVDAT 3 02-NOV-16 5JT2 1 JRNL
REVDAT 2 21-SEP-16 5JT2 1 JRNL
REVDAT 1 14-SEP-16 5JT2 0
JRNL AUTH M.GRASSO,M.A.ESTRADA,C.VENTOCILLA,M.SAMANTA,J.MAKSIMOSKA,
JRNL AUTH 2 J.VILLANUEVA,J.D.WINKLER,R.MARMORSTEIN
JRNL TITL CHEMICALLY LINKED VEMURAFENIB INHIBITORS PROMOTE AN INACTIVE
JRNL TITL 2 BRAF(V600E) CONFORMATION.
JRNL REF ACS CHEM.BIOL. V. 11 2876 2016
JRNL REFN ESSN 1554-8937
JRNL PMID 27571413
JRNL DOI 10.1021/ACSCHEMBIO.6B00529
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.2_1309
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.59
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 34618
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.770
REMARK 3 FREE R VALUE TEST SET COUNT : 1999
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 29.5865 - 6.4902 0.98 2477 152 0.2282 0.2543
REMARK 3 2 6.4902 - 5.1604 1.00 2413 145 0.2186 0.2885
REMARK 3 3 5.1604 - 4.5107 1.00 2350 141 0.1820 0.2380
REMARK 3 4 4.5107 - 4.0994 1.00 2329 150 0.1763 0.2381
REMARK 3 5 4.0994 - 3.8062 1.00 2326 144 0.2036 0.2551
REMARK 3 6 3.8062 - 3.5822 1.00 2336 143 0.2091 0.2737
REMARK 3 7 3.5822 - 3.4031 0.99 2306 138 0.2337 0.2805
REMARK 3 8 3.4031 - 3.2552 1.00 2287 138 0.2243 0.3189
REMARK 3 9 3.2552 - 3.1300 1.00 2328 135 0.2158 0.2727
REMARK 3 10 3.1300 - 3.0221 1.00 2309 162 0.2163 0.3059
REMARK 3 11 3.0221 - 2.9277 1.00 2318 130 0.2254 0.3286
REMARK 3 12 2.9277 - 2.8441 1.00 2275 142 0.2493 0.3492
REMARK 3 13 2.8441 - 2.7692 1.00 2317 138 0.2520 0.3479
REMARK 3 14 2.7692 - 2.7017 0.99 2248 141 0.2413 0.3081
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) : 0.380
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.990
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 57.39
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.07
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 : 0.009 7942
REMARK 3 ANGLE : 1.278 10753
REMARK 3 CHIRALITY : 0.053 1179
REMARK 3 PLANARITY : 0.007 1359
REMARK 3 DIHEDRAL : 14.047 2822
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 : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND SEGID
REMARK 3 SELECTION : CHAIN B AND SEGID
REMARK 3 ATOM PAIRS NUMBER : 4481
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A AND SEGID
REMARK 3 SELECTION : CHAIN C AND SEGID
REMARK 3 ATOM PAIRS NUMBER : 4481
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A AND SEGID
REMARK 3 SELECTION : CHAIN D AND SEGID
REMARK 3 ATOM PAIRS NUMBER : 4481
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5JT2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000221173.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34678
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.54000
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: PHENIX
REMARK 200 STARTING MODEL: 5JSM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS PH 8.5 5% ETHANOL 2%
REMARK 280 BENZAMIDINE HCL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 32.55100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 137.80150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.22100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 137.80150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.55100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.22100
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
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: DIMERIC
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 SER A 605
REMARK 465 GLY A 606
REMARK 465 SER A 607
REMARK 465 HIS A 608
