HEADER RNA BINDING PROTEIN 21-FEB-17 5X6C
TITLE CRYSTAL STRUCTURE OF SEPRS-SEPCYSE FROM METHANOCALDOCOCCUS JANNASCHII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: O-PHOSPHOSERINE--TRNA(CYS) LIGASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: O-PHOSPHOSERINE--TRNA LIGASE,NON-CANONICAL O-PHOSPHOSERYL-
COMPND 5 TRNA(CYS) SYNTHETASE,O-PHOSPHOSERYL-TRNA(CYS) SYNTHETASE,SEPRS;
COMPND 6 EC: 6.1.1.27;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: UNCHARACTERIZED PROTEIN MJ1481;
COMPND 10 CHAIN: E, F;
COMPND 11 FRAGMENT: UNP RESIDUES 1-24;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOCALDOCOCCUS JANNASCHII DSM 2661;
SOURCE 3 ORGANISM_TAXID: 243232;
SOURCE 4 STRAIN: DSM 2661;
SOURCE 5 GENE: MJ1660;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: METHANOCALDOCOCCUS JANNASCHII;
SOURCE 10 ORGANISM_TAXID: 243232;
SOURCE 11 STRAIN: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
SOURCE 12 GENE: MJ1481;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS O-PHOSPHOSERYL-TRNA SYNTHETASE, MULTIPLE DOMAIN PROTEIN, COILED-COIL
KEYWDS 2 INSERTION, RNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.CHEN,K.KATO,M.YAO
REVDAT 2 22-NOV-23 5X6C 1 REMARK
REVDAT 1 06-DEC-17 5X6C 0
JRNL AUTH M.CHEN,K.KATO,Y.KUBO,Y.TANAKA,Y.LIU,F.LONG,W.B.WHITMAN,
JRNL AUTH 2 P.LILL,C.GATSOGIANNIS,S.RAUNSER,N.SHIMIZU,A.SHINODA,
JRNL AUTH 3 A.NAKAMURA,I.TANAKA,M.YAO
JRNL TITL STRUCTURAL BASIS FOR TRNA-DEPENDENT CYSTEINE BIOSYNTHESIS
JRNL REF NAT COMMUN V. 8 1521 2017
JRNL REFN ESSN 2041-1723
JRNL PMID 29142195
JRNL DOI 10.1038/S41467-017-01543-Y
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.99
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 65625
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 3328
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 47.9946 - 8.9267 0.98 2654 158 0.1801 0.1837
REMARK 3 2 8.9267 - 7.0927 1.00 2673 124 0.1564 0.1561
REMARK 3 3 7.0927 - 6.1983 1.00 2625 135 0.2074 0.2449
REMARK 3 4 6.1983 - 5.6325 1.00 2612 141 0.1938 0.2163
REMARK 3 5 5.6325 - 5.2293 1.00 2625 131 0.1727 0.1906
REMARK 3 6 5.2293 - 4.9213 1.00 2597 134 0.1617 0.1892
REMARK 3 7 4.9213 - 4.6751 1.00 2610 149 0.1417 0.1674
REMARK 3 8 4.6751 - 4.4717 1.00 2598 132 0.1361 0.1629
REMARK 3 9 4.4717 - 4.2997 1.00 2593 141 0.1479 0.1647
REMARK 3 10 4.2997 - 4.1514 1.00 2587 141 0.1440 0.1741
REMARK 3 11 4.1514 - 4.0217 1.00 2589 139 0.1582 0.1831
REMARK 3 12 4.0217 - 3.9068 1.00 2603 130 0.1633 0.2014
REMARK 3 13 3.9068 - 3.8040 1.00 2563 144 0.1826 0.1837
REMARK 3 14 3.8040 - 3.7112 1.00 2600 143 0.1840 0.2359
REMARK 3 15 3.7112 - 3.6269 1.00 2557 142 0.1962 0.2092
REMARK 3 16 3.6269 - 3.5497 1.00 2622 142 0.2122 0.2740
REMARK 3 17 3.5497 - 3.4787 1.00 2571 141 0.2232 0.2846
REMARK 3 18 3.4787 - 3.4131 1.00 2526 134 0.2254 0.2690
REMARK 3 19 3.4131 - 3.3522 1.00 2639 150 0.2467 0.2884
REMARK 3 20 3.3522 - 3.2953 1.00 2554 134 0.2592 0.3059
REMARK 3 21 3.2953 - 3.2422 1.00 2593 131 0.2645 0.2877
REMARK 3 22 3.2422 - 3.1923 1.00 2559 122 0.2756 0.2763
REMARK 3 23 3.1923 - 3.1454 1.00 2599 142 0.2673 0.2904
REMARK 3 24 3.1454 - 3.1011 0.99 2548 148 0.2852 0.3195
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.660
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 : 0.014 9436
REMARK 3 ANGLE : 1.346 12726
REMARK 3 CHIRALITY : 0.063 1400
REMARK 3 PLANARITY : 0.006 1614
REMARK 3 DIHEDRAL : 16.260 3662
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 5X6C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1300002929.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-DEC-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0-7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-5A
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 : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65670
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
