HEADER HYDROLASE 07-AUG-11 3TBK
TITLE MOUSE RIG-I ATPASE DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIG-I HELICASE DOMAIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DEAD BOX PROTEIN 58, RETINOIC ACID-INDUCIBLE GENE 1 PROTEIN,
COMPND 5 RIG-1, RETINOIC ACID-INDUCIBLE GENE I PROTEIN, RIG-I;
COMPND 6 EC: 3.6.4.13;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: DDX58;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DECH HELICASE, HELICASE, ATP BINDING, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.CIVRIL,M.D.BENNETT,K.-P.HOPFNER
REVDAT 3 08-NOV-17 3TBK 1 REMARK
REVDAT 2 14-DEC-11 3TBK 1 JRNL
REVDAT 1 26-OCT-11 3TBK 0
JRNL AUTH F.CIVRIL,M.BENNETT,M.MOLDT,T.DEIMLING,G.WITTE,S.SCHIESSER,
JRNL AUTH 2 T.CARELL,K.P.HOPFNER
JRNL TITL THE RIG-I ATPASE DOMAIN STRUCTURE REVEALS INSIGHTS INTO
JRNL TITL 2 ATP-DEPENDENT ANTIVIRAL SIGNALLING.
JRNL REF EMBO REP. V. 12 1127 2011
JRNL REFN ISSN 1469-221X
JRNL PMID 21979817
JRNL DOI 10.1038/EMBOR.2011.190
REMARK 2
REMARK 2 RESOLUTION. 2.14 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743)
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) : 2.14
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.89
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.040
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 34468
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1724
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 43.9000 - 4.8919 1.00 2941 155 0.1958 0.2499
REMARK 3 2 4.8919 - 3.8836 1.00 2790 147 0.1608 0.1574
REMARK 3 3 3.8836 - 3.3929 1.00 2771 146 0.1776 0.2273
REMARK 3 4 3.3929 - 3.0828 1.00 2716 143 0.1875 0.2330
REMARK 3 5 3.0828 - 2.8619 1.00 2741 144 0.1922 0.2644
REMARK 3 6 2.8619 - 2.6932 1.00 2719 143 0.2046 0.2874
REMARK 3 7 2.6932 - 2.5583 1.00 2720 143 0.2110 0.3063
REMARK 3 8 2.5583 - 2.4470 1.00 2693 142 0.2085 0.2900
REMARK 3 9 2.4470 - 2.3528 1.00 2726 144 0.1940 0.2652
REMARK 3 10 2.3528 - 2.2716 1.00 2688 141 0.1780 0.2509
REMARK 3 11 2.2716 - 2.2006 1.00 2673 141 0.1846 0.2183
REMARK 3 12 2.2006 - 2.1400 0.95 2566 135 0.2087 0.2792
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.95
REMARK 3 K_SOL : 0.32
REMARK 3 B_SOL : 33.29
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.620
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.380
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) : -6.17790
REMARK 3 B22 (A**2) : 0.42080
REMARK 3 B33 (A**2) : 5.75710
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 : 0.008 4284
REMARK 3 ANGLE : 1.081 5782
REMARK 3 CHIRALITY : 0.066 662
REMARK 3 PLANARITY : 0.004 734
REMARK 3 DIHEDRAL : 14.234 1636
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 3TBK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-AUG-11.
REMARK 100 THE DEPOSITION ID IS D_1000067278.
