HEADER CIRCADIAN CLOCK PROTEIN, TRANSFERASE 23-SEP-09 3JZM
TITLE CRYSTAL STRUCTURE OF THE PHOSPHORYLATION-SITE MUTANT T432A OF THE KAIC
TITLE 2 CIRCADIAN CLOCK PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CIRCADIAN CLOCK PROTEIN KINASE KAIC;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 EC: 2.7.11.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNECHOCOCCUS ELONGATUS PCC 7942;
SOURCE 3 ORGANISM_COMMON: ANACYSTIS NIDULANS R2;
SOURCE 4 ORGANISM_TAXID: 1140;
SOURCE 5 STRAIN: PCC7942;
SOURCE 6 GENE: KAIC, SEE0011, SYNPCC7942_1216;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET3
KEYWDS KAIC, CIRCADIAN CLOCK PROTEIN, KINASE, HEXAMER, ATP-BINDING,
KEYWDS 2 BIOLOGICAL RHYTHMS, DNA-BINDING, MAGNESIUM, METAL-BINDING,
KEYWDS 3 NUCLEOTIDE-BINDING, PHOSPHOPROTEIN, REPRESSOR, SERINE/THREONINE-
KEYWDS 4 PROTEIN KINASE, TRANSCRIPTION, TRANSCRIPTION REGULATION, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.PATTANAYEK,M.EGLI,S.PATTANAYEK
REVDAT 3 06-SEP-23 3JZM 1 REMARK
REVDAT 2 13-OCT-21 3JZM 1 REMARK SEQADV LINK
REVDAT 1 31-MAR-10 3JZM 0
JRNL AUTH R.PATTANAYEK,T.MORI,Y.XU,S.PATTANAYEK,C.H.JOHNSON,M.EGLI
JRNL TITL STRUCTURES OF KAIC CIRCADIAN CLOCK MUTANT PROTEINS: A NEW
JRNL TITL 2 PHOSPHORYLATION SITE AT T426 AND MECHANISMS OF KINASE,
JRNL TITL 3 ATPASE AND PHOSPHATASE.
JRNL REF PLOS ONE V. 4 E7529 2009
JRNL REFN ESSN 1932-6203
JRNL PMID 19956664
JRNL DOI 10.1371/JOURNAL.PONE.0007529
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.24
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.0
REMARK 3 NUMBER OF REFLECTIONS : 75321
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.282
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 7551
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.92
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 1.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3520
REMARK 3 BIN FREE R VALUE : 0.4010
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 148
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 22902
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 390
REMARK 3 SOLVENT ATOMS : 63
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3JZM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-OCT-09.
REMARK 100 THE DEPOSITION ID IS D_1000055359.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-FEB-08
REMARK 200 TEMPERATURE (KELVIN) : 113.15
REMARK 200 PH : 4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
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 : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR 300MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77061
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 6.240
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.56400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 2GBL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM FORMATE, GLYCEROL, PH 4, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 66.18500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 102.25000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 67.55500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 102.25000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 66.18500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 67.55500
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 53420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 91230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -282.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 SER A 3
REMARK 465 ALA A 4
REMARK 465 GLU A 5
REMARK 465 MET A 6
REMARK 465 THR A 7
REMARK 465 SER A 8
REMARK 465 PRO A 9
REMARK 465 ASN A 10
REMARK 465 ASN A 11
REMARK 465 ASN A 12
REMARK 465 SER A 13
REMARK 465 THR A 498
REMARK 465 VAL A 499
REMARK 465 ASP A 500
REMARK 465 GLU A 501
REMARK 465 LYS A 502
REMARK 465 SER A 503
REMARK 465 GLU A 504
REMARK 465 LEU A 505
REMARK 465 SER A 506
REMARK 465 ARG A 507
REMARK 465 ILE A 508
REMARK 465 VAL A 509
REMARK 465 ARG A 510
REMARK 465 GLY A 511
REMARK 465 VAL A 512
REMARK 465 GLN A 513
REMARK 465 GLU A 514
REMARK 465 LYS A 515
REMARK 465 GLY A 516
REMARK 465 PRO A 517
REMARK 465 GLU A 518
REMARK 465 SER A 519
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 SER B 3
REMARK 465 ALA B 4
REMARK 465 GLU B 5