REMARK 200 RESOLUTION RANGE LOW (A) : 48.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : 0.13000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 2DU7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 82.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL PH7.0, 0.3M AMMONIUM
REMARK 280 SULFATE, 36% MPD, EVAPORATION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 3
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 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X,-Y+1/2,Z
REMARK 290 15555 -X+1/2,Y,-Z
REMARK 290 16555 X,-Y,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z,-X,-Y+1/2
REMARK 290 19555 -Z,-X+1/2,Y
REMARK 290 20555 -Z+1/2,X,-Y
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z,-X
REMARK 290 23555 Y,-Z,-X+1/2
REMARK 290 24555 -Y,-Z+1/2,X
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 139.91050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 139.91050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 139.91050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 139.91050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 139.91050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 139.91050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 139.91050
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 139.91050
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 139.91050
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 139.91050
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 139.91050
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 139.91050
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 139.91050
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 139.91050
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 139.91050
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 139.91050
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 139.91050
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 139.91050
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 139.91050
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 139.91050
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 139.91050
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 139.91050
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 139.91050
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 139.91050
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 139.91050
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 139.91050
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 139.91050
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 139.91050
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 139.91050
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 139.91050
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 139.91050
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 139.91050
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 139.91050
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 139.91050
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 139.91050
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 139.91050
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 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: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 45500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 87930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -283.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -139.91050
REMARK 350 BIOMT3 2 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 -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 LYS A 2
REMARK 465 LEU A 3
REMARK 465 LYS A 4
REMARK 465 HIS A 5
REMARK 465 LYS A 6
REMARK 465 ARG A 7
REMARK 465 ASP A 8
REMARK 465 ASP A 9
REMARK 465 LYS A 10
REMARK 465 MET B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 LYS B 2
REMARK 465 LEU B 3
REMARK 465 LYS B 4