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) : 100
REMARK 200 PH : NULL
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) : 0.97972
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
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
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34468
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.140
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
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) : 2.14
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.5
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: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 23.07200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 76.54850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.01350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 76.54850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.07200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.01350
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLU A 577
REMARK 465 ALA A 578
REMARK 465 ALA A 579
REMARK 465 PHE A 580
REMARK 465 ASP A 581
REMARK 465 ARG A 665
REMARK 465 GLY A 666
REMARK 465 ARG A 667
REMARK 465 THR A 668
REMARK 465 ASN A 669
REMARK 465 ARG A 670
REMARK 465 ALA A 671
REMARK 465 THR A 672
REMARK 465 GLY A 673
REMARK 465 MSE A 674
REMARK 465 THR A 675
REMARK 465 LEU A 676
REMARK 465 PRO A 677
REMARK 465 ALA A 678
REMARK 465 GLN A 679
REMARK 465 LYS A 680
REMARK 465 CYS A 681
REMARK 465 VAL A 682
REMARK 465 LEU A 683
REMARK 465 GLU A 684
REMARK 465 ALA A 685
REMARK 465 PHE A 686
REMARK 465 ARG A 687
REMARK 465 ALA A 688
REMARK 465 SER A 689
REMARK 465 GLY A 690
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 509 CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH2 ARG A 735 O HOH A 811 3755 2.11
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 LYS A 380 -129.62 54.45
REMARK 500 VAL A 415 -7.48 -141.79
REMARK 500 ASN A 470 85.96 -153.15
REMARK 500 ALA A 559 -152.22 -137.63
REMARK 500 VAL A 700 88.19 -152.07
REMARK 500 ASP A 702 57.50 -94.20
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 ANP A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 795
DBREF 3TBK A 240 794 UNP Q6Q899 DDX58_MOUSE 240 794
SEQRES 1 A 555 SER PRO LEU LYS PRO ARG ASN TYR GLN LEU GLU LEU ALA
SEQRES 2 A 555 LEU PRO ALA LYS LYS GLY LYS ASN THR ILE ILE CYS ALA
SEQRES 3 A 555 PRO THR GLY CYS GLY LYS THR PHE VAL SER LEU LEU ILE
SEQRES 4 A 555 CYS GLU HIS HIS LEU LYS LYS PHE PRO CYS GLY GLN LYS
SEQRES 5 A 555 GLY LYS VAL VAL PHE PHE ALA ASN GLN ILE PRO VAL TYR
SEQRES 6 A 555 GLU GLN GLN ALA THR VAL PHE SER ARG TYR PHE GLU ARG
SEQRES 7 A 555 LEU GLY TYR ASN ILE ALA SER ILE SER GLY ALA THR SER
SEQRES 8 A 555 ASP SER VAL SER VAL GLN HIS ILE ILE GLU ASP ASN ASP
SEQRES 9 A 555 ILE ILE ILE LEU THR PRO GLN ILE LEU VAL ASN ASN LEU
SEQRES 10 A 555 ASN ASN GLY ALA ILE PRO SER LEU SER VAL PHE THR LEU
SEQRES 11 A 555 MSE ILE PHE ASP GLU CYS HIS ASN THR SER LYS ASN HIS
SEQRES 12 A 555 PRO TYR ASN GLN ILE MSE PHE ARG TYR LEU ASP HIS LYS