REMARK 465 GLN A 609
REMARK 465 PHE A 610
REMARK 465 GLU A 611
REMARK 465 GLN A 612
REMARK 465 LEU A 613
REMARK 465 SER A 614
REMARK 465 GLY A 615
REMARK 465 ARG A 626
REMARK 465 MET A 627
REMARK 465 GLN A 628
REMARK 465 ASP A 629
REMARK 465 SER A 630
REMARK 465 ASN A 631
REMARK 465 ASN A 661
REMARK 465 ARG A 662
REMARK 465 GLU A 720
REMARK 465 LEU A 721
REMARK 465 SER A 722
REMARK 465 GLY A 723
REMARK 465 GLY B 444
REMARK 465 SER B 445
REMARK 465 GLU B 446
REMARK 465 VAL B 487
REMARK 465 THR B 488
REMARK 465 ALA B 489
REMARK 465 PRO B 490
REMARK 465 GLU B 600
REMARK 465 LYS B 601
REMARK 465 SER B 602
REMARK 465 ARG B 603
REMARK 465 TRP B 604
REMARK 465 SER B 605
REMARK 465 GLY B 606
REMARK 465 SER B 607
REMARK 465 HIS B 608
REMARK 465 GLN B 609
REMARK 465 PHE B 610
REMARK 465 GLU B 611
REMARK 465 GLN B 612
REMARK 465 LEU B 613
REMARK 465 SER B 614
REMARK 465 GLY B 615
REMARK 465 GLN B 628
REMARK 465 ASP B 629
REMARK 465 GLU B 720
REMARK 465 LEU B 721
REMARK 465 SER B 722
REMARK 465 GLY B 723
REMARK 465 THR C 488
REMARK 465 ALA C 489
REMARK 465 TRP C 604
REMARK 465 SER C 605
REMARK 465 GLY C 606
REMARK 465 SER C 607
REMARK 465 HIS C 608
REMARK 465 GLN C 609
REMARK 465 PHE C 610
REMARK 465 GLU C 611
REMARK 465 GLN C 612
REMARK 465 LEU C 613
REMARK 465 SER C 614
REMARK 465 GLY C 615
REMARK 465 MET C 627
REMARK 465 GLN C 628
REMARK 465 ASP C 629
REMARK 465 SER C 630
REMARK 465 ASN C 631
REMARK 465 ASN C 658
REMARK 465 ARG C 662
REMARK 465 ASP C 663
REMARK 465 GLN C 664
REMARK 465 SER C 673
REMARK 465 LEU C 674
REMARK 465 GLU C 720
REMARK 465 LEU C 721
REMARK 465 SER C 722
REMARK 465 GLY C 723
REMARK 465 GLY D 444
REMARK 465 SER D 445
REMARK 465 THR D 488
REMARK 465 ALA D 489
REMARK 465 LYS D 601
REMARK 465 SER D 602
REMARK 465 ARG D 603
REMARK 465 TRP D 604
REMARK 465 SER D 605
REMARK 465 GLY D 606
REMARK 465 SER D 607
REMARK 465 HIS D 608
REMARK 465 GLN D 609
REMARK 465 PHE D 610
REMARK 465 GLU D 611
REMARK 465 GLN D 612
REMARK 465 LEU D 613
REMARK 465 SER D 614
REMARK 465 GLY D 615
REMARK 465 MET D 627
REMARK 465 GLN D 628
REMARK 465 ASP D 629
REMARK 465 SER D 630
REMARK 465 ASN D 658
REMARK 465 ILE D 659
REMARK 465 ASN D 660
REMARK 465 ASN D 661
REMARK 465 ARG D 662
REMARK 465 ASP D 663
REMARK 465 GLN D 664
REMARK 465 ILE D 665
REMARK 465 ILE D 666
REMARK 465 GLU D 667
REMARK 465 MET D 668
REMARK 465 VAL D 669
REMARK 465 GLY D 670
REMARK 465 ARG D 671
REMARK 465 GLY D 672
REMARK 465 SER D 673
REMARK 465 LEU D 674
REMARK 465 SER D 683
REMARK 465 ARG D 719
REMARK 465 GLU D 720
REMARK 465 LEU D 721
REMARK 465 SER D 722
REMARK 465 GLY D 723
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 499 CE NZ
REMARK 470 LYS A 507 NZ
REMARK 470 LYS A 522 CG CD CE NZ
REMARK 470 LEU A 525 CG CD1 CD2
REMARK 470 GLU A 545 CG CD OE1 OE2
REMARK 470 LYS A 547 CG CD CE NZ
REMARK 470 GLU A 549 CG CD OE1 OE2
REMARK 470 LYS A 551 CD CE NZ
REMARK 470 TRP A 604 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 604 CZ3 CH2
REMARK 470 GLN A 636 OE1 NE2
REMARK 470 GLN A 653 CD OE1 NE2
REMARK 470 ASN A 658 CG OD1 ND2
REMARK 470 ILE A 659 CG1 CG2 CD1
REMARK 470 ASN A 660 CG OD1 ND2
REMARK 470 ASP A 663 CG OD1 OD2
REMARK 470 GLN A 664 CG CD OE1 NE2
REMARK 470 ILE A 665 CG1 CG2 CD1
REMARK 470 ILE A 666 CG1 CG2 CD1
REMARK 470 GLU A 667 CG CD OE1 OE2
REMARK 470 ARG A 671 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 680 CE NZ
REMARK 470 SER A 683 OG
REMARK 470 LYS A 687 CG CD CE NZ
REMARK 470 LYS A 690 CD CE NZ