REMARK 465 HIS B 5
REMARK 465 LYS B 6
REMARK 465 ARG B 7
REMARK 465 ASP B 8
REMARK 465 ASP B 9
REMARK 465 LYS B 10
REMARK 465 MET E -2
REMARK 465 ILE E 25
REMARK 465 ARG E 26
REMARK 465 VAL E 27
REMARK 465 GLU E 28
REMARK 465 LYS E 29
REMARK 465 ASP E 30
REMARK 465 ASP E 31
REMARK 465 LYS E 32
REMARK 465 LYS E 33
REMARK 465 ILE E 34
REMARK 465 SER E 35
REMARK 465 TYR E 36
REMARK 465 LYS E 37
REMARK 465 ASP E 38
REMARK 465 ALA E 39
REMARK 465 LYS E 40
REMARK 465 PRO E 41
REMARK 465 GLY E 42
REMARK 465 LYS E 43
REMARK 465 ILE E 44
REMARK 465 ASP E 45
REMARK 465 VAL E 46
REMARK 465 ASN E 47
REMARK 465 GLU E 48
REMARK 465 PHE E 49
REMARK 465 LYS E 50
REMARK 465 LYS E 51
REMARK 465 ALA E 52
REMARK 465 ILE E 53
REMARK 465 TYR E 54
REMARK 465 LEU E 55
REMARK 465 LEU E 56
REMARK 465 ILE E 57
REMARK 465 GLU E 58
REMARK 465 ALA E 59
REMARK 465 ASP E 60
REMARK 465 ASP E 61
REMARK 465 PHE E 62
REMARK 465 LEU E 63
REMARK 465 TYR E 64
REMARK 465 LYS E 65
REMARK 465 LYS E 66
REMARK 465 ALA E 67
REMARK 465 PRO E 68
REMARK 465 LYS E 69
REMARK 465 HIS E 70
REMARK 465 GLU E 71
REMARK 465 LEU E 72
REMARK 465 ASN E 73
REMARK 465 GLU E 74
REMARK 465 GLU E 75
REMARK 465 GLU E 76
REMARK 465 ALA E 77
REMARK 465 LYS E 78
REMARK 465 GLU E 79
REMARK 465 PHE E 80
REMARK 465 CYS E 81
REMARK 465 LYS E 82
REMARK 465 LEU E 83
REMARK 465 ILE E 84
REMARK 465 ILE E 85
REMARK 465 LYS E 86
REMARK 465 CYS E 87
REMARK 465 GLN E 88
REMARK 465 GLU E 89
REMARK 465 HIS E 90
REMARK 465 LEU E 91
REMARK 465 ASN E 92
REMARK 465 LYS E 93
REMARK 465 ILE E 94
REMARK 465 LEU E 95
REMARK 465 ALA E 96
REMARK 465 ASN E 97
REMARK 465 PHE E 98
REMARK 465 GLY E 99
REMARK 465 PHE E 100
REMARK 465 GLU E 101
REMARK 465 PHE E 102
REMARK 465 GLU E 103
REMARK 465 GLU E 104
REMARK 465 LYS E 105
REMARK 465 GLU E 106
REMARK 465 ILE E 107
REMARK 465 ASP E 108
REMARK 465 GLU E 109
REMARK 465 GLY E 110
REMARK 465 ALA E 111
REMARK 465 LEU E 112
REMARK 465 TYR E 113
REMARK 465 ILE E 114
REMARK 465 VAL E 115
REMARK 465 SER E 116
REMARK 465 ASN E 117
REMARK 465 LYS E 118
REMARK 465 LYS E 119
REMARK 465 LEU E 120
REMARK 465 PHE E 121
REMARK 465 LYS E 122
REMARK 465 LYS E 123
REMARK 465 LEU E 124
REMARK 465 LYS E 125
REMARK 465 ASN E 126
REMARK 465 LYS E 127
REMARK 465 ASN E 128
REMARK 465 PRO E 129
REMARK 465 ASN E 130
REMARK 465 LEU E 131
REMARK 465 LYS E 132
REMARK 465 VAL E 133
REMARK 465 VAL E 134
REMARK 465 CYS E 135
REMARK 465 THR E 136
REMARK 465 GLU E 137
REMARK 465 GLY E 138
REMARK 465 MET E 139
REMARK 465 LEU E 140
REMARK 465 ASP E 141
REMARK 465 ILE E 142
REMARK 465 GLU E 143
REMARK 465 ASP E 144
REMARK 465 MET E 145
REMARK 465 ARG E 146
REMARK 465 ALA E 147
REMARK 465 ILE E 148
REMARK 465 GLY E 149
REMARK 465 VAL E 150
REMARK 465 PRO E 151
REMARK 465 GLU E 152
REMARK 465 LYS E 153
REMARK 465 ALA E 154
REMARK 465 LEU E 155
REMARK 465 GLU E 156
REMARK 465 GLY E 157
REMARK 465 LEU E 158
REMARK 465 LYS E 159
REMARK 465 LYS E 160
REMARK 465 LYS E 161
REMARK 465 VAL E 162
REMARK 465 GLU E 163
REMARK 465 ILE E 164
REMARK 465 ALA E 165
REMARK 465 ARG E 166
REMARK 465 LYS E 167
REMARK 465 ASN E 168
REMARK 465 VAL E 169
REMARK 465 GLU E 170
REMARK 465 ARG E 171
REMARK 465 PHE E 172
REMARK 465 ILE E 173
REMARK 465 GLU E 174
REMARK 465 LYS E 175
REMARK 465 TYR E 176
REMARK 465 LYS E 177
REMARK 465 PRO E 178
REMARK 465 GLU E 179
REMARK 465 LYS E 180
REMARK 465 ILE E 181
REMARK 465 PHE E 182
REMARK 465 VAL E 183
REMARK 465 VAL E 184
REMARK 465 VAL E 185
REMARK 465 GLU E 186
REMARK 465 ASP E 187
REMARK 465 ASP E 188
REMARK 465 LYS E 189
REMARK 465 ASP E 190
REMARK 465 GLU E 191
REMARK 465 LEU E 192
REMARK 465 LEU E 193
REMARK 465 TYR E 194
REMARK 465 LEU E 195
REMARK 465 ARG E 196
REMARK 465 ALA E 197
REMARK 465 LYS E 198
REMARK 465 ASN E 199
REMARK 465 LEU E 200
REMARK 465 TYR E 201
REMARK 465 ASN E 202
REMARK 465 ALA E 203
REMARK 465 GLU E 204
REMARK 465 LYS E 205