REMARK 465 MET B 6
REMARK 465 THR B 7
REMARK 465 SER B 8
REMARK 465 PRO B 9
REMARK 465 ASN B 10
REMARK 465 ASN B 11
REMARK 465 ASN B 12
REMARK 465 SER B 13
REMARK 465 THR B 498
REMARK 465 VAL B 499
REMARK 465 ASP B 500
REMARK 465 GLU B 501
REMARK 465 LYS B 502
REMARK 465 SER B 503
REMARK 465 GLU B 504
REMARK 465 LEU B 505
REMARK 465 SER B 506
REMARK 465 ARG B 507
REMARK 465 ILE B 508
REMARK 465 VAL B 509
REMARK 465 ARG B 510
REMARK 465 GLY B 511
REMARK 465 VAL B 512
REMARK 465 GLN B 513
REMARK 465 GLU B 514
REMARK 465 LYS B 515
REMARK 465 GLY B 516
REMARK 465 PRO B 517
REMARK 465 GLU B 518
REMARK 465 SER B 519
REMARK 465 MET C 1
REMARK 465 THR C 2
REMARK 465 SER C 3
REMARK 465 ALA C 4
REMARK 465 GLU C 5
REMARK 465 MET C 6
REMARK 465 THR C 7
REMARK 465 SER C 8
REMARK 465 PRO C 9
REMARK 465 ASN C 10
REMARK 465 ASN C 11
REMARK 465 ASN C 12
REMARK 465 SER C 13
REMARK 465 THR C 498
REMARK 465 VAL C 499
REMARK 465 ASP C 500
REMARK 465 GLU C 501
REMARK 465 LYS C 502
REMARK 465 SER C 503
REMARK 465 GLU C 504
REMARK 465 LEU C 505
REMARK 465 SER C 506
REMARK 465 ARG C 507
REMARK 465 ILE C 508
REMARK 465 VAL C 509
REMARK 465 ARG C 510
REMARK 465 GLY C 511
REMARK 465 VAL C 512
REMARK 465 GLN C 513
REMARK 465 GLU C 514
REMARK 465 LYS C 515
REMARK 465 GLY C 516
REMARK 465 PRO C 517
REMARK 465 GLU C 518
REMARK 465 SER C 519
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 SER D 3
REMARK 465 ALA D 4
REMARK 465 GLU D 5
REMARK 465 MET D 6
REMARK 465 THR D 7
REMARK 465 SER D 8
REMARK 465 PRO D 9
REMARK 465 ASN D 10
REMARK 465 ASN D 11
REMARK 465 ASN D 12
REMARK 465 SER D 13
REMARK 465 THR D 498
REMARK 465 VAL D 499
REMARK 465 ASP D 500
REMARK 465 GLU D 501
REMARK 465 LYS D 502
REMARK 465 SER D 503
REMARK 465 GLU D 504
REMARK 465 LEU D 505
REMARK 465 SER D 506
REMARK 465 ARG D 507
REMARK 465 ILE D 508
REMARK 465 VAL D 509
REMARK 465 ARG D 510
REMARK 465 GLY D 511
REMARK 465 VAL D 512
REMARK 465 GLN D 513
REMARK 465 GLU D 514
REMARK 465 LYS D 515
REMARK 465 GLY D 516
REMARK 465 PRO D 517
REMARK 465 GLU D 518
REMARK 465 SER D 519
REMARK 465 MET E 1
REMARK 465 THR E 2
REMARK 465 SER E 3
REMARK 465 ALA E 4
REMARK 465 GLU E 5
REMARK 465 MET E 6
REMARK 465 THR E 7
REMARK 465 SER E 8
REMARK 465 PRO E 9
REMARK 465 ASN E 10
REMARK 465 ASN E 11
REMARK 465 ASN E 12
REMARK 465 SER E 13
REMARK 465 THR E 498
REMARK 465 VAL E 499
REMARK 465 ASP E 500
REMARK 465 GLU E 501
REMARK 465 LYS E 502
REMARK 465 SER E 503
REMARK 465 GLU E 504
REMARK 465 LEU E 505
REMARK 465 SER E 506
REMARK 465 ARG E 507
REMARK 465 ILE E 508
REMARK 465 VAL E 509
REMARK 465 ARG E 510
REMARK 465 GLY E 511
REMARK 465 VAL E 512
REMARK 465 GLN E 513
REMARK 465 GLU E 514
REMARK 465 LYS E 515
REMARK 465 GLY E 516
REMARK 465 PRO E 517
REMARK 465 GLU E 518
REMARK 465 SER E 519
REMARK 465 MET F 1
REMARK 465 THR F 2
REMARK 465 SER F 3
REMARK 465 ALA F 4
REMARK 465 GLU F 5
REMARK 465 MET F 6
REMARK 465 THR F 7
REMARK 465 SER F 8
REMARK 465 PRO F 9
REMARK 465 ASN F 10
REMARK 465 ASN F 11
REMARK 465 ASN F 12
REMARK 465 SER F 13
REMARK 465 THR F 498
REMARK 465 VAL F 499
REMARK 465 ASP F 500
REMARK 465 GLU F 501
REMARK 465 LYS F 502
REMARK 465 SER F 503
REMARK 465 GLU F 504
REMARK 465 LEU F 505
REMARK 465 SER F 506
REMARK 465 ARG F 507
REMARK 465 ILE F 508
REMARK 465 VAL F 509
REMARK 465 ARG F 510
REMARK 465 GLY F 511
REMARK 465 VAL F 512
REMARK 465 GLN F 513
REMARK 465 GLU F 514
REMARK 465 LYS F 515
REMARK 465 GLY F 516
REMARK 465 PRO F 517
REMARK 465 GLU F 518
REMARK 465 SER F 519
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 ALA A 17 -126.33 -49.81
REMARK 500 MET A 24 5.74 53.01
REMARK 500 GLU A 77 -60.39 -129.77
REMARK 500 SER A 89 -39.37 -38.61
REMARK 500 PRO A 112 -0.58 -51.59
REMARK 500 VAL A 117 98.27 27.97
REMARK 500 SER A 146 69.58 60.05
REMARK 500 GLN A 152 32.20 -87.79
REMARK 500 TYR A 154 50.13 163.44
REMARK 500 ARG A 184 -165.40 -113.04
REMARK 500 ILE A 185 -23.28 -149.64
REMARK 500 LEU A 211 -116.91 -70.16
REMARK 500 GLU A 212 98.63 83.11
REMARK 500 GLU A 214 -6.59 58.16
REMARK 500 THR A 240 -166.74 -111.62
REMARK 500 LEU A 249 -12.80 -46.60
REMARK 500 LEU A 254 57.30 -96.87
REMARK 500 LYS A 309 69.96 34.74
REMARK 500 SER A 320 -176.26 -66.66
REMARK 500 MET A 333 126.42 -12.45
REMARK 500 VAL A 347 -75.63 -93.96