REMARK 470 ARG A 691 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 698 CE NZ
REMARK 470 LYS A 699 CG CD CE NZ
REMARK 470 LYS A 700 CG CD CE NZ
REMARK 470 GLU A 713 CG CD OE1 OE2
REMARK 470 GLN B 461 CG CD OE1 NE2
REMARK 470 SER B 467 OG
REMARK 470 PHE B 468 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 475 CG CD CE NZ
REMARK 470 LEU B 495 CG CD1 CD2
REMARK 470 LYS B 507 NZ
REMARK 470 ARG B 509 NH1 NH2
REMARK 470 LYS B 547 CG CD CE NZ
REMARK 470 GLU B 549 CG CD OE1 OE2
REMARK 470 LYS B 551 CD CE NZ
REMARK 470 ARG B 575 NH1 NH2
REMARK 470 ASN B 658 CG OD1 ND2
REMARK 470 ILE B 659 CG1 CG2 CD1
REMARK 470 ASN B 660 CG OD1 ND2
REMARK 470 ARG B 662 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 663 CG OD1 OD2
REMARK 470 ILE B 665 CG1 CG2 CD1
REMARK 470 GLU B 667 CG CD OE1 OE2
REMARK 470 MET B 668 CG SD CE
REMARK 470 ARG B 671 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 680 CE NZ
REMARK 470 SER B 683 OG
REMARK 470 LYS B 687 CG CD CE NZ
REMARK 470 LYS B 690 CD CE NZ
REMARK 470 ARG B 691 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 698 CE NZ
REMARK 470 LYS B 700 CG CD CE NZ
REMARK 470 ARG B 709 CG CD NE CZ NH1 NH2
REMARK 470 SER C 445 OG
REMARK 470 SER C 467 OG
REMARK 470 PHE C 468 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN C 493 CG CD OE1 NE2
REMARK 470 LYS C 499 CE NZ
REMARK 470 LYS C 507 NZ
REMARK 470 LYS C 522 CE NZ
REMARK 470 GLU C 545 CD OE1 OE2
REMARK 470 LYS C 547 CG CD CE NZ
REMARK 470 GLU C 549 CG CD OE1 OE2
REMARK 470 LYS C 551 CD CE NZ
REMARK 470 LYS C 552 NZ
REMARK 470 GLN C 636 OE1 NE2
REMARK 470 GLN C 653 CD OE1 NE2
REMARK 470 ILE C 659 CG1 CG2 CD1
REMARK 470 ASN C 660 CG OD1 ND2
REMARK 470 ILE C 666 CG1 CG2 CD1
REMARK 470 GLU C 667 CG CD OE1 OE2
REMARK 470 ARG C 682 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 687 CG CD CE NZ
REMARK 470 LYS C 690 CD CE NZ
REMARK 470 ARG C 691 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 698 CE NZ
REMARK 470 LYS C 699 CG CD CE NZ
REMARK 470 LYS C 700 CG CD CE NZ
REMARK 470 ASP C 702 CG OD1 OD2
REMARK 470 ARG C 709 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 446 CG CD OE1 OE2
REMARK 470 SER D 467 OG
REMARK 470 PHE D 468 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS D 475 CG CD CE NZ
REMARK 470 GLN D 493 CG CD OE1 NE2
REMARK 470 LYS D 499 CE NZ
REMARK 470 LYS D 507 NZ
REMARK 470 LYS D 522 CG CD CE NZ
REMARK 470 LYS D 547 CG CD CE NZ
REMARK 470 GLU D 549 CG CD OE1 OE2
REMARK 470 LYS D 551 CD CE NZ
REMARK 470 GLU D 600 CG CD OE1 OE2
REMARK 470 ARG D 626 CG CD NE CZ NH1 NH2
REMARK 470 ASN D 631 CG OD1 ND2
REMARK 470 GLN D 636 OE1 NE2
REMARK 470 LEU D 654 CG CD1 CD2
REMARK 470 LEU D 678 CG CD1 CD2
REMARK 470 SER D 679 OG
REMARK 470 LYS D 680 CG CD CE NZ
REMARK 470 VAL D 681 CG1 CG2
REMARK 470 LYS D 687 CG CD CE NZ
REMARK 470 LYS D 690 CD CE NZ
REMARK 470 ARG D 691 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 698 CE NZ
REMARK 470 LYS D 700 CG CD CE NZ
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 931 O HOH A 944 1.86
REMARK 500 O HOH A 901 O HOH B 901 1.90
REMARK 500 OD1 ASP D 448 O HOH D 801 2.13
REMARK 500 NE2 HIS B 539 O HOH B 901 2.17
REMARK 500 NE2 GLN A 461 O HOH B 901 2.18
REMARK 500 O PRO B 492 N LEU B 495 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO B 453 C - N - CA ANGL. DEV. = 9.5 DEGREES
REMARK 500 PRO B 492 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 PRO B 492 C - N - CD ANGL. DEV. = -13.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PHE A 468 -1.53 66.61