REMARK 465 LEU E 206
REMARK 465 ASP E 207
REMARK 465 ALA E 208
REMARK 465 ASP E 209
REMARK 465 GLU E 210
REMARK 465 ILE E 211
REMARK 465 LEU E 212
REMARK 465 ASP E 213
REMARK 465 MET F -2
REMARK 465 ILE F 25
REMARK 465 ARG F 26
REMARK 465 VAL F 27
REMARK 465 GLU F 28
REMARK 465 LYS F 29
REMARK 465 ASP F 30
REMARK 465 ASP F 31
REMARK 465 LYS F 32
REMARK 465 LYS F 33
REMARK 465 ILE F 34
REMARK 465 SER F 35
REMARK 465 TYR F 36
REMARK 465 LYS F 37
REMARK 465 ASP F 38
REMARK 465 ALA F 39
REMARK 465 LYS F 40
REMARK 465 PRO F 41
REMARK 465 GLY F 42
REMARK 465 LYS F 43
REMARK 465 ILE F 44
REMARK 465 ASP F 45
REMARK 465 VAL F 46
REMARK 465 ASN F 47
REMARK 465 GLU F 48
REMARK 465 PHE F 49
REMARK 465 LYS F 50
REMARK 465 LYS F 51
REMARK 465 ALA F 52
REMARK 465 ILE F 53
REMARK 465 TYR F 54
REMARK 465 LEU F 55
REMARK 465 LEU F 56
REMARK 465 ILE F 57
REMARK 465 GLU F 58
REMARK 465 ALA F 59
REMARK 465 ASP F 60
REMARK 465 ASP F 61
REMARK 465 PHE F 62
REMARK 465 LEU F 63
REMARK 465 TYR F 64
REMARK 465 LYS F 65
REMARK 465 LYS F 66
REMARK 465 ALA F 67
REMARK 465 PRO F 68
REMARK 465 LYS F 69
REMARK 465 HIS F 70
REMARK 465 GLU F 71
REMARK 465 LEU F 72
REMARK 465 ASN F 73
REMARK 465 GLU F 74
REMARK 465 GLU F 75
REMARK 465 GLU F 76
REMARK 465 ALA F 77
REMARK 465 LYS F 78
REMARK 465 GLU F 79
REMARK 465 PHE F 80
REMARK 465 CYS F 81
REMARK 465 LYS F 82
REMARK 465 LEU F 83
REMARK 465 ILE F 84
REMARK 465 ILE F 85
REMARK 465 LYS F 86
REMARK 465 CYS F 87
REMARK 465 GLN F 88
REMARK 465 GLU F 89
REMARK 465 HIS F 90
REMARK 465 LEU F 91
REMARK 465 ASN F 92
REMARK 465 LYS F 93
REMARK 465 ILE F 94
REMARK 465 LEU F 95
REMARK 465 ALA F 96
REMARK 465 ASN F 97
REMARK 465 PHE F 98
REMARK 465 GLY F 99
REMARK 465 PHE F 100
REMARK 465 GLU F 101
REMARK 465 PHE F 102
REMARK 465 GLU F 103
REMARK 465 GLU F 104
REMARK 465 LYS F 105
REMARK 465 GLU F 106
REMARK 465 ILE F 107
REMARK 465 ASP F 108
REMARK 465 GLU F 109
REMARK 465 GLY F 110
REMARK 465 ALA F 111
REMARK 465 LEU F 112
REMARK 465 TYR F 113
REMARK 465 ILE F 114
REMARK 465 VAL F 115
REMARK 465 SER F 116
REMARK 465 ASN F 117
REMARK 465 LYS F 118
REMARK 465 LYS F 119
REMARK 465 LEU F 120
REMARK 465 PHE F 121
REMARK 465 LYS F 122
REMARK 465 LYS F 123
REMARK 465 LEU F 124
REMARK 465 LYS F 125
REMARK 465 ASN F 126
REMARK 465 LYS F 127
REMARK 465 ASN F 128
REMARK 465 PRO F 129
REMARK 465 ASN F 130
REMARK 465 LEU F 131
REMARK 465 LYS F 132
REMARK 465 VAL F 133
REMARK 465 VAL F 134
REMARK 465 CYS F 135
REMARK 465 THR F 136
REMARK 465 GLU F 137
REMARK 465 GLY F 138
REMARK 465 MET F 139
REMARK 465 LEU F 140
REMARK 465 ASP F 141
REMARK 465 ILE F 142
REMARK 465 GLU F 143
REMARK 465 ASP F 144
REMARK 465 MET F 145
REMARK 465 ARG F 146
REMARK 465 ALA F 147
REMARK 465 ILE F 148
REMARK 465 GLY F 149
REMARK 465 VAL F 150
REMARK 465 PRO F 151
REMARK 465 GLU F 152
REMARK 465 LYS F 153
REMARK 465 ALA F 154
REMARK 465 LEU F 155
REMARK 465 GLU F 156
REMARK 465 GLY F 157
REMARK 465 LEU F 158
REMARK 465 LYS F 159
REMARK 465 LYS F 160
REMARK 465 LYS F 161
REMARK 465 VAL F 162
REMARK 465 GLU F 163
REMARK 465 ILE F 164
REMARK 465 ALA F 165
REMARK 465 ARG F 166
REMARK 465 LYS F 167
REMARK 465 ASN F 168
REMARK 465 VAL F 169
REMARK 465 GLU F 170
REMARK 465 ARG F 171
REMARK 465 PHE F 172
REMARK 465 ILE F 173
REMARK 465 GLU F 174
REMARK 465 LYS F 175
REMARK 465 TYR F 176
REMARK 465 LYS F 177
REMARK 465 PRO F 178
REMARK 465 GLU F 179
REMARK 465 LYS F 180
REMARK 465 ILE F 181
REMARK 465 PHE F 182
REMARK 465 VAL F 183
REMARK 465 VAL F 184
REMARK 465 VAL F 185
REMARK 465 GLU F 186
REMARK 465 ASP F 187
REMARK 465 ASP F 188
REMARK 465 LYS F 189
REMARK 465 ASP F 190
REMARK 465 GLU F 191
REMARK 465 LEU F 192
REMARK 465 LEU F 193
REMARK 465 TYR F 194
REMARK 465 LEU F 195
REMARK 465 ARG F 196
REMARK 465 ALA F 197
REMARK 465 LYS F 198
REMARK 465 ASN F 199
REMARK 465 LEU F 200
REMARK 465 TYR F 201
REMARK 465 ASN F 202