SEQRES 13 A 555 LEU GLY GLU SER ARG ASP PRO LEU PRO GLN VAL VAL GLY
SEQRES 14 A 555 LEU THR ALA SER VAL GLY VAL GLY ASP ALA LYS THR ALA
SEQRES 15 A 555 GLU GLU ALA MSE GLN HIS ILE CYS LYS LEU CYS ALA ALA
SEQRES 16 A 555 LEU ASP ALA SER VAL ILE ALA THR VAL ARG ASP ASN VAL
SEQRES 17 A 555 ALA GLU LEU GLU GLN VAL VAL TYR LYS PRO GLN LYS ILE
SEQRES 18 A 555 SER ARG LYS VAL ALA SER ARG THR SER ASN THR PHE LYS
SEQRES 19 A 555 CYS ILE ILE SER GLN LEU MSE LYS GLU THR GLU LYS LEU
SEQRES 20 A 555 ALA LYS ASP VAL SER GLU GLU LEU GLY LYS LEU PHE GLN
SEQRES 21 A 555 ILE GLN ASN ARG GLU PHE GLY THR GLN LYS TYR GLU GLN
SEQRES 22 A 555 TRP ILE VAL GLY VAL HIS LYS ALA CYS SER VAL PHE GLN
SEQRES 23 A 555 MSE ALA ASP LYS GLU GLU GLU SER ARG VAL CYS LYS ALA
SEQRES 24 A 555 LEU PHE LEU TYR THR SER HIS LEU ARG LYS TYR ASN ASP
SEQRES 25 A 555 ALA LEU ILE ILE SER GLU ASP ALA GLN MSE THR ASP ALA
SEQRES 26 A 555 LEU ASN TYR LEU LYS ALA PHE PHE HIS ASP VAL ARG GLU
SEQRES 27 A 555 ALA ALA PHE ASP GLU THR GLU ARG GLU LEU THR ARG ARG
SEQRES 28 A 555 PHE GLU GLU LYS LEU GLU GLU LEU GLU LYS VAL SER ARG
SEQRES 29 A 555 ASP PRO SER ASN GLU ASN PRO LYS LEU ARG ASP LEU TYR
SEQRES 30 A 555 LEU VAL LEU GLN GLU GLU TYR HIS LEU LYS PRO GLU THR
SEQRES 31 A 555 LYS THR ILE LEU PHE VAL LYS THR ARG ALA LEU VAL ASP
SEQRES 32 A 555 ALA LEU LYS LYS TRP ILE GLU GLU ASN PRO ALA LEU SER
SEQRES 33 A 555 PHE LEU LYS PRO GLY ILE LEU THR GLY ARG GLY ARG THR
SEQRES 34 A 555 ASN ARG ALA THR GLY MSE THR LEU PRO ALA GLN LYS CYS
SEQRES 35 A 555 VAL LEU GLU ALA PHE ARG ALA SER GLY ASP ASN ASN ILE
SEQRES 36 A 555 LEU ILE ALA THR SER VAL ALA ASP GLU GLY ILE ASP ILE
SEQRES 37 A 555 ALA GLU CYS ASN LEU VAL ILE LEU TYR GLU TYR VAL GLY
SEQRES 38 A 555 ASN VAL ILE LYS MSE ILE GLN THR ARG GLY ARG GLY ARG
SEQRES 39 A 555 ALA ARG ASP SER LYS CYS PHE LEU LEU THR SER SER ALA
SEQRES 40 A 555 ASP VAL ILE GLU LYS GLU LYS ALA ASN MSE ILE LYS GLU
SEQRES 41 A 555 LYS ILE MSE ASN GLU SER ILE LEU ARG LEU GLN THR TRP
SEQRES 42 A 555 ASP GLU MSE LYS PHE GLY LYS THR VAL HIS ARG ILE GLN
SEQRES 43 A 555 VAL ASN GLU LYS LEU LEU ARG ASP SER
MODRES 3TBK MSE A 370 MET SELENOMETHIONINE
MODRES 3TBK MSE A 388 MET SELENOMETHIONINE
MODRES 3TBK MSE A 425 MET SELENOMETHIONINE
MODRES 3TBK MSE A 480 MET SELENOMETHIONINE
MODRES 3TBK MSE A 526 MET SELENOMETHIONINE
MODRES 3TBK MSE A 561 MET SELENOMETHIONINE
MODRES 3TBK MSE A 725 MET SELENOMETHIONINE
MODRES 3TBK MSE A 756 MET SELENOMETHIONINE
MODRES 3TBK MSE A 762 MET SELENOMETHIONINE
MODRES 3TBK MSE A 775 MET SELENOMETHIONINE
HET MSE A 370 8
HET MSE A 388 8
HET MSE A 425 8
HET MSE A 480 8
HET MSE A 526 8
HET MSE A 561 8
HET MSE A 725 8
HET MSE A 756 8
HET MSE A 762 8
HET MSE A 775 8
HET ANP A 1 31
HET EDO A 795 4
HETNAM MSE SELENOMETHIONINE
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 10(C5 H11 N O2 SE)
FORMUL 2 ANP C10 H17 N6 O12 P3
FORMUL 3 EDO C2 H6 O2
FORMUL 4 HOH *306(H2 O)
HELIX 1 1 ARG A 245 LYS A 257 1 13
HELIX 2 2 GLY A 270 LYS A 285 1 16
HELIX 3 3 GLN A 300 ARG A 317 1 18
HELIX 4 4 THR A 329 VAL A 333 5 5
HELIX 5 5 SER A 334 ASN A 342 1 9