REMARK 500 TRP A 476 -119.86 -111.58
REMARK 500 SER A 535 -148.49 50.07
REMARK 500 ARG A 575 -6.74 79.46
REMARK 500 ASP A 576 28.21 -147.56
REMARK 500 PHE B 468 -4.39 66.64
REMARK 500 PRO B 492 -118.01 0.81
REMARK 500 GLN B 493 -49.53 3.04
REMARK 500 SER B 535 -151.56 49.31
REMARK 500 ARG B 575 -8.57 82.51
REMARK 500 ASP B 576 33.17 -152.50
REMARK 500 ASN B 631 63.42 33.67
REMARK 500 PHE C 468 -3.41 66.85
REMARK 500 TRP C 476 -116.64 -110.62
REMARK 500 SER C 535 -151.14 50.02
REMARK 500 ARG C 575 -10.11 80.65
REMARK 500 ASP C 576 24.19 -146.59
REMARK 500 ILE C 666 -51.62 54.46
REMARK 500 PHE D 468 -2.77 65.44
REMARK 500 PRO D 492 -21.45 -39.45
REMARK 500 SER D 535 -152.35 49.10
REMARK 500 ALA D 543 -70.13 -113.74
REMARK 500 ARG D 575 -10.11 83.18
REMARK 500 ASP D 576 31.59 -149.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 962 DISTANCE = 8.07 ANGSTROMS
REMARK 525 HOH B 963 DISTANCE = 8.90 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BEN A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6NC A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BEN B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6NC C 801
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5JRQ RELATED DB: PDB
REMARK 900 RELATED ID: 5JSM RELATED DB: PDB
DBREF 5JT2 A 448 723 UNP P15056 BRAF_HUMAN 448 723
DBREF 5JT2 B 448 723 UNP P15056 BRAF_HUMAN 448 723
DBREF 5JT2 C 448 723 UNP P15056 BRAF_HUMAN 448 723
DBREF 5JT2 D 448 723 UNP P15056 BRAF_HUMAN 448 723
SEQADV 5JT2 GLY A 444 UNP P15056 EXPRESSION TAG
SEQADV 5JT2 SER A 445 UNP P15056 EXPRESSION TAG
SEQADV 5JT2 GLU A 446 UNP P15056 EXPRESSION TAG
SEQADV 5JT2 PHE A 447 UNP P15056 EXPRESSION TAG
SEQADV 5JT2 ALA A 543 UNP P15056 ILE 543 ENGINEERED MUTATION
SEQADV 5JT2 SER A 544 UNP P15056 ILE 544 ENGINEERED MUTATION
SEQADV 5JT2 LYS A 551 UNP P15056 ILE 551 ENGINEERED MUTATION
SEQADV 5JT2 ARG A 562 UNP P15056 GLN 562 ENGINEERED MUTATION
SEQADV 5JT2 ASN A 588 UNP P15056 LEU 588 ENGINEERED MUTATION
SEQADV 5JT2 GLU A 600 UNP P15056 VAL 600 ENGINEERED MUTATION
SEQADV 5JT2 SER A 630 UNP P15056 LYS 630 ENGINEERED MUTATION
SEQADV 5JT2 GLU A 667 UNP P15056 PHE 667 ENGINEERED MUTATION
SEQADV 5JT2 SER A 673 UNP P15056 TYR 673 ENGINEERED MUTATION
SEQADV 5JT2 ARG A 688 UNP P15056 ALA 688 ENGINEERED MUTATION
SEQADV 5JT2 SER A 706 UNP P15056 LEU 706 ENGINEERED MUTATION
SEQADV 5JT2 ARG A 709 UNP P15056 GLN 709 ENGINEERED MUTATION
SEQADV 5JT2 GLU A 713 UNP P15056 SER 713 ENGINEERED MUTATION
SEQADV 5JT2 GLU A 716 UNP P15056 LEU 716 ENGINEERED MUTATION
SEQADV 5JT2 GLU A 720 UNP P15056 SER 720 ENGINEERED MUTATION
SEQADV 5JT2 SER A 722 UNP P15056 PRO 722 ENGINEERED MUTATION
SEQADV 5JT2 GLY A 723 UNP P15056 LYS 723 ENGINEERED MUTATION
SEQADV 5JT2 GLY B 444 UNP P15056 EXPRESSION TAG
SEQADV 5JT2 SER B 445 UNP P15056 EXPRESSION TAG
SEQADV 5JT2 GLU B 446 UNP P15056 EXPRESSION TAG
SEQADV 5JT2 PHE B 447 UNP P15056 EXPRESSION TAG
SEQADV 5JT2 ALA B 543 UNP P15056 ILE 543 ENGINEERED MUTATION
SEQADV 5JT2 SER B 544 UNP P15056 ILE 544 ENGINEERED MUTATION
SEQADV 5JT2 LYS B 551 UNP P15056 ILE 551 ENGINEERED MUTATION
SEQADV 5JT2 ARG B 562 UNP P15056 GLN 562 ENGINEERED MUTATION
SEQADV 5JT2 ASN B 588 UNP P15056 LEU 588 ENGINEERED MUTATION
SEQADV 5JT2 GLU B 600 UNP P15056 VAL 600 ENGINEERED MUTATION
SEQADV 5JT2 SER B 630 UNP P15056 LYS 630 ENGINEERED MUTATION
SEQADV 5JT2 GLU B 667 UNP P15056 PHE 667 ENGINEERED MUTATION
SEQADV 5JT2 SER B 673 UNP P15056 TYR 673 ENGINEERED MUTATION
SEQADV 5JT2 ARG B 688 UNP P15056 ALA 688 ENGINEERED MUTATION