REMARK 465 ALA F 203
REMARK 465 GLU F 204
REMARK 465 LYS F 205
REMARK 465 LEU F 206
REMARK 465 ASP F 207
REMARK 465 ALA F 208
REMARK 465 ASP F 209
REMARK 465 GLU F 210
REMARK 465 ILE F 211
REMARK 465 LEU F 212
REMARK 465 ASP F 213
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 PHE B 411 OG SER E 15 2.10
REMARK 500 OE1 GLU A 386 NH1 ARG A 407 2.10
REMARK 500 OH TYR A 313 OD1 ASN A 329 2.13
REMARK 500 O PHE A 411 OG SER F 15 2.15
REMARK 500 OD1 ASP B 25 OG1 THR B 28 2.19
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 ASP A 133 -177.85 -63.29
REMARK 500 THR A 191 -160.02 -119.93
REMARK 500 ALA A 244 74.07 -101.28
REMARK 500 TYR A 352 69.29 -113.34
REMARK 500 TYR A 356 -159.37 -128.93
REMARK 500 ASP A 372 -73.32 -72.33
REMARK 500 ASN A 412 -116.22 61.83
REMARK 500 PRO A 507 -94.73 -79.95
REMARK 500 LEU B 117 -100.56 -93.73
REMARK 500 ASP B 133 -177.74 -63.32
REMARK 500 THR B 191 -159.47 -120.71
REMARK 500 ALA B 244 73.72 -101.67
REMARK 500 TYR B 352 69.45 -113.34
REMARK 500 TYR B 356 -159.77 -129.81
REMARK 500 ASP B 372 -74.14 -72.12
REMARK 500 ASN B 412 -115.94 61.61
REMARK 500 PRO B 507 -95.06 -76.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY B 118 ASN B 119 -149.64
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 755 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH B 756 DISTANCE = 6.91 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5X6B RELATED DB: PDB
DBREF 5X6C A -3 549 PDB 5X6C 5X6C -3 549
DBREF 5X6C B -3 549 PDB 5X6C 5X6C -3 549
DBREF 5X6C E 1 213 UNP Q58876 Y1481_METJA 1 213
DBREF 5X6C F 1 213 UNP Q58876 Y1481_METJA 1 213
SEQADV 5X6C MET E -2 UNP Q58876 INITIATING METHIONINE
SEQADV 5X6C ASN E -1 UNP Q58876 EXPRESSION TAG
SEQADV 5X6C HIS E 0 UNP Q58876 EXPRESSION TAG
SEQADV 5X6C MET F -2 UNP Q58876 INITIATING METHIONINE
SEQADV 5X6C ASN F -1 UNP Q58876 EXPRESSION TAG
SEQADV 5X6C HIS F 0 UNP Q58876 EXPRESSION TAG
SEQRES 1 A 553 MET GLY SER SER MET LYS LEU LYS HIS LYS ARG ASP ASP
SEQRES 2 A 553 LYS MET ARG PHE ASP ILE LYS LYS VAL LEU GLU LEU ALA
SEQRES 3 A 553 GLU LYS ASP PHE GLU THR ALA TRP ARG GLU THR ARG ALA
SEQRES 4 A 553 LEU ILE LYS ASP LYS HIS ILE ASP ASN LYS TYR PRO ARG
SEQRES 5 A 553 LEU LYS PRO VAL TYR GLY LYS PRO HIS PRO VAL MET GLU
SEQRES 6 A 553 THR ILE GLU ARG LEU ARG GLN ALA TYR LEU ARG MET GLY
SEQRES 7 A 553 PHE GLU GLU MET ILE ASN PRO VAL ILE VAL ASP GLU MET
SEQRES 8 A 553 GLU ILE TYR LYS GLN PHE GLY PRO GLU ALA MET ALA VAL
SEQRES 9 A 553 LEU ASP ARG CYS PHE TYR LEU ALA GLY LEU PRO ARG PRO
SEQRES 10 A 553 ASP VAL GLY LEU GLY ASN GLU LYS VAL GLU ILE ILE LYS
SEQRES 11 A 553 ASN LEU GLY ILE ASP ILE ASP GLU GLU LYS LYS GLU ARG
SEQRES 12 A 553 LEU ARG GLU VAL LEU HIS LEU TYR LYS LYS GLY ALA ILE
SEQRES 13 A 553 ASP GLY ASP ASP LEU VAL PHE GLU ILE ALA LYS ALA LEU
SEQRES 14 A 553 ASN VAL SER ASN GLU MET GLY LEU LYS VAL LEU GLU THR
SEQRES 15 A 553 ALA PHE PRO GLU PHE LYS ASP LEU LYS PRO GLU SER THR
SEQRES 16 A 553 THR LEU THR LEU ARG SER HIS MET THR SER GLY TRP PHE
SEQRES 17 A 553 ILE THR LEU SER SER LEU ILE LYS LYS ARG LYS LEU PRO
SEQRES 18 A 553 LEU LYS LEU PHE SER ILE ASP ARG CYS PHE ARG ARG GLU
SEQRES 19 A 553 GLN ARG GLU ASP ARG SER HIS LEU MET SER TYR HIS SER
SEQRES 20 A 553 ALA SER CYS VAL VAL VAL GLY GLU ASP VAL SER VAL ASP
SEQRES 21 A 553 ASP GLY LYS VAL VAL ALA GLU GLY LEU LEU ALA GLN PHE
SEQRES 22 A 553 GLY PHE THR LYS PHE LYS PHE LYS PRO ASP GLU LYS LYS
SEQRES 23 A 553 SER LYS TYR TYR THR PRO GLU THR GLN THR GLU VAL TYR
SEQRES 24 A 553 ALA TYR HIS PRO LYS LEU GLY GLU TRP ILE GLU VAL ALA
SEQRES 25 A 553 THR PHE GLY VAL TYR SER PRO ILE ALA LEU ALA LYS TYR
SEQRES 26 A 553 ASN ILE ASP VAL PRO VAL MET ASN LEU GLY LEU GLY VAL
SEQRES 27 A 553 GLU ARG LEU ALA MET ILE ILE TYR GLY TYR GLU ASP VAL
SEQRES 28 A 553 ARG ALA MET VAL TYR PRO GLN PHE TYR GLU TYR ARG LEU
SEQRES 29 A 553 SER ASP ARG ASP ILE ALA GLY MET ILE ARG VAL ASP LYS