REMARK 500 CYS A 348 127.69 76.29
REMARK 500 ALA A 349 136.45 -179.84
REMARK 500 SER A 379 92.09 83.75
REMARK 500 MET A 420 123.49 59.81
REMARK 500 ALA A 422 124.07 -39.65
REMARK 500 HIS A 429 46.29 76.37
REMARK 500 SEP A 431 -19.07 -43.03
REMARK 500 ARG A 446 50.39 39.92
REMARK 500 HIS A 463 139.55 47.81
REMARK 500 LYS A 480 -133.11 -90.65
REMARK 500 PRO A 494 -173.17 -63.21
REMARK 500 HIS B 15 40.47 -90.29
REMARK 500 ALA B 17 175.07 -55.16
REMARK 500 TYR B 61 -70.62 -65.72
REMARK 500 ASN B 62 -31.36 -39.10
REMARK 500 PHE B 67 13.18 -147.88
REMARK 500 GLU B 77 -66.54 -128.17
REMARK 500 GLU B 100 19.16 -68.98
REMARK 500 ALA B 108 15.93 -140.34
REMARK 500 GLN B 115 -153.01 -137.35
REMARK 500 VAL B 118 59.85 -112.18
REMARK 500 TYR B 132 -70.87 -51.16
REMARK 500 TYR B 154 49.41 166.61
REMARK 500 ARG B 193 -50.60 -25.87
REMARK 500 ASN B 209 62.71 -119.79
REMARK 500 LEU B 211 -107.11 -71.76
REMARK 500 GLU B 212 101.19 77.59
REMARK 500 GLU B 214 -2.88 60.45
REMARK 500 THR B 240 -165.89 -112.82
REMARK 500
REMARK 500 THIS ENTRY HAS 202 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 701 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 53 OG1
REMARK 620 2 GLU A 78 OE2 140.7
REMARK 620 3 ATP A 903 O2G 76.2 139.2
REMARK 620 4 ATP A 903 O3G 85.3 118.7 69.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 801 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 295 OG1
REMARK 620 2 GLU A 318 OE1 136.1
REMARK 620 3 ATP A 901 O2G 117.1 102.3
REMARK 620 4 ATP A 901 O3B 89.4 127.1 63.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 802 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 415 OG1
REMARK 620 2 ATP A 901 O1G 151.5
REMARK 620 3 ATP A 901 O3B 132.9 75.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 801 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 295 OG1
REMARK 620 2 GLU B 318 OE1 147.7
REMARK 620 3 ATP B 901 O2G 111.6 100.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 520 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 78 OE2
REMARK 620 2 ATP C 903 O2G 133.0
REMARK 620 3 ATP C 903 O3G 136.3 73.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 801 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 295 OG1
REMARK 620 2 ATP C 901 O2G 138.9
REMARK 620 3 ATP C 901 O3B 100.9 69.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 702 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR D 53 OG1
REMARK 620 2 GLU D 78 OE2 105.1
REMARK 620 3 ATP D 903 O2G 61.8 136.4
REMARK 620 4 ATP D 903 O3G 54.3 82.0 56.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 802 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR D 295 OG1
REMARK 620 2 ATP D 901 O2G 149.1
REMARK 620 3 ATP D 901 O3A 95.4 115.4
REMARK 620 4 ATP D 901 O3B 132.8 68.7 62.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 701 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP D 903 O1G
REMARK 620 2 ATP D 903 O3B 61.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 702 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR E 53 OG1
REMARK 620 2 ASP E 145 OD2 84.5
REMARK 620 3 ATP E 903 O2G 70.1 123.8
REMARK 620 4 ATP E 903 O3B 79.5 160.1 61.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 801 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR E 295 OG1
REMARK 620 2 ATP E 901 O2G 127.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 701 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP E 903 O1G
REMARK 620 2 ATP E 903 O2B 79.5
REMARK 620 3 ATP E 903 O3B 60.1 52.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 702 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY F 49 N
REMARK 620 2 ATP F 903 O1G 164.0
REMARK 620 3 ATP F 903 O3G 97.8 68.8
REMARK 620 4 ATP F 903 O3B 105.1 60.7 56.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 701 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR F 53 OG1
REMARK 620 2 ATP F 903 O2G 132.0
REMARK 620 3 ATP F 903 O3B 114.2 69.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 802 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR F 295 OG1
REMARK 620 2 GLU F 318 OE1 135.0
REMARK 620 3 ATP F 901 O2G 96.0 120.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 801 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR F 415 OG1
REMARK 620 2 ATP F 901 O1G 129.5
REMARK 620 N 1