SEQADV 5JT2 SER B 706 UNP P15056 LEU 706 ENGINEERED MUTATION
SEQADV 5JT2 ARG B 709 UNP P15056 GLN 709 ENGINEERED MUTATION
SEQADV 5JT2 GLU B 713 UNP P15056 SER 713 ENGINEERED MUTATION
SEQADV 5JT2 GLU B 716 UNP P15056 LEU 716 ENGINEERED MUTATION
SEQADV 5JT2 GLU B 720 UNP P15056 SER 720 ENGINEERED MUTATION
SEQADV 5JT2 SER B 722 UNP P15056 PRO 722 ENGINEERED MUTATION
SEQADV 5JT2 GLY B 723 UNP P15056 LYS 723 ENGINEERED MUTATION
SEQADV 5JT2 GLY C 444 UNP P15056 EXPRESSION TAG
SEQADV 5JT2 SER C 445 UNP P15056 EXPRESSION TAG
SEQADV 5JT2 GLU C 446 UNP P15056 EXPRESSION TAG
SEQADV 5JT2 PHE C 447 UNP P15056 EXPRESSION TAG
SEQADV 5JT2 ALA C 543 UNP P15056 ILE 543 ENGINEERED MUTATION
SEQADV 5JT2 SER C 544 UNP P15056 ILE 544 ENGINEERED MUTATION
SEQADV 5JT2 LYS C 551 UNP P15056 ILE 551 ENGINEERED MUTATION
SEQADV 5JT2 ARG C 562 UNP P15056 GLN 562 ENGINEERED MUTATION
SEQADV 5JT2 ASN C 588 UNP P15056 LEU 588 ENGINEERED MUTATION
SEQADV 5JT2 GLU C 600 UNP P15056 VAL 600 ENGINEERED MUTATION
SEQADV 5JT2 SER C 630 UNP P15056 LYS 630 ENGINEERED MUTATION
SEQADV 5JT2 GLU C 667 UNP P15056 PHE 667 ENGINEERED MUTATION
SEQADV 5JT2 SER C 673 UNP P15056 TYR 673 ENGINEERED MUTATION
SEQADV 5JT2 ARG C 688 UNP P15056 ALA 688 ENGINEERED MUTATION
SEQADV 5JT2 SER C 706 UNP P15056 LEU 706 ENGINEERED MUTATION
SEQADV 5JT2 ARG C 709 UNP P15056 GLN 709 ENGINEERED MUTATION
SEQADV 5JT2 GLU C 713 UNP P15056 SER 713 ENGINEERED MUTATION
SEQADV 5JT2 GLU C 716 UNP P15056 LEU 716 ENGINEERED MUTATION
SEQADV 5JT2 GLU C 720 UNP P15056 SER 720 ENGINEERED MUTATION
SEQADV 5JT2 SER C 722 UNP P15056 PRO 722 ENGINEERED MUTATION
SEQADV 5JT2 GLY C 723 UNP P15056 LYS 723 ENGINEERED MUTATION
SEQADV 5JT2 GLY D 444 UNP P15056 EXPRESSION TAG
SEQADV 5JT2 SER D 445 UNP P15056 EXPRESSION TAG
SEQADV 5JT2 GLU D 446 UNP P15056 EXPRESSION TAG
SEQADV 5JT2 PHE D 447 UNP P15056 EXPRESSION TAG
SEQADV 5JT2 ALA D 543 UNP P15056 ILE 543 ENGINEERED MUTATION
SEQADV 5JT2 SER D 544 UNP P15056 ILE 544 ENGINEERED MUTATION
SEQADV 5JT2 LYS D 551 UNP P15056 ILE 551 ENGINEERED MUTATION
SEQADV 5JT2 ARG D 562 UNP P15056 GLN 562 ENGINEERED MUTATION
SEQADV 5JT2 ASN D 588 UNP P15056 LEU 588 ENGINEERED MUTATION
SEQADV 5JT2 GLU D 600 UNP P15056 VAL 600 ENGINEERED MUTATION
SEQADV 5JT2 SER D 630 UNP P15056 LYS 630 ENGINEERED MUTATION
SEQADV 5JT2 GLU D 667 UNP P15056 PHE 667 ENGINEERED MUTATION
SEQADV 5JT2 SER D 673 UNP P15056 TYR 673 ENGINEERED MUTATION
SEQADV 5JT2 ARG D 688 UNP P15056 ALA 688 ENGINEERED MUTATION
SEQADV 5JT2 SER D 706 UNP P15056 LEU 706 ENGINEERED MUTATION
SEQADV 5JT2 ARG D 709 UNP P15056 GLN 709 ENGINEERED MUTATION
SEQADV 5JT2 GLU D 713 UNP P15056 SER 713 ENGINEERED MUTATION
SEQADV 5JT2 GLU D 716 UNP P15056 LEU 716 ENGINEERED MUTATION
SEQADV 5JT2 GLU D 720 UNP P15056 SER 720 ENGINEERED MUTATION
SEQADV 5JT2 SER D 722 UNP P15056 PRO 722 ENGINEERED MUTATION
SEQADV 5JT2 GLY D 723 UNP P15056 LYS 723 ENGINEERED MUTATION
SEQRES 1 A 280 GLY SER GLU PHE ASP ASP TRP GLU ILE PRO ASP GLY GLN
SEQRES 2 A 280 ILE THR VAL GLY GLN ARG ILE GLY SER GLY SER PHE GLY
SEQRES 3 A 280 THR VAL TYR LYS GLY LYS TRP HIS GLY ASP VAL ALA VAL
SEQRES 4 A 280 LYS MET LEU ASN VAL THR ALA PRO THR PRO GLN GLN LEU
SEQRES 5 A 280 GLN ALA PHE LYS ASN GLU VAL GLY VAL LEU ARG LYS THR
SEQRES 6 A 280 ARG HIS VAL ASN ILE LEU LEU PHE MET GLY TYR SER THR
SEQRES 7 A 280 LYS PRO GLN LEU ALA ILE VAL THR GLN TRP CYS GLU GLY
SEQRES 8 A 280 SER SER LEU TYR HIS HIS LEU HIS ALA SER GLU THR LYS
SEQRES 9 A 280 PHE GLU MET LYS LYS LEU ILE ASP ILE ALA ARG GLN THR