SEQRES 30 A 553 VAL PRO ILE LEU ASP GLU PHE TYR ASN PHE ALA ASN GLU
SEQRES 31 A 553 LEU ILE ASP ILE CYS ILE ALA ASN LYS ASP LYS GLU SER
SEQRES 32 A 553 PRO CYS SER VAL GLU VAL LYS ARG GLU PHE ASN PHE ASN
SEQRES 33 A 553 GLY GLU ARG ARG VAL ILE LYS VAL GLU ILE PHE GLU ASN
SEQRES 34 A 553 GLU PRO ASN LYS LYS LEU LEU GLY PRO SER VAL LEU ASN
SEQRES 35 A 553 GLU VAL TYR VAL TYR ASP GLY ASN ILE TYR GLY ILE PRO
SEQRES 36 A 553 PRO THR PHE GLU GLY VAL LYS GLU GLN TYR ILE PRO ILE
SEQRES 37 A 553 LEU LYS LYS ALA LYS GLU GLU GLY VAL SER THR ASN ILE
SEQRES 38 A 553 ARG TYR ILE ASP GLY ILE ILE TYR LYS LEU VAL ALA LYS
SEQRES 39 A 553 ILE GLU GLU ALA LEU VAL SER ASN VAL ASP GLU PHE LYS
SEQRES 40 A 553 PHE ARG VAL PRO ILE VAL ARG SER LEU SER ASP ILE ASN
SEQRES 41 A 553 LEU LYS ILE ASP GLU LEU ALA LEU LYS GLN ILE MET GLY
SEQRES 42 A 553 GLU ASN LYS VAL ILE ASP VAL ARG GLY PRO VAL PHE LEU
SEQRES 43 A 553 ASN ALA LYS VAL GLU ILE LYS
SEQRES 1 B 553 MET GLY SER SER MET LYS LEU LYS HIS LYS ARG ASP ASP
SEQRES 2 B 553 LYS MET ARG PHE ASP ILE LYS LYS VAL LEU GLU LEU ALA
SEQRES 3 B 553 GLU LYS ASP PHE GLU THR ALA TRP ARG GLU THR ARG ALA
SEQRES 4 B 553 LEU ILE LYS ASP LYS HIS ILE ASP ASN LYS TYR PRO ARG
SEQRES 5 B 553 LEU LYS PRO VAL TYR GLY LYS PRO HIS PRO VAL MET GLU
SEQRES 6 B 553 THR ILE GLU ARG LEU ARG GLN ALA TYR LEU ARG MET GLY
SEQRES 7 B 553 PHE GLU GLU MET ILE ASN PRO VAL ILE VAL ASP GLU MET
SEQRES 8 B 553 GLU ILE TYR LYS GLN PHE GLY PRO GLU ALA MET ALA VAL
SEQRES 9 B 553 LEU ASP ARG CYS PHE TYR LEU ALA GLY LEU PRO ARG PRO
SEQRES 10 B 553 ASP VAL GLY LEU GLY ASN GLU LYS VAL GLU ILE ILE LYS
SEQRES 11 B 553 ASN LEU GLY ILE ASP ILE ASP GLU GLU LYS LYS GLU ARG
SEQRES 12 B 553 LEU ARG GLU VAL LEU HIS LEU TYR LYS LYS GLY ALA ILE
SEQRES 13 B 553 ASP GLY ASP ASP LEU VAL PHE GLU ILE ALA LYS ALA LEU
SEQRES 14 B 553 ASN VAL SER ASN GLU MET GLY LEU LYS VAL LEU GLU THR
SEQRES 15 B 553 ALA PHE PRO GLU PHE LYS ASP LEU LYS PRO GLU SER THR
SEQRES 16 B 553 THR LEU THR LEU ARG SER HIS MET THR SER GLY TRP PHE
SEQRES 17 B 553 ILE THR LEU SER SER LEU ILE LYS LYS ARG LYS LEU PRO
SEQRES 18 B 553 LEU LYS LEU PHE SER ILE ASP ARG CYS PHE ARG ARG GLU
SEQRES 19 B 553 GLN ARG GLU ASP ARG SER HIS LEU MET SER TYR HIS SER
SEQRES 20 B 553 ALA SER CYS VAL VAL VAL GLY GLU ASP VAL SER VAL ASP
SEQRES 21 B 553 ASP GLY LYS VAL VAL ALA GLU GLY LEU LEU ALA GLN PHE
SEQRES 22 B 553 GLY PHE THR LYS PHE LYS PHE LYS PRO ASP GLU LYS LYS
SEQRES 23 B 553 SER LYS TYR TYR THR PRO GLU THR GLN THR GLU VAL TYR
SEQRES 24 B 553 ALA TYR HIS PRO LYS LEU GLY GLU TRP ILE GLU VAL ALA
SEQRES 25 B 553 THR PHE GLY VAL TYR SER PRO ILE ALA LEU ALA LYS TYR
SEQRES 26 B 553 ASN ILE ASP VAL PRO VAL MET ASN LEU GLY LEU GLY VAL
SEQRES 27 B 553 GLU ARG LEU ALA MET ILE ILE TYR GLY TYR GLU ASP VAL
SEQRES 28 B 553 ARG ALA MET VAL TYR PRO GLN PHE TYR GLU TYR ARG LEU
SEQRES 29 B 553 SER ASP ARG ASP ILE ALA GLY MET ILE ARG VAL ASP LYS
SEQRES 30 B 553 VAL PRO ILE LEU ASP GLU PHE TYR ASN PHE ALA ASN GLU
SEQRES 31 B 553 LEU ILE ASP ILE CYS ILE ALA ASN LYS ASP LYS GLU SER
SEQRES 32 B 553 PRO CYS SER VAL GLU VAL LYS ARG GLU PHE ASN PHE ASN
SEQRES 33 B 553 GLY GLU ARG ARG VAL ILE LYS VAL GLU ILE PHE GLU ASN
SEQRES 34 B 553 GLU PRO ASN LYS LYS LEU LEU GLY PRO SER VAL LEU ASN
SEQRES 35 B 553 GLU VAL TYR VAL TYR ASP GLY ASN ILE TYR GLY ILE PRO
SEQRES 36 B 553 PRO THR PHE GLU GLY VAL LYS GLU GLN TYR ILE PRO ILE
SEQRES 37 B 553 LEU LYS LYS ALA LYS GLU GLU GLY VAL SER THR ASN ILE
SEQRES 38 B 553 ARG TYR ILE ASP GLY ILE ILE TYR LYS LEU VAL ALA LYS
SEQRES 39 B 553 ILE GLU GLU ALA LEU VAL SER ASN VAL ASP GLU PHE LYS
SEQRES 40 B 553 PHE ARG VAL PRO ILE VAL ARG SER LEU SER ASP ILE ASN
SEQRES 41 B 553 LEU LYS ILE ASP GLU LEU ALA LEU LYS GLN ILE MET GLY
SEQRES 42 B 553 GLU ASN LYS VAL ILE ASP VAL ARG GLY PRO VAL PHE LEU
SEQRES 43 B 553 ASN ALA LYS VAL GLU ILE LYS