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 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 527
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP C 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP C 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP D 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP D 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP E 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP E 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP F 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP F 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 801
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3DVL RELATED DB: PDB
REMARK 900 RELATED ID: 3K09 RELATED DB: PDB
REMARK 900 RELATED ID: 3K0A RELATED DB: PDB
REMARK 900 RELATED ID: 3K0C RELATED DB: PDB
REMARK 900 RELATED ID: 3K0E RELATED DB: PDB
REMARK 900 RELATED ID: 3K0F RELATED DB: PDB
DBREF 3JZM A 1 519 UNP Q79PF4 KAIC_SYNE7 1 519
DBREF 3JZM B 1 519 UNP Q79PF4 KAIC_SYNE7 1 519
DBREF 3JZM C 1 519 UNP Q79PF4 KAIC_SYNE7 1 519
DBREF 3JZM D 1 519 UNP Q79PF4 KAIC_SYNE7 1 519
DBREF 3JZM E 1 519 UNP Q79PF4 KAIC_SYNE7 1 519
DBREF 3JZM F 1 519 UNP Q79PF4 KAIC_SYNE7 1 519
SEQADV 3JZM ALA A 432 UNP Q79PF4 THR 432 ENGINEERED MUTATION
SEQADV 3JZM ALA B 432 UNP Q79PF4 THR 432 ENGINEERED MUTATION
SEQADV 3JZM ALA C 432 UNP Q79PF4 THR 432 ENGINEERED MUTATION
SEQADV 3JZM ALA D 432 UNP Q79PF4 THR 432 ENGINEERED MUTATION
SEQADV 3JZM ALA E 432 UNP Q79PF4 THR 432 ENGINEERED MUTATION
SEQADV 3JZM ALA F 432 UNP Q79PF4 THR 432 ENGINEERED MUTATION
SEQRES 1 A 519 MET THR SER ALA GLU MET THR SER PRO ASN ASN ASN SER
SEQRES 2 A 519 GLU HIS GLN ALA ILE ALA LYS MET ARG THR MET ILE GLU
SEQRES 3 A 519 GLY PHE ASP ASP ILE SER HIS GLY GLY LEU PRO ILE GLY
SEQRES 4 A 519 ARG SER THR LEU VAL SER GLY THR SER GLY THR GLY LYS
SEQRES 5 A 519 THR LEU PHE SER ILE GLN PHE LEU TYR ASN GLY ILE ILE
SEQRES 6 A 519 GLU PHE ASP GLU PRO GLY VAL PHE VAL THR PHE GLU GLU
SEQRES 7 A 519 THR PRO GLN ASP ILE ILE LYS ASN ALA ARG SER PHE GLY
SEQRES 8 A 519 TRP ASP LEU ALA LYS LEU VAL ASP GLU GLY LYS LEU PHE
SEQRES 9 A 519 ILE LEU ASP ALA SER PRO ASP PRO GLU GLY GLN GLU VAL
SEQRES 10 A 519 VAL GLY GLY PHE ASP LEU SER ALA LEU ILE GLU ARG ILE
SEQRES 11 A 519 ASN TYR ALA ILE GLN LYS TYR ARG ALA ARG ARG VAL SER
SEQRES 12 A 519 ILE ASP SER VAL THR SER VAL PHE GLN GLN TYR ASP ALA
SEQRES 13 A 519 SER SER VAL VAL ARG ARG GLU LEU PHE ARG LEU VAL ALA
SEQRES 14 A 519 ARG LEU LYS GLN ILE GLY ALA THR THR VAL MET THR THR
SEQRES 15 A 519 GLU ARG ILE GLU GLU TYR GLY PRO ILE ALA ARG TYR GLY
SEQRES 16 A 519 VAL GLU GLU PHE VAL SER ASP ASN VAL VAL ILE LEU ARG
SEQRES 17 A 519 ASN VAL LEU GLU GLY GLU ARG ARG ARG ARG THR LEU GLU
SEQRES 18 A 519 ILE LEU LYS LEU ARG GLY THR SER HIS MET LYS GLY GLU
SEQRES 19 A 519 TYR PRO PHE THR ILE THR ASP HIS GLY ILE ASN ILE PHE
SEQRES 20 A 519 PRO LEU GLY ALA MET ARG LEU THR GLN ARG SER SER ASN
SEQRES 21 A 519 VAL ARG VAL SER SER GLY VAL VAL ARG LEU ASP GLU MET
SEQRES 22 A 519 CYS GLY GLY GLY PHE PHE LYS ASP SER ILE ILE LEU ALA
SEQRES 23 A 519 THR GLY ALA THR GLY THR GLY LYS THR LEU LEU VAL SER
SEQRES 24 A 519 ARG PHE VAL GLU ASN ALA CYS ALA ASN LYS GLU ARG ALA
SEQRES 25 A 519 ILE LEU PHE ALA TYR GLU GLU SER ARG ALA GLN LEU LEU
SEQRES 26 A 519 ARG ASN ALA TYR SER TRP GLY MET ASP PHE GLU GLU MET
SEQRES 27 A 519 GLU ARG GLN ASN LEU LEU LYS ILE VAL CYS ALA TYR PRO
SEQRES 28 A 519 GLU SER ALA GLY LEU GLU ASP HIS LEU GLN ILE ILE LYS
SEQRES 29 A 519 SER GLU ILE ASN ASP PHE LYS PRO ALA ARG ILE ALA ILE
SEQRES 30 A 519 ASP SER LEU SER ALA LEU ALA ARG GLY VAL SER ASN ASN
SEQRES 31 A 519 ALA PHE ARG GLN PHE VAL ILE GLY VAL THR GLY TYR ALA
SEQRES 32 A 519 LYS GLN GLU GLU ILE THR GLY LEU PHE THR ASN THR SER
SEQRES 33 A 519 ASP GLN PHE MET GLY ALA HIS SER ILE THR ASP SER HIS
SEQRES 34 A 519 ILE SEP ALA ILE THR ASP THR ILE ILE LEU LEU GLN TYR
SEQRES 35 A 519 VAL GLU ILE ARG GLY GLU MET SER ARG ALA ILE ASN VAL
SEQRES 36 A 519 PHE LYS MET ARG GLY SER TRP HIS ASP LYS ALA ILE ARG
SEQRES 37 A 519 GLU PHE MET ILE SER ASP LYS GLY PRO ASP ILE LYS ASP
SEQRES 38 A 519 SER PHE ARG ASN PHE GLU ARG ILE ILE SER GLY SER PRO
SEQRES 39 A 519 THR ARG ILE THR VAL ASP GLU LYS SER GLU LEU SER ARG
SEQRES 40 A 519 ILE VAL ARG GLY VAL GLN GLU LYS GLY PRO GLU SER