SEQRES 10 A 280 ALA ARG GLY MET ASP TYR LEU HIS ALA LYS SER ILE ILE
SEQRES 11 A 280 HIS ARG ASP LEU LYS SER ASN ASN ILE PHE LEU HIS GLU
SEQRES 12 A 280 ASP ASN THR VAL LYS ILE GLY ASP PHE GLY LEU ALA THR
SEQRES 13 A 280 GLU LYS SER ARG TRP SER GLY SER HIS GLN PHE GLU GLN
SEQRES 14 A 280 LEU SER GLY SER ILE LEU TRP MET ALA PRO GLU VAL ILE
SEQRES 15 A 280 ARG MET GLN ASP SER ASN PRO TYR SER PHE GLN SER ASP
SEQRES 16 A 280 VAL TYR ALA PHE GLY ILE VAL LEU TYR GLU LEU MET THR
SEQRES 17 A 280 GLY GLN LEU PRO TYR SER ASN ILE ASN ASN ARG ASP GLN
SEQRES 18 A 280 ILE ILE GLU MET VAL GLY ARG GLY SER LEU SER PRO ASP
SEQRES 19 A 280 LEU SER LYS VAL ARG SER ASN CYS PRO LYS ARG MET LYS
SEQRES 20 A 280 ARG LEU MET ALA GLU CYS LEU LYS LYS LYS ARG ASP GLU
SEQRES 21 A 280 ARG PRO SER PHE PRO ARG ILE LEU ALA GLU ILE GLU GLU
SEQRES 22 A 280 LEU ALA ARG GLU LEU SER GLY
SEQRES 1 B 280 GLY SER GLU PHE ASP ASP TRP GLU ILE PRO ASP GLY GLN
SEQRES 2 B 280 ILE THR VAL GLY GLN ARG ILE GLY SER GLY SER PHE GLY
SEQRES 3 B 280 THR VAL TYR LYS GLY LYS TRP HIS GLY ASP VAL ALA VAL
SEQRES 4 B 280 LYS MET LEU ASN VAL THR ALA PRO THR PRO GLN GLN LEU
SEQRES 5 B 280 GLN ALA PHE LYS ASN GLU VAL GLY VAL LEU ARG LYS THR
SEQRES 6 B 280 ARG HIS VAL ASN ILE LEU LEU PHE MET GLY TYR SER THR
SEQRES 7 B 280 LYS PRO GLN LEU ALA ILE VAL THR GLN TRP CYS GLU GLY
SEQRES 8 B 280 SER SER LEU TYR HIS HIS LEU HIS ALA SER GLU THR LYS
SEQRES 9 B 280 PHE GLU MET LYS LYS LEU ILE ASP ILE ALA ARG GLN THR
SEQRES 10 B 280 ALA ARG GLY MET ASP TYR LEU HIS ALA LYS SER ILE ILE
SEQRES 11 B 280 HIS ARG ASP LEU LYS SER ASN ASN ILE PHE LEU HIS GLU
SEQRES 12 B 280 ASP ASN THR VAL LYS ILE GLY ASP PHE GLY LEU ALA THR
SEQRES 13 B 280 GLU LYS SER ARG TRP SER GLY SER HIS GLN PHE GLU GLN
SEQRES 14 B 280 LEU SER GLY SER ILE LEU TRP MET ALA PRO GLU VAL ILE
SEQRES 15 B 280 ARG MET GLN ASP SER ASN PRO TYR SER PHE GLN SER ASP
SEQRES 16 B 280 VAL TYR ALA PHE GLY ILE VAL LEU TYR GLU LEU MET THR
SEQRES 17 B 280 GLY GLN LEU PRO TYR SER ASN ILE ASN ASN ARG ASP GLN
SEQRES 18 B 280 ILE ILE GLU MET VAL GLY ARG GLY SER LEU SER PRO ASP
SEQRES 19 B 280 LEU SER LYS VAL ARG SER ASN CYS PRO LYS ARG MET LYS
SEQRES 20 B 280 ARG LEU MET ALA GLU CYS LEU LYS LYS LYS ARG ASP GLU
SEQRES 21 B 280 ARG PRO SER PHE PRO ARG ILE LEU ALA GLU ILE GLU GLU
SEQRES 22 B 280 LEU ALA ARG GLU LEU SER GLY
SEQRES 1 C 280 GLY SER GLU PHE ASP ASP TRP GLU ILE PRO ASP GLY GLN
SEQRES 2 C 280 ILE THR VAL GLY GLN ARG ILE GLY SER GLY SER PHE GLY
SEQRES 3 C 280 THR VAL TYR LYS GLY LYS TRP HIS GLY ASP VAL ALA VAL
SEQRES 4 C 280 LYS MET LEU ASN VAL THR ALA PRO THR PRO GLN GLN LEU
SEQRES 5 C 280 GLN ALA PHE LYS ASN GLU VAL GLY VAL LEU ARG LYS THR
SEQRES 6 C 280 ARG HIS VAL ASN ILE LEU LEU PHE MET GLY TYR SER THR
SEQRES 7 C 280 LYS PRO GLN LEU ALA ILE VAL THR GLN TRP CYS GLU GLY
SEQRES 8 C 280 SER SER LEU TYR HIS HIS LEU HIS ALA SER GLU THR LYS
SEQRES 9 C 280 PHE GLU MET LYS LYS LEU ILE ASP ILE ALA ARG GLN THR
SEQRES 10 C 280 ALA ARG GLY MET ASP TYR LEU HIS ALA LYS SER ILE ILE
SEQRES 11 C 280 HIS ARG ASP LEU LYS SER ASN ASN ILE PHE LEU HIS GLU
SEQRES 12 C 280 ASP ASN THR VAL LYS ILE GLY ASP PHE GLY LEU ALA THR
SEQRES 13 C 280 GLU LYS SER ARG TRP SER GLY SER HIS GLN PHE GLU GLN
SEQRES 14 C 280 LEU SER GLY SER ILE LEU TRP MET ALA PRO GLU VAL ILE
SEQRES 15 C 280 ARG MET GLN ASP SER ASN PRO TYR SER PHE GLN SER ASP
SEQRES 16 C 280 VAL TYR ALA PHE GLY ILE VAL LEU TYR GLU LEU MET THR
SEQRES 17 C 280 GLY GLN LEU PRO TYR SER ASN ILE ASN ASN ARG ASP GLN