SEQRES 1 E 216 MET ASN HIS MET ARG VAL GLU TYR SER LYS ASP LEU ILE
SEQRES 2 E 216 ARG LYS GLY ILE SER THR ILE SER GLN LEU LYS LYS ALA
SEQRES 3 E 216 LYS ILE ARG VAL GLU LYS ASP ASP LYS LYS ILE SER TYR
SEQRES 4 E 216 LYS ASP ALA LYS PRO GLY LYS ILE ASP VAL ASN GLU PHE
SEQRES 5 E 216 LYS LYS ALA ILE TYR LEU LEU ILE GLU ALA ASP ASP PHE
SEQRES 6 E 216 LEU TYR LYS LYS ALA PRO LYS HIS GLU LEU ASN GLU GLU
SEQRES 7 E 216 GLU ALA LYS GLU PHE CYS LYS LEU ILE ILE LYS CYS GLN
SEQRES 8 E 216 GLU HIS LEU ASN LYS ILE LEU ALA ASN PHE GLY PHE GLU
SEQRES 9 E 216 PHE GLU GLU LYS GLU ILE ASP GLU GLY ALA LEU TYR ILE
SEQRES 10 E 216 VAL SER ASN LYS LYS LEU PHE LYS LYS LEU LYS ASN LYS
SEQRES 11 E 216 ASN PRO ASN LEU LYS VAL VAL CYS THR GLU GLY MET LEU
SEQRES 12 E 216 ASP ILE GLU ASP MET ARG ALA ILE GLY VAL PRO GLU LYS
SEQRES 13 E 216 ALA LEU GLU GLY LEU LYS LYS LYS VAL GLU ILE ALA ARG
SEQRES 14 E 216 LYS ASN VAL GLU ARG PHE ILE GLU LYS TYR LYS PRO GLU
SEQRES 15 E 216 LYS ILE PHE VAL VAL VAL GLU ASP ASP LYS ASP GLU LEU
SEQRES 16 E 216 LEU TYR LEU ARG ALA LYS ASN LEU TYR ASN ALA GLU LYS
SEQRES 17 E 216 LEU ASP ALA ASP GLU ILE LEU ASP
SEQRES 1 F 216 MET ASN HIS MET ARG VAL GLU TYR SER LYS ASP LEU ILE
SEQRES 2 F 216 ARG LYS GLY ILE SER THR ILE SER GLN LEU LYS LYS ALA
SEQRES 3 F 216 LYS ILE ARG VAL GLU LYS ASP ASP LYS LYS ILE SER TYR
SEQRES 4 F 216 LYS ASP ALA LYS PRO GLY LYS ILE ASP VAL ASN GLU PHE
SEQRES 5 F 216 LYS LYS ALA ILE TYR LEU LEU ILE GLU ALA ASP ASP PHE
SEQRES 6 F 216 LEU TYR LYS LYS ALA PRO LYS HIS GLU LEU ASN GLU GLU
SEQRES 7 F 216 GLU ALA LYS GLU PHE CYS LYS LEU ILE ILE LYS CYS GLN
SEQRES 8 F 216 GLU HIS LEU ASN LYS ILE LEU ALA ASN PHE GLY PHE GLU
SEQRES 9 F 216 PHE GLU GLU LYS GLU ILE ASP GLU GLY ALA LEU TYR ILE
SEQRES 10 F 216 VAL SER ASN LYS LYS LEU PHE LYS LYS LEU LYS ASN LYS
SEQRES 11 F 216 ASN PRO ASN LEU LYS VAL VAL CYS THR GLU GLY MET LEU
SEQRES 12 F 216 ASP ILE GLU ASP MET ARG ALA ILE GLY VAL PRO GLU LYS
SEQRES 13 F 216 ALA LEU GLU GLY LEU LYS LYS LYS VAL GLU ILE ALA ARG
SEQRES 14 F 216 LYS ASN VAL GLU ARG PHE ILE GLU LYS TYR LYS PRO GLU
SEQRES 15 F 216 LYS ILE PHE VAL VAL VAL GLU ASP ASP LYS ASP GLU LEU
SEQRES 16 F 216 LEU TYR LEU ARG ALA LYS ASN LEU TYR ASN ALA GLU LYS
SEQRES 17 F 216 LEU ASP ALA ASP GLU ILE LEU ASP
HET ATP A 601 31
HET SO4 A 602 5
HET ATP B 601 31
HET SO4 B 602 5
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETNAM SO4 SULFATE ION
FORMUL 5 ATP 2(C10 H16 N5 O13 P3)
FORMUL 6 SO4 2(O4 S 2-)
FORMUL 9 HOH *109(H2 O)
HELIX 1 AA1 ASP A 14 ASP A 25 1 12
HELIX 2 AA2 ASP A 25 THR A 33 1 9
HELIX 3 AA3 ARG A 34 ILE A 37 5 4
HELIX 4 AA4 HIS A 41 LYS A 45 5 5
HELIX 5 AA5 HIS A 57 ARG A 72 1 16
HELIX 6 AA6 GLU A 86 GLY A 94 1 9
HELIX 7 AA7 GLU A 96 LEU A 101 1 6
HELIX 8 AA8 ASN A 119 LEU A 128 1 10
HELIX 9 AA9 ASP A 133 LYS A 149 1 17
HELIX 10 AB1 ASP A 153 ASP A 155 5 3
HELIX 11 AB2 ASP A 156 ASN A 166 1 11
HELIX 12 AB3 SER A 168 PHE A 180 1 13
HELIX 13 AB4 PRO A 181 LEU A 186 5 6
HELIX 14 AB5 MET A 199 ILE A 211 1 13
HELIX 15 AB6 LYS A 212 ARG A 214 5 3
HELIX 16 AB7 SER A 254 GLN A 268 1 15
HELIX 17 AB8 SER A 314 TYR A 321 1 8
HELIX 18 AB9 VAL A 334 GLY A 343 1 10
HELIX 19 AC1 ASP A 346 TYR A 352 1 7
HELIX 20 AC2 PRO A 353 TYR A 356 5 4
HELIX 21 AC3 SER A 361 GLY A 367 1 7
HELIX 22 AC4 LEU A 377 ASN A 394 1 18
HELIX 23 AC5 GLN A 460 GLY A 472 1 13
HELIX 24 AC6 TYR A 479 SER A 497 1 19
HELIX 25 AC7 LEU A 512 ILE A 515 5 4
HELIX 26 AC8 ASP A 520 GLU A 530 1 11
HELIX 27 AC9 ASP B 14 ASP B 25 1 12
HELIX 28 AD1 ASP B 25 THR B 33 1 9
HELIX 29 AD2 ARG B 34 ILE B 37 5 4
HELIX 30 AD3 HIS B 41 LYS B 45 5 5
HELIX 31 AD4 HIS B 57 ARG B 72 1 16
HELIX 32 AD5 GLU B 86 GLY B 94 1 9
HELIX 33 AD6 GLU B 96 LEU B 101 1 6
HELIX 34 AD7 GLY B 118 LEU B 128 1 11
HELIX 35 AD8 ASP B 133 LYS B 149 1 17
HELIX 36 AD9 ASP B 156 ASN B 166 1 11
HELIX 37 AE1 SER B 168 PHE B 180 1 13
HELIX 38 AE2 PRO B 181 LEU B 186 5 6