SEQRES 1 B 519 MET THR SER ALA GLU MET THR SER PRO ASN ASN ASN SER
SEQRES 2 B 519 GLU HIS GLN ALA ILE ALA LYS MET ARG THR MET ILE GLU
SEQRES 3 B 519 GLY PHE ASP ASP ILE SER HIS GLY GLY LEU PRO ILE GLY
SEQRES 4 B 519 ARG SER THR LEU VAL SER GLY THR SER GLY THR GLY LYS
SEQRES 5 B 519 THR LEU PHE SER ILE GLN PHE LEU TYR ASN GLY ILE ILE
SEQRES 6 B 519 GLU PHE ASP GLU PRO GLY VAL PHE VAL THR PHE GLU GLU
SEQRES 7 B 519 THR PRO GLN ASP ILE ILE LYS ASN ALA ARG SER PHE GLY
SEQRES 8 B 519 TRP ASP LEU ALA LYS LEU VAL ASP GLU GLY LYS LEU PHE
SEQRES 9 B 519 ILE LEU ASP ALA SER PRO ASP PRO GLU GLY GLN GLU VAL
SEQRES 10 B 519 VAL GLY GLY PHE ASP LEU SER ALA LEU ILE GLU ARG ILE
SEQRES 11 B 519 ASN TYR ALA ILE GLN LYS TYR ARG ALA ARG ARG VAL SER
SEQRES 12 B 519 ILE ASP SER VAL THR SER VAL PHE GLN GLN TYR ASP ALA
SEQRES 13 B 519 SER SER VAL VAL ARG ARG GLU LEU PHE ARG LEU VAL ALA
SEQRES 14 B 519 ARG LEU LYS GLN ILE GLY ALA THR THR VAL MET THR THR
SEQRES 15 B 519 GLU ARG ILE GLU GLU TYR GLY PRO ILE ALA ARG TYR GLY
SEQRES 16 B 519 VAL GLU GLU PHE VAL SER ASP ASN VAL VAL ILE LEU ARG
SEQRES 17 B 519 ASN VAL LEU GLU GLY GLU ARG ARG ARG ARG THR LEU GLU
SEQRES 18 B 519 ILE LEU LYS LEU ARG GLY THR SER HIS MET LYS GLY GLU
SEQRES 19 B 519 TYR PRO PHE THR ILE THR ASP HIS GLY ILE ASN ILE PHE
SEQRES 20 B 519 PRO LEU GLY ALA MET ARG LEU THR GLN ARG SER SER ASN
SEQRES 21 B 519 VAL ARG VAL SER SER GLY VAL VAL ARG LEU ASP GLU MET
SEQRES 22 B 519 CYS GLY GLY GLY PHE PHE LYS ASP SER ILE ILE LEU ALA
SEQRES 23 B 519 THR GLY ALA THR GLY THR GLY LYS THR LEU LEU VAL SER
SEQRES 24 B 519 ARG PHE VAL GLU ASN ALA CYS ALA ASN LYS GLU ARG ALA
SEQRES 25 B 519 ILE LEU PHE ALA TYR GLU GLU SER ARG ALA GLN LEU LEU
SEQRES 26 B 519 ARG ASN ALA TYR SER TRP GLY MET ASP PHE GLU GLU MET
SEQRES 27 B 519 GLU ARG GLN ASN LEU LEU LYS ILE VAL CYS ALA TYR PRO
SEQRES 28 B 519 GLU SER ALA GLY LEU GLU ASP HIS LEU GLN ILE ILE LYS
SEQRES 29 B 519 SER GLU ILE ASN ASP PHE LYS PRO ALA ARG ILE ALA ILE
SEQRES 30 B 519 ASP SER LEU SER ALA LEU ALA ARG GLY VAL SER ASN ASN
SEQRES 31 B 519 ALA PHE ARG GLN PHE VAL ILE GLY VAL THR GLY TYR ALA
SEQRES 32 B 519 LYS GLN GLU GLU ILE THR GLY LEU PHE THR ASN THR SER
SEQRES 33 B 519 ASP GLN PHE MET GLY ALA HIS SER ILE THR ASP SER HIS
SEQRES 34 B 519 ILE SEP ALA ILE THR ASP THR ILE ILE LEU LEU GLN TYR
SEQRES 35 B 519 VAL GLU ILE ARG GLY GLU MET SER ARG ALA ILE ASN VAL
SEQRES 36 B 519 PHE LYS MET ARG GLY SER TRP HIS ASP LYS ALA ILE ARG
SEQRES 37 B 519 GLU PHE MET ILE SER ASP LYS GLY PRO ASP ILE LYS ASP
SEQRES 38 B 519 SER PHE ARG ASN PHE GLU ARG ILE ILE SER GLY SER PRO
SEQRES 39 B 519 THR ARG ILE THR VAL ASP GLU LYS SER GLU LEU SER ARG
SEQRES 40 B 519 ILE VAL ARG GLY VAL GLN GLU LYS GLY PRO GLU SER
SEQRES 1 C 519 MET THR SER ALA GLU MET THR SER PRO ASN ASN ASN SER
SEQRES 2 C 519 GLU HIS GLN ALA ILE ALA LYS MET ARG THR MET ILE GLU
SEQRES 3 C 519 GLY PHE ASP ASP ILE SER HIS GLY GLY LEU PRO ILE GLY
SEQRES 4 C 519 ARG SER THR LEU VAL SER GLY THR SER GLY THR GLY LYS
SEQRES 5 C 519 THR LEU PHE SER ILE GLN PHE LEU TYR ASN GLY ILE ILE
SEQRES 6 C 519 GLU PHE ASP GLU PRO GLY VAL PHE VAL THR PHE GLU GLU
SEQRES 7 C 519 THR PRO GLN ASP ILE ILE LYS ASN ALA ARG SER PHE GLY
SEQRES 8 C 519 TRP ASP LEU ALA LYS LEU VAL ASP GLU GLY LYS LEU PHE
SEQRES 9 C 519 ILE LEU ASP ALA SER PRO ASP PRO GLU GLY GLN GLU VAL
SEQRES 10 C 519 VAL GLY GLY PHE ASP LEU SER ALA LEU ILE GLU ARG ILE
SEQRES 11 C 519 ASN TYR ALA ILE GLN LYS TYR ARG ALA ARG ARG VAL SER
SEQRES 12 C 519 ILE ASP SER VAL THR SER VAL PHE GLN GLN TYR ASP ALA
SEQRES 13 C 519 SER SER VAL VAL ARG ARG GLU LEU PHE ARG LEU VAL ALA
SEQRES 14 C 519 ARG LEU LYS GLN ILE GLY ALA THR THR VAL MET THR THR
SEQRES 15 C 519 GLU ARG ILE GLU GLU TYR GLY PRO ILE ALA ARG TYR GLY
SEQRES 16 C 519 VAL GLU GLU PHE VAL SER ASP ASN VAL VAL ILE LEU ARG
SEQRES 17 C 519 ASN VAL LEU GLU GLY GLU ARG ARG ARG ARG THR LEU GLU
SEQRES 18 C 519 ILE LEU LYS LEU ARG GLY THR SER HIS MET LYS GLY GLU
SEQRES 19 C 519 TYR PRO PHE THR ILE THR ASP HIS GLY ILE ASN ILE PHE
SEQRES 20 C 519 PRO LEU GLY ALA MET ARG LEU THR GLN ARG SER SER ASN
SEQRES 21 C 519 VAL ARG VAL SER SER GLY VAL VAL ARG LEU ASP GLU MET
SEQRES 22 C 519 CYS GLY GLY GLY PHE PHE LYS ASP SER ILE ILE LEU ALA
SEQRES 23 C 519 THR GLY ALA THR GLY THR GLY LYS THR LEU LEU VAL SER