SEQRES 18 C 280 ILE ILE GLU MET VAL GLY ARG GLY SER LEU SER PRO ASP
SEQRES 19 C 280 LEU SER LYS VAL ARG SER ASN CYS PRO LYS ARG MET LYS
SEQRES 20 C 280 ARG LEU MET ALA GLU CYS LEU LYS LYS LYS ARG ASP GLU
SEQRES 21 C 280 ARG PRO SER PHE PRO ARG ILE LEU ALA GLU ILE GLU GLU
SEQRES 22 C 280 LEU ALA ARG GLU LEU SER GLY
SEQRES 1 D 280 GLY SER GLU PHE ASP ASP TRP GLU ILE PRO ASP GLY GLN
SEQRES 2 D 280 ILE THR VAL GLY GLN ARG ILE GLY SER GLY SER PHE GLY
SEQRES 3 D 280 THR VAL TYR LYS GLY LYS TRP HIS GLY ASP VAL ALA VAL
SEQRES 4 D 280 LYS MET LEU ASN VAL THR ALA PRO THR PRO GLN GLN LEU
SEQRES 5 D 280 GLN ALA PHE LYS ASN GLU VAL GLY VAL LEU ARG LYS THR
SEQRES 6 D 280 ARG HIS VAL ASN ILE LEU LEU PHE MET GLY TYR SER THR
SEQRES 7 D 280 LYS PRO GLN LEU ALA ILE VAL THR GLN TRP CYS GLU GLY
SEQRES 8 D 280 SER SER LEU TYR HIS HIS LEU HIS ALA SER GLU THR LYS
SEQRES 9 D 280 PHE GLU MET LYS LYS LEU ILE ASP ILE ALA ARG GLN THR
SEQRES 10 D 280 ALA ARG GLY MET ASP TYR LEU HIS ALA LYS SER ILE ILE
SEQRES 11 D 280 HIS ARG ASP LEU LYS SER ASN ASN ILE PHE LEU HIS GLU
SEQRES 12 D 280 ASP ASN THR VAL LYS ILE GLY ASP PHE GLY LEU ALA THR
SEQRES 13 D 280 GLU LYS SER ARG TRP SER GLY SER HIS GLN PHE GLU GLN
SEQRES 14 D 280 LEU SER GLY SER ILE LEU TRP MET ALA PRO GLU VAL ILE
SEQRES 15 D 280 ARG MET GLN ASP SER ASN PRO TYR SER PHE GLN SER ASP
SEQRES 16 D 280 VAL TYR ALA PHE GLY ILE VAL LEU TYR GLU LEU MET THR
SEQRES 17 D 280 GLY GLN LEU PRO TYR SER ASN ILE ASN ASN ARG ASP GLN
SEQRES 18 D 280 ILE ILE GLU MET VAL GLY ARG GLY SER LEU SER PRO ASP
SEQRES 19 D 280 LEU SER LYS VAL ARG SER ASN CYS PRO LYS ARG MET LYS
SEQRES 20 D 280 ARG LEU MET ALA GLU CYS LEU LYS LYS LYS ARG ASP GLU
SEQRES 21 D 280 ARG PRO SER PHE PRO ARG ILE LEU ALA GLU ILE GLU GLU
SEQRES 22 D 280 LEU ALA ARG GLU LEU SER GLY
HET BEN A 801 17
HET 6NC A 802 119
HET BEN B 801 17
HET 6NC C 801 119
HETNAM BEN BENZAMIDINE
HETNAM 6NC 2,2'-OXYBIS(N-{[4-(3-{2,6-DIFLUORO-3-[(PROPANE-1-
HETNAM 2 6NC SULFONYL)AMINO]BENZOYL}-1H-PYRROLO[2,3-B]PYRIDIN-5-
HETNAM 3 6NC YL)PHENYL]METHYL}ACETAMIDE)
FORMUL 5 BEN 2(C7 H8 N2)
FORMUL 6 6NC 2(C52 H46 F4 N8 O9 S2)
FORMUL 9 HOH *174(H2 O)
HELIX 1 AA1 GLU A 446 GLU A 451 5 6
HELIX 2 AA2 THR A 491 THR A 508 1 18
HELIX 3 AA3 SER A 536 ALA A 543 1 8
HELIX 4 AA4 GLU A 549 LYS A 570 1 22
HELIX 5 AA5 LEU A 597 ARG A 603 1 7
HELIX 6 AA6 SER A 616 MET A 620 5 5
HELIX 7 AA7 SER A 634 GLY A 652 1 19
HELIX 8 AA8 GLN A 664 ARG A 671 1 8
HELIX 9 AA9 ASP A 677 VAL A 681 5 5
HELIX 10 AB1 PRO A 686 LEU A 697 1 12
HELIX 11 AB2 LYS A 700 ARG A 704 5 5
HELIX 12 AB3 SER A 706 ALA A 718 1 13
HELIX 13 AB4 GLN B 493 THR B 508 1 16
HELIX 14 AB5 SER B 536 ALA B 543 1 8
HELIX 15 AB6 GLU B 549 LYS B 570 1 22
HELIX 16 AB7 LYS B 578 ASN B 580 5 3
HELIX 17 AB8 SER B 616 MET B 620 5 5
HELIX 18 AB9 ALA B 621 ARG B 626 1 6
HELIX 19 AC1 SER B 634 GLY B 652 1 19
HELIX 20 AC2 ASN B 661 ARG B 671 1 11
HELIX 21 AC3 ASP B 677 VAL B 681 5 5
HELIX 22 AC4 PRO B 686 LEU B 697 1 12
HELIX 23 AC5 LYS B 700 ARG B 704 5 5
HELIX 24 AC6 SER B 706 ARG B 719 1 14
HELIX 25 AC7 GLU C 446 GLU C 451 5 6
HELIX 26 AC8 THR C 491 ARG C 506 1 16
HELIX 27 AC9 SER C 536 ALA C 543 1 8
HELIX 28 AD1 GLU C 549 LYS C 570 1 22
HELIX 29 AD2 LYS C 578 ASN C 580 5 3
HELIX 30 AD3 LEU C 597 ARG C 603 1 7
HELIX 31 AD4 ALA C 621 ARG C 626 1 6
HELIX 32 AD5 SER C 634 GLY C 652 1 19
HELIX 33 AD6 ILE C 666 GLY C 672 1 7
HELIX 34 AD7 ASP C 677 VAL C 681 5 5
HELIX 35 AD8 PRO C 686 LEU C 697 1 12
HELIX 36 AD9 LYS C 700 ARG C 704 5 5