HELIX 39 AE3 MET B 199 ILE B 211 1 13
HELIX 40 AE4 LYS B 212 ARG B 214 5 3
HELIX 41 AE5 SER B 254 GLN B 268 1 15
HELIX 42 AE6 SER B 314 LYS B 320 1 7
HELIX 43 AE7 VAL B 334 GLY B 343 1 10
HELIX 44 AE8 ASP B 346 TYR B 352 1 7
HELIX 45 AE9 PRO B 353 TYR B 356 5 4
HELIX 46 AF1 SER B 361 GLY B 367 1 7
HELIX 47 AF2 LEU B 377 LYS B 395 1 19
HELIX 48 AF3 GLN B 460 GLY B 472 1 13
HELIX 49 AF4 TYR B 479 SER B 497 1 19
HELIX 50 AF5 LEU B 512 ILE B 515 5 4
HELIX 51 AF6 ASP B 520 GLU B 530 1 11
HELIX 52 AF7 HIS E 0 LYS E 24 1 25
HELIX 53 AF8 HIS F 0 LYS F 24 1 25
SHEET 1 AA1 7 GLU A 76 GLU A 77 0
SHEET 2 AA1 7 LEU A 218 PHE A 227 1 O LYS A 219 N GLU A 76
SHEET 3 AA1 7 SER A 240 VAL A 249 -1 O TYR A 241 N CYS A 226
SHEET 4 AA1 7 VAL A 327 GLY A 333 -1 O LEU A 332 N ALA A 244
SHEET 5 AA1 7 TRP A 304 VAL A 312 -1 N THR A 309 O GLY A 331
SHEET 6 AA1 7 THR A 292 TYR A 297 -1 N THR A 292 O PHE A 310
SHEET 7 AA1 7 PHE A 274 PRO A 278 -1 N LYS A 275 O TYR A 295
SHEET 1 AA2 3 ILE A 83 ASP A 85 0
SHEET 2 AA2 3 GLU A 189 LEU A 195 -1 O THR A 194 N VAL A 84
SHEET 3 AA2 3 TYR A 106 GLY A 109 -1 N LEU A 107 O LEU A 193
SHEET 1 AA3 2 ILE A 369 VAL A 371 0
SHEET 2 AA3 2 LEU A 517 ILE A 519 -1 O LYS A 518 N ARG A 370
SHEET 1 AA4 4 CYS A 401 PHE A 411 0
SHEET 2 AA4 4 GLU A 414 GLU A 424 -1 O ARG A 416 N PHE A 409
SHEET 3 AA4 4 GLY A 538 LYS A 549 -1 O GLU A 547 N LYS A 419
SHEET 4 AA4 4 GLU A 501 VAL A 509 -1 N VAL A 509 O GLY A 538
SHEET 1 AA5 4 VAL A 473 ARG A 478 0
SHEET 2 AA5 4 GLU A 439 TYR A 443 -1 N VAL A 442 O VAL A 473
SHEET 3 AA5 4 ASN A 446 ILE A 450 -1 O TYR A 448 N TYR A 441
SHEET 4 AA5 4 ILE A 534 ASP A 535 1 O ASP A 535 N ILE A 447
SHEET 1 AA6 7 GLU B 76 GLU B 77 0
SHEET 2 AA6 7 LEU B 218 PHE B 227 1 O LYS B 219 N GLU B 76
SHEET 3 AA6 7 SER B 240 VAL B 249 -1 O TYR B 241 N CYS B 226
SHEET 4 AA6 7 VAL B 327 GLY B 333 -1 O LEU B 332 N ALA B 244
SHEET 5 AA6 7 TRP B 304 VAL B 312 -1 N THR B 309 O GLY B 331
SHEET 6 AA6 7 THR B 292 TYR B 297 -1 N THR B 292 O PHE B 310
SHEET 7 AA6 7 PHE B 274 PRO B 278 -1 N LYS B 275 O TYR B 295
SHEET 1 AA7 3 ILE B 83 ASP B 85 0
SHEET 2 AA7 3 GLU B 189 LEU B 195 -1 O THR B 194 N VAL B 84
SHEET 3 AA7 3 TYR B 106 GLY B 109 -1 N LEU B 107 O LEU B 193
SHEET 1 AA8 2 ILE B 369 VAL B 371 0
SHEET 2 AA8 2 LEU B 517 ILE B 519 -1 O LYS B 518 N ARG B 370
SHEET 1 AA9 4 CYS B 401 PHE B 411 0
SHEET 2 AA9 4 GLU B 414 GLU B 424 -1 O ILE B 418 N ARG B 407
SHEET 3 AA9 4 GLY B 538 ILE B 548 -1 O GLU B 547 N LYS B 419
SHEET 4 AA9 4 GLU B 501 VAL B 509 -1 N VAL B 509 O GLY B 538
SHEET 1 AB1 4 VAL B 473 ARG B 478 0
SHEET 2 AB1 4 GLU B 439 TYR B 443 -1 N VAL B 442 O VAL B 473
SHEET 3 AB1 4 ASN B 446 ILE B 450 -1 O TYR B 448 N TYR B 441
SHEET 4 AB1 4 ILE B 534 ASP B 535 1 O ASP B 535 N ILE B 447
CISPEP 1 TYR A 46 PRO A 47 0 8.89
CISPEP 2 GLY A 118 ASN A 119 0 -27.56
CISPEP 3 LEU A 216 PRO A 217 0 6.91
CISPEP 4 SER A 399 PRO A 400 0 -1.87
CISPEP 5 TYR B 46 PRO B 47 0 8.87
CISPEP 6 LEU B 216 PRO B 217 0 6.24
CISPEP 7 SER B 399 PRO B 400 0 -2.12
SITE 1 AC1 13 ASP A 155 ARG A 228 GLU A 230 HIS A 237
SITE 2 AC1 13 LEU A 238 TYR A 241 LYS A 281 GLU A 306
SITE 3 AC1 13 VAL A 307 ALA A 308 GLY A 333 ARG A 336
SITE 4 AC1 13 HOH A 704
SITE 1 AC2 8 HIS A 198 MET A 199 THR A 200 SER A 243
SITE 2 AC2 8 SER A 245 ASN A 329 LEU A 330 GLY A 331
SITE 1 AC3 14 ASP B 155 ARG B 228 GLU B 230 HIS B 237
SITE 2 AC3 14 LEU B 238 TYR B 241 LYS B 281 GLU B 306
SITE 3 AC3 14 VAL B 307 ALA B 308 THR B 309 GLY B 333
SITE 4 AC3 14 ARG B 336 HOH B 704
SITE 1 AC4 7 HIS B 198 MET B 199 THR B 200 SER B 243
SITE 2 AC4 7 SER B 245 ASN B 329 GLY B 331
CRYST1 279.821 279.821 279.821 90.00 90.00 90.00 I 21 3 48
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 0.003574 0.000000 0.000000 0.00000
SCALE2 0.000000 0.003574 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003574 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