SEQRES 24 C 519 ARG PHE VAL GLU ASN ALA CYS ALA ASN LYS GLU ARG ALA
SEQRES 25 C 519 ILE LEU PHE ALA TYR GLU GLU SER ARG ALA GLN LEU LEU
SEQRES 26 C 519 ARG ASN ALA TYR SER TRP GLY MET ASP PHE GLU GLU MET
SEQRES 27 C 519 GLU ARG GLN ASN LEU LEU LYS ILE VAL CYS ALA TYR PRO
SEQRES 28 C 519 GLU SER ALA GLY LEU GLU ASP HIS LEU GLN ILE ILE LYS
SEQRES 29 C 519 SER GLU ILE ASN ASP PHE LYS PRO ALA ARG ILE ALA ILE
SEQRES 30 C 519 ASP SER LEU SER ALA LEU ALA ARG GLY VAL SER ASN ASN
SEQRES 31 C 519 ALA PHE ARG GLN PHE VAL ILE GLY VAL THR GLY TYR ALA
SEQRES 32 C 519 LYS GLN GLU GLU ILE THR GLY LEU PHE THR ASN THR SER
SEQRES 33 C 519 ASP GLN PHE MET GLY ALA HIS SER ILE THR ASP SER HIS
SEQRES 34 C 519 ILE SEP ALA ILE THR ASP THR ILE ILE LEU LEU GLN TYR
SEQRES 35 C 519 VAL GLU ILE ARG GLY GLU MET SER ARG ALA ILE ASN VAL
SEQRES 36 C 519 PHE LYS MET ARG GLY SER TRP HIS ASP LYS ALA ILE ARG
SEQRES 37 C 519 GLU PHE MET ILE SER ASP LYS GLY PRO ASP ILE LYS ASP
SEQRES 38 C 519 SER PHE ARG ASN PHE GLU ARG ILE ILE SER GLY SER PRO
SEQRES 39 C 519 THR ARG ILE THR VAL ASP GLU LYS SER GLU LEU SER ARG
SEQRES 40 C 519 ILE VAL ARG GLY VAL GLN GLU LYS GLY PRO GLU SER
SEQRES 1 D 519 MET THR SER ALA GLU MET THR SER PRO ASN ASN ASN SER
SEQRES 2 D 519 GLU HIS GLN ALA ILE ALA LYS MET ARG THR MET ILE GLU
SEQRES 3 D 519 GLY PHE ASP ASP ILE SER HIS GLY GLY LEU PRO ILE GLY
SEQRES 4 D 519 ARG SER THR LEU VAL SER GLY THR SER GLY THR GLY LYS
SEQRES 5 D 519 THR LEU PHE SER ILE GLN PHE LEU TYR ASN GLY ILE ILE
SEQRES 6 D 519 GLU PHE ASP GLU PRO GLY VAL PHE VAL THR PHE GLU GLU
SEQRES 7 D 519 THR PRO GLN ASP ILE ILE LYS ASN ALA ARG SER PHE GLY
SEQRES 8 D 519 TRP ASP LEU ALA LYS LEU VAL ASP GLU GLY LYS LEU PHE
SEQRES 9 D 519 ILE LEU ASP ALA SER PRO ASP PRO GLU GLY GLN GLU VAL
SEQRES 10 D 519 VAL GLY GLY PHE ASP LEU SER ALA LEU ILE GLU ARG ILE
SEQRES 11 D 519 ASN TYR ALA ILE GLN LYS TYR ARG ALA ARG ARG VAL SER
SEQRES 12 D 519 ILE ASP SER VAL THR SER VAL PHE GLN GLN TYR ASP ALA
SEQRES 13 D 519 SER SER VAL VAL ARG ARG GLU LEU PHE ARG LEU VAL ALA
SEQRES 14 D 519 ARG LEU LYS GLN ILE GLY ALA THR THR VAL MET THR THR
SEQRES 15 D 519 GLU ARG ILE GLU GLU TYR GLY PRO ILE ALA ARG TYR GLY
SEQRES 16 D 519 VAL GLU GLU PHE VAL SER ASP ASN VAL VAL ILE LEU ARG
SEQRES 17 D 519 ASN VAL LEU GLU GLY GLU ARG ARG ARG ARG THR LEU GLU
SEQRES 18 D 519 ILE LEU LYS LEU ARG GLY THR SER HIS MET LYS GLY GLU
SEQRES 19 D 519 TYR PRO PHE THR ILE THR ASP HIS GLY ILE ASN ILE PHE
SEQRES 20 D 519 PRO LEU GLY ALA MET ARG LEU THR GLN ARG SER SER ASN
SEQRES 21 D 519 VAL ARG VAL SER SER GLY VAL VAL ARG LEU ASP GLU MET
SEQRES 22 D 519 CYS GLY GLY GLY PHE PHE LYS ASP SER ILE ILE LEU ALA
SEQRES 23 D 519 THR GLY ALA THR GLY THR GLY LYS THR LEU LEU VAL SER
SEQRES 24 D 519 ARG PHE VAL GLU ASN ALA CYS ALA ASN LYS GLU ARG ALA
SEQRES 25 D 519 ILE LEU PHE ALA TYR GLU GLU SER ARG ALA GLN LEU LEU
SEQRES 26 D 519 ARG ASN ALA TYR SER TRP GLY MET ASP PHE GLU GLU MET
SEQRES 27 D 519 GLU ARG GLN ASN LEU LEU LYS ILE VAL CYS ALA TYR PRO
SEQRES 28 D 519 GLU SER ALA GLY LEU GLU ASP HIS LEU GLN ILE ILE LYS
SEQRES 29 D 519 SER GLU ILE ASN ASP PHE LYS PRO ALA ARG ILE ALA ILE
SEQRES 30 D 519 ASP SER LEU SER ALA LEU ALA ARG GLY VAL SER ASN ASN
SEQRES 31 D 519 ALA PHE ARG GLN PHE VAL ILE GLY VAL THR GLY TYR ALA
SEQRES 32 D 519 LYS GLN GLU GLU ILE THR GLY LEU PHE THR ASN THR SER
SEQRES 33 D 519 ASP GLN PHE MET GLY ALA HIS SER ILE THR ASP SER HIS
SEQRES 34 D 519 ILE SEP ALA ILE THR ASP THR ILE ILE LEU LEU GLN TYR
SEQRES 35 D 519 VAL GLU ILE ARG GLY GLU MET SER ARG ALA ILE ASN VAL
SEQRES 36 D 519 PHE LYS MET ARG GLY SER TRP HIS ASP LYS ALA ILE ARG
SEQRES 37 D 519 GLU PHE MET ILE SER ASP LYS GLY PRO ASP ILE LYS ASP
SEQRES 38 D 519 SER PHE ARG ASN PHE GLU ARG ILE ILE SER GLY SER PRO
SEQRES 39 D 519 THR ARG ILE THR VAL ASP GLU LYS SER GLU LEU SER ARG
SEQRES 40 D 519 ILE VAL ARG GLY VAL GLN GLU LYS GLY PRO GLU SER
SEQRES 1 E 519 MET THR SER ALA GLU MET THR SER PRO ASN ASN ASN SER
SEQRES 2 E 519 GLU HIS GLN ALA ILE ALA LYS MET ARG THR MET ILE GLU
SEQRES 3 E 519 GLY PHE ASP ASP ILE SER HIS GLY GLY LEU PRO ILE GLY
SEQRES 4 E 519 ARG SER THR LEU VAL SER GLY THR SER GLY THR GLY LYS
SEQRES 5 E 519 THR LEU PHE SER ILE GLN PHE LEU TYR ASN GLY ILE ILE