HELIX 37 AE1 SER C 706 ALA C 718 1 13
HELIX 38 AE2 THR D 491 ARG D 506 1 16
HELIX 39 AE3 SER D 536 ALA D 543 1 8
HELIX 40 AE4 GLU D 549 LYS D 570 1 22
HELIX 41 AE5 SER D 616 MET D 620 5 5
HELIX 42 AE6 ALA D 621 ARG D 626 1 6
HELIX 43 AE7 SER D 634 GLY D 652 1 19
HELIX 44 AE8 ASP D 677 VAL D 681 5 5
HELIX 45 AE9 PRO D 686 LEU D 697 1 12
HELIX 46 AF1 LYS D 700 ARG D 704 5 5
HELIX 47 AF2 SER D 706 ALA D 718 1 13
SHEET 1 AA1 5 THR A 458 GLY A 466 0
SHEET 2 AA1 5 GLY A 469 LYS A 475 -1 O LYS A 473 N GLN A 461
SHEET 3 AA1 5 ASP A 479 LEU A 485 -1 O MET A 484 N THR A 470
SHEET 4 AA1 5 ALA A 526 GLN A 530 -1 O THR A 529 N ALA A 481
SHEET 5 AA1 5 PHE A 516 SER A 520 -1 N MET A 517 O VAL A 528
SHEET 1 AA2 2 ILE A 582 LEU A 584 0
SHEET 2 AA2 2 VAL A 590 ILE A 592 -1 O LYS A 591 N PHE A 583
SHEET 1 AA3 5 THR B 458 GLY B 466 0
SHEET 2 AA3 5 GLY B 469 LYS B 475 -1 O VAL B 471 N GLY B 464
SHEET 3 AA3 5 ASP B 479 LEU B 485 -1 O MET B 484 N THR B 470
SHEET 4 AA3 5 ALA B 526 GLN B 530 -1 O ILE B 527 N LYS B 483
SHEET 5 AA3 5 PHE B 516 SER B 520 -1 N MET B 517 O VAL B 528
SHEET 1 AA4 2 ILE B 582 LEU B 584 0
SHEET 2 AA4 2 VAL B 590 ILE B 592 -1 O LYS B 591 N PHE B 583
SHEET 1 AA5 5 THR C 458 GLY C 466 0
SHEET 2 AA5 5 GLY C 469 LYS C 475 -1 O LYS C 473 N GLN C 461
SHEET 3 AA5 5 ASP C 479 LEU C 485 -1 O VAL C 482 N TYR C 472
SHEET 4 AA5 5 ALA C 526 GLN C 530 -1 O ILE C 527 N LYS C 483
SHEET 5 AA5 5 PHE C 516 SER C 520 -1 N MET C 517 O VAL C 528
SHEET 1 AA6 2 ILE C 582 LEU C 584 0
SHEET 2 AA6 2 VAL C 590 ILE C 592 -1 O LYS C 591 N PHE C 583
SHEET 1 AA7 5 THR D 458 GLY D 464 0
SHEET 2 AA7 5 GLY D 469 LYS D 475 -1 O LYS D 473 N GLY D 460
SHEET 3 AA7 5 ASP D 479 LEU D 485 -1 O VAL D 482 N TYR D 472
SHEET 4 AA7 5 ALA D 526 GLN D 530 -1 O ILE D 527 N LYS D 483
SHEET 5 AA7 5 PHE D 516 SER D 520 -1 N MET D 517 O VAL D 528
SHEET 1 AA8 2 ILE D 582 LEU D 584 0
SHEET 2 AA8 2 VAL D 590 ILE D 592 -1 O LYS D 591 N PHE D 583
CISPEP 1 LYS A 522 PRO A 523 0 0.44
CISPEP 2 LYS B 522 PRO B 523 0 6.07
CISPEP 3 LYS C 522 PRO C 523 0 2.92
CISPEP 4 LYS D 522 PRO D 523 0 2.48
SITE 1 AC1 7 ASP A 449 TRP A 450 GLU A 451 MET A 517
SITE 2 AC1 7 TRP D 450 ARG D 509 MET D 517
SITE 1 AC2 32 GLN A 461 VAL A 471 ALA A 481 VAL A 482
SITE 2 AC2 32 LYS A 483 LEU A 514 THR A 529 GLN A 530
SITE 3 AC2 32 TRP A 531 CYS A 532 SER A 535 PHE A 583
SITE 4 AC2 32 GLY A 593 ASP A 594 PHE A 595 GLY A 596
SITE 5 AC2 32 HOH A 910 VAL B 471 ALA B 481 LYS B 483
SITE 6 AC2 32 LEU B 505 LEU B 514 THR B 529 GLN B 530
SITE 7 AC2 32 CYS B 532 SER B 535 HIS B 539 PHE B 583
SITE 8 AC2 32 GLY B 593 ASP B 594 PHE B 595 GLY B 596
SITE 1 AC3 8 TRP B 450 PHE B 516 MET B 517 HOH B 945
SITE 2 AC3 8 ASP C 449 TRP C 450 GLU C 451 MET C 517
SITE 1 AC4 34 GLN C 461 ILE C 463 VAL C 471 ALA C 481
SITE 2 AC4 34 LYS C 483 LEU C 514 THR C 529 GLN C 530
SITE 3 AC4 34 TRP C 531 CYS C 532 SER C 535 PHE C 583
SITE 4 AC4 34 GLY C 593 ASP C 594 PHE C 595 GLY C 596
SITE 5 AC4 34 GLN D 461 ILE D 463 VAL D 471 ALA D 481
SITE 6 AC4 34 LYS D 483 LEU D 505 LEU D 514 PHE D 516
SITE 7 AC4 34 THR D 529 GLN D 530 CYS D 532 SER D 535
SITE 8 AC4 34 HIS D 539 PHE D 583 GLY D 593 ASP D 594
SITE 9 AC4 34 PHE D 595 GLY D 596
CRYST1 65.102 68.442 275.603 90.00 90.00 90.00 P 21 21 21 16
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 0.015361 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014611 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003628 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