HELIX 6 6 THR A 348 ASN A 358 1 11
HELIX 7 7 SER A 363 PHE A 367 5 5
HELIX 8 8 GLU A 374 THR A 378 5 5
HELIX 9 9 HIS A 382 LEU A 396 1 15
HELIX 10 10 THR A 420 LEU A 435 1 16
HELIX 11 11 ASN A 446 GLN A 452 1 7
HELIX 12 12 ASN A 470 ASP A 489 1 20
HELIX 13 13 SER A 491 LYS A 496 1 6
HELIX 14 14 LEU A 497 ILE A 500 5 4
HELIX 15 15 THR A 507 VAL A 523 1 17
HELIX 16 16 ASP A 528 ALA A 559 1 32
HELIX 17 17 GLN A 560 ARG A 576 1 17
HELIX 18 18 THR A 583 GLU A 593 1 11
HELIX 19 19 LYS A 594 ASP A 604 1 11
HELIX 20 20 PRO A 605 GLU A 608 5 4
HELIX 21 21 ASN A 609 LYS A 626 1 18
HELIX 22 22 THR A 637 ASN A 651 1 15
HELIX 23 23 PRO A 652 SER A 655 5 4
HELIX 24 24 SER A 745 TRP A 772 1 28
HELIX 25 25 ASP A 773 SER A 794 1 22
SHEET 1 A 7 ILE A 322 ILE A 325 0
SHEET 2 A 7 ILE A 344 LEU A 347 1 O ILE A 346 N ALA A 323
SHEET 3 A 7 VAL A 294 PHE A 297 1 N PHE A 296 O ILE A 345
SHEET 4 A 7 LEU A 369 PHE A 372 1 O ILE A 371 N PHE A 297
SHEET 5 A 7 GLN A 405 THR A 410 1 O VAL A 407 N PHE A 372
SHEET 6 A 7 THR A 261 CYS A 264 1 N ILE A 263 O GLY A 408
SHEET 7 A 7 VAL A 439 ALA A 441 1 O VAL A 439 N ILE A 262
SHEET 1 B 6 LYS A 459 LYS A 463 0
SHEET 2 B 6 LYS A 738 THR A 743 1 O LEU A 741 N ARG A 462
SHEET 3 B 6 LEU A 712 TYR A 716 1 N LEU A 715 O PHE A 740
SHEET 4 B 6 THR A 631 PHE A 634 1 N PHE A 634 O ILE A 714
SHEET 5 B 6 ILE A 694 ALA A 697 1 O LEU A 695 N LEU A 633
SHEET 6 B 6 PRO A 659 ILE A 661 1 N GLY A 660 O ILE A 694
SHEET 1 C 2 ILE A 705 ASP A 706 0
SHEET 2 C 2 MSE A 725 ILE A 726 1 O ILE A 726 N ILE A 705
LINK C LEU A 369 N MSE A 370 1555 1555 1.33
LINK C MSE A 370 N ILE A 371 1555 1555 1.32
LINK C ILE A 387 N MSE A 388 1555 1555 1.34
LINK C MSE A 388 N PHE A 389 1555 1555 1.33
LINK C ALA A 424 N MSE A 425 1555 1555 1.33
LINK C MSE A 425 N GLN A 426 1555 1555 1.33
LINK C LEU A 479 N MSE A 480 1555 1555 1.33
LINK C MSE A 480 N LYS A 481 1555 1555 1.33
LINK C GLN A 525 N MSE A 526 1555 1555 1.33
LINK C MSE A 526 N ALA A 527 1555 1555 1.33
LINK C GLN A 560 N MSE A 561 1555 1555 1.33
LINK C MSE A 561 N THR A 562 1555 1555 1.33
LINK C LYS A 724 N MSE A 725 1555 1555 1.33
LINK C MSE A 725 N ILE A 726 1555 1555 1.33
LINK C ASN A 755 N MSE A 756 1555 1555 1.33
LINK C MSE A 756 N ILE A 757 1555 1555 1.33
LINK C ILE A 761 N MSE A 762 1555 1555 1.33
LINK C MSE A 762 N ASN A 763 1555 1555 1.33
LINK C GLU A 774 N MSE A 775 1555 1555 1.33
LINK C MSE A 775 N LYS A 776 1555 1555 1.33
CISPEP 1 ALA A 701 ASP A 702 0 -3.44
SITE 1 AC1 15 HOH A 44 HOH A 137 HOH A 159 HOH A 190
SITE 2 AC1 15 HOH A 231 LYS A 243 ARG A 245 GLN A 248
SITE 3 AC1 15 THR A 267 GLY A 268 CYS A 269 GLY A 270
SITE 4 AC1 15 LYS A 271 THR A 272 PHE A 273
SITE 1 AC2 6 HOH A 113 VAL A 439 ILE A 440 LEU A 769
SITE 2 AC2 6 GLN A 770 HOH A 803
CRYST1 46.144 86.027 153.097 90.00 90.00 90.00 P 21 21 21 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 0.021671 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011624 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006532 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