SEQRES 6 E 519 GLU PHE ASP GLU PRO GLY VAL PHE VAL THR PHE GLU GLU
SEQRES 7 E 519 THR PRO GLN ASP ILE ILE LYS ASN ALA ARG SER PHE GLY
SEQRES 8 E 519 TRP ASP LEU ALA LYS LEU VAL ASP GLU GLY LYS LEU PHE
SEQRES 9 E 519 ILE LEU ASP ALA SER PRO ASP PRO GLU GLY GLN GLU VAL
SEQRES 10 E 519 VAL GLY GLY PHE ASP LEU SER ALA LEU ILE GLU ARG ILE
SEQRES 11 E 519 ASN TYR ALA ILE GLN LYS TYR ARG ALA ARG ARG VAL SER
SEQRES 12 E 519 ILE ASP SER VAL THR SER VAL PHE GLN GLN TYR ASP ALA
SEQRES 13 E 519 SER SER VAL VAL ARG ARG GLU LEU PHE ARG LEU VAL ALA
SEQRES 14 E 519 ARG LEU LYS GLN ILE GLY ALA THR THR VAL MET THR THR
SEQRES 15 E 519 GLU ARG ILE GLU GLU TYR GLY PRO ILE ALA ARG TYR GLY
SEQRES 16 E 519 VAL GLU GLU PHE VAL SER ASP ASN VAL VAL ILE LEU ARG
SEQRES 17 E 519 ASN VAL LEU GLU GLY GLU ARG ARG ARG ARG THR LEU GLU
SEQRES 18 E 519 ILE LEU LYS LEU ARG GLY THR SER HIS MET LYS GLY GLU
SEQRES 19 E 519 TYR PRO PHE THR ILE THR ASP HIS GLY ILE ASN ILE PHE
SEQRES 20 E 519 PRO LEU GLY ALA MET ARG LEU THR GLN ARG SER SER ASN
SEQRES 21 E 519 VAL ARG VAL SER SER GLY VAL VAL ARG LEU ASP GLU MET
SEQRES 22 E 519 CYS GLY GLY GLY PHE PHE LYS ASP SER ILE ILE LEU ALA
SEQRES 23 E 519 THR GLY ALA THR GLY THR GLY LYS THR LEU LEU VAL SER
SEQRES 24 E 519 ARG PHE VAL GLU ASN ALA CYS ALA ASN LYS GLU ARG ALA
SEQRES 25 E 519 ILE LEU PHE ALA TYR GLU GLU SER ARG ALA GLN LEU LEU
SEQRES 26 E 519 ARG ASN ALA TYR SER TRP GLY MET ASP PHE GLU GLU MET
SEQRES 27 E 519 GLU ARG GLN ASN LEU LEU LYS ILE VAL CYS ALA TYR PRO
SEQRES 28 E 519 GLU SER ALA GLY LEU GLU ASP HIS LEU GLN ILE ILE LYS
SEQRES 29 E 519 SER GLU ILE ASN ASP PHE LYS PRO ALA ARG ILE ALA ILE
SEQRES 30 E 519 ASP SER LEU SER ALA LEU ALA ARG GLY VAL SER ASN ASN
SEQRES 31 E 519 ALA PHE ARG GLN PHE VAL ILE GLY VAL THR GLY TYR ALA
SEQRES 32 E 519 LYS GLN GLU GLU ILE THR GLY LEU PHE THR ASN THR SER
SEQRES 33 E 519 ASP GLN PHE MET GLY ALA HIS SER ILE THR ASP SER HIS
SEQRES 34 E 519 ILE SEP ALA ILE THR ASP THR ILE ILE LEU LEU GLN TYR
SEQRES 35 E 519 VAL GLU ILE ARG GLY GLU MET SER ARG ALA ILE ASN VAL
SEQRES 36 E 519 PHE LYS MET ARG GLY SER TRP HIS ASP LYS ALA ILE ARG
SEQRES 37 E 519 GLU PHE MET ILE SER ASP LYS GLY PRO ASP ILE LYS ASP
SEQRES 38 E 519 SER PHE ARG ASN PHE GLU ARG ILE ILE SER GLY SER PRO
SEQRES 39 E 519 THR ARG ILE THR VAL ASP GLU LYS SER GLU LEU SER ARG
SEQRES 40 E 519 ILE VAL ARG GLY VAL GLN GLU LYS GLY PRO GLU SER
SEQRES 1 F 519 MET THR SER ALA GLU MET THR SER PRO ASN ASN ASN SER
SEQRES 2 F 519 GLU HIS GLN ALA ILE ALA LYS MET ARG THR MET ILE GLU
SEQRES 3 F 519 GLY PHE ASP ASP ILE SER HIS GLY GLY LEU PRO ILE GLY
SEQRES 4 F 519 ARG SER THR LEU VAL SER GLY THR SER GLY THR GLY LYS
SEQRES 5 F 519 THR LEU PHE SER ILE GLN PHE LEU TYR ASN GLY ILE ILE
SEQRES 6 F 519 GLU PHE ASP GLU PRO GLY VAL PHE VAL THR PHE GLU GLU
SEQRES 7 F 519 THR PRO GLN ASP ILE ILE LYS ASN ALA ARG SER PHE GLY
SEQRES 8 F 519 TRP ASP LEU ALA LYS LEU VAL ASP GLU GLY LYS LEU PHE
SEQRES 9 F 519 ILE LEU ASP ALA SER PRO ASP PRO GLU GLY GLN GLU VAL
SEQRES 10 F 519 VAL GLY GLY PHE ASP LEU SER ALA LEU ILE GLU ARG ILE
SEQRES 11 F 519 ASN TYR ALA ILE GLN LYS TYR ARG ALA ARG ARG VAL SER
SEQRES 12 F 519 ILE ASP SER VAL THR SER VAL PHE GLN GLN TYR ASP ALA
SEQRES 13 F 519 SER SER VAL VAL ARG ARG GLU LEU PHE ARG LEU VAL ALA
SEQRES 14 F 519 ARG LEU LYS GLN ILE GLY ALA THR THR VAL MET THR THR
SEQRES 15 F 519 GLU ARG ILE GLU GLU TYR GLY PRO ILE ALA ARG TYR GLY
SEQRES 16 F 519 VAL GLU GLU PHE VAL SER ASP ASN VAL VAL ILE LEU ARG
SEQRES 17 F 519 ASN VAL LEU GLU GLY GLU ARG ARG ARG ARG THR LEU GLU
SEQRES 18 F 519 ILE LEU LYS LEU ARG GLY THR SER HIS MET LYS GLY GLU
SEQRES 19 F 519 TYR PRO PHE THR ILE THR ASP HIS GLY ILE ASN ILE PHE
SEQRES 20 F 519 PRO LEU GLY ALA MET ARG LEU THR GLN ARG SER SER ASN
SEQRES 21 F 519 VAL ARG VAL SER SER GLY VAL VAL ARG LEU ASP GLU MET
SEQRES 22 F 519 CYS GLY GLY GLY PHE PHE LYS ASP SER ILE ILE LEU ALA
SEQRES 23 F 519 THR GLY ALA THR GLY THR GLY LYS THR LEU LEU VAL SER
SEQRES 24 F 519 ARG PHE VAL GLU ASN ALA CYS ALA ASN LYS GLU ARG ALA
SEQRES 25 F 519 ILE LEU PHE ALA TYR GLU GLU SER ARG ALA GLN LEU LEU
SEQRES 26 F 519 ARG ASN ALA TYR SER TRP GLY MET ASP PHE GLU GLU MET
SEQRES 27 F 519 GLU ARG GLN ASN LEU LEU LYS ILE VAL CYS ALA TYR PRO
SEQRES 28 F 519 GLU SER ALA GLY LEU GLU ASP HIS LEU GLN ILE ILE LYS
SEQRES 29 F 519 SER GLU ILE ASN ASP PHE LYS PRO ALA ARG ILE ALA ILE
SEQRES 30 F 519 ASP SER LEU SER ALA LEU ALA ARG GLY VAL SER ASN ASN
SEQRES 31 F 519 ALA PHE ARG GLN PHE VAL ILE GLY VAL THR GLY TYR ALA
SEQRES 32 F 519 LYS GLN GLU GLU ILE THR GLY LEU PHE THR ASN THR SER
SEQRES 33 F 519 ASP GLN PHE MET GLY ALA HIS SER ILE THR ASP SER HIS
SEQRES 34 F 519 ILE SEP ALA ILE THR ASP THR ILE ILE LEU LEU GLN TYR
SEQRES 35 F 519 VAL GLU ILE ARG GLY GLU MET SER ARG ALA ILE ASN VAL
SEQRES 36 F 519 PHE LYS MET ARG GLY SER TRP HIS ASP LYS ALA ILE ARG
SEQRES 37 F 519 GLU PHE MET ILE SER ASP LYS GLY PRO ASP ILE LYS ASP
SEQRES 38 F 519 SER PHE ARG ASN PHE GLU ARG ILE ILE SER GLY SER PRO
SEQRES 39 F 519 THR ARG ILE THR VAL ASP GLU LYS SER GLU LEU SER ARG
SEQRES 40 F 519 ILE VAL ARG GLY VAL GLN GLU LYS GLY PRO GLU SER
MODRES 3JZM SEP A 431 SER PHOSPHOSERINE
MODRES 3JZM SEP B 431 SER PHOSPHOSERINE
MODRES 3JZM SEP C 431 SER PHOSPHOSERINE
MODRES 3JZM SEP D 431 SER PHOSPHOSERINE
MODRES 3JZM SEP E 431 SER PHOSPHOSERINE
MODRES 3JZM SEP F 431 SER PHOSPHOSERINE
HET SEP A 431 10
HET SEP B 431 10
HET SEP C 431 10
HET SEP D 431 10
HET SEP E 431 10
HET SEP F 431 10
HET ATP A 901 31
HET ATP A 903 31
HET MG A 801 1
HET MG A 802 1
HET MG A 701 1
HET MG B 527 1
HET ATP B 901 31
HET ATP B 903 31
HET MG B 801 1
HET MG B 701 1
HET ATP C 901 31
HET ATP C 903 31
HET MG C 801 1
HET MG C 520 1
HET ATP D 901 31
HET ATP D 903 31
HET MG D 802 1
HET MG D 701 1
HET MG D 702 1
HET ATP E 901 31
HET ATP E 903 31
HET MG E 801 1
HET MG E 701 1
HET MG E 702 1
HET ATP F 901 31
HET ATP F 903 31
HET MG F 701 1
HET MG F 702 1
HET MG F 802 1
HET MG F 801 1
HETNAM SEP PHOSPHOSERINE
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 SEP 6(C3 H8 N O6 P)
FORMUL 7 ATP 12(C10 H16 N5 O13 P3)
FORMUL 9 MG 18(MG 2+)
FORMUL 37 HOH *63(H2 O)
HELIX 1 1 GLY A 27 SER A 32 1 6
HELIX 2 2 GLY A 51 ASP A 68 1 18
HELIX 3 3 THR A 79 ARG A 88 1 10
HELIX 4 4 SER A 89 GLY A 91 5 3
HELIX 5 5 ASP A 93 GLU A 100 1 8
HELIX 6 6 GLY A 120 ARG A 138 1 19
HELIX 7 7 SER A 146 PHE A 151 1 6
HELIX 8 8 ALA A 156 GLY A 175 1 20
HELIX 9 9 VAL A 196 SER A 201 1 6
HELIX 10 10 VAL A 267 CYS A 274 1 8
HELIX 11 11 GLY A 293 ALA A 307 1 15
HELIX 12 12 SER A 320 SER A 330 1 11
HELIX 13 13 ASP A 334 GLN A 341 1 8
HELIX 14 14 TYR A 350 ALA A 354 5 5
HELIX 15 15 GLY A 355 ASP A 369 1 15
HELIX 16 16 SER A 379 ALA A 384 1 6
HELIX 17 17 SER A 388 GLU A 406 1 19
HELIX 18 18 GLY B 27 SER B 32 1 6
HELIX 19 19 GLY B 51 ASP B 68 1 18
HELIX 20 20 THR B 79 ARG B 88 1 10
HELIX 21 21 SER B 89 GLY B 91 5 3
HELIX 22 22 ASP B 93 GLU B 100 1 8
HELIX 23 23 GLY B 119 TYR B 137 1 19
HELIX 24 24 SER B 146 PHE B 151 1 6
HELIX 25 25 ALA B 156 ILE B 174 1 19
HELIX 26 26 VAL B 196 SER B 201 1 6
HELIX 27 27 VAL B 267 CYS B 274 1 8
HELIX 28 28 GLY B 293 ASN B 308 1 16
HELIX 29 29 SER B 320 SER B 330 1 11
HELIX 30 30 ASP B 334 GLN B 341 1 8
HELIX 31 31 TYR B 350 ALA B 354 5 5
HELIX 32 32 GLY B 355 ASP B 369 1 15
HELIX 33 33 SER B 379 ALA B 384 1 6
HELIX 34 34 SER B 388 GLU B 406 1 19
HELIX 35 35 ILE B 430 THR B 434 5 5
HELIX 36 36 GLY C 27 SER C 32 1 6
HELIX 37 37 GLY C 51 ASP C 68 1 18
HELIX 38 38 THR C 79 ARG C 88 1 10
HELIX 39 39 ASP C 93 GLU C 100 1 8
HELIX 40 40 ALA C 125 ARG C 138 1 14
HELIX 41 41 ALA C 156 ILE C 174 1 19
HELIX 42 42 VAL C 196 SER C 201 1 6
HELIX 43 43 VAL C 267 CYS C 274 1 8
HELIX 44 44 GLY C 293 ASN C 308 1 16
HELIX 45 45 SER C 320 SER C 330 1 11
HELIX 46 46 ASP C 334 GLN C 341 1 8
HELIX 47 47 TYR C 350 ALA C 354 5 5
HELIX 48 48 GLY C 355 ASP C 369 1 15
HELIX 49 49 SER C 381 ARG C 385 5 5
HELIX 50 50 SER C 388 GLU C 406 1 19
HELIX 51 51 ILE C 430 THR C 434 5 5
HELIX 52 52 GLY D 27 SER D 32 1 6
HELIX 53 53 GLY D 51 ASP D 68 1 18
HELIX 54 54 THR D 79 ARG D 88 1 10
HELIX 55 55 SER D 89 GLY D 91 5 3
HELIX 56 56 ASP D 93 GLU D 100 1 8
HELIX 57 57 PHE D 121 ARG D 138 1 18
HELIX 58 58 SER D 146 GLN D 152 1 7
HELIX 59 59 ALA D 156 ILE D 174 1 19
HELIX 60 60 VAL D 196 SER D 201 1 6
HELIX 61 61 VAL D 267 CYS D 274 1 8
HELIX 62 62 GLY D 293 ASN D 308 1 16
HELIX 63 63 SER D 320 SER D 330 1 11
HELIX 64 64 ASP D 334 GLN D 341 1 8
HELIX 65 65 TYR D 350 ALA D 354 5 5
HELIX 66 66 GLY D 355 ASP D 369 1 15
HELIX 67 67 SER D 379 ALA D 384 1 6
HELIX 68 68 SER D 388 GLU D 406 1 19
HELIX 69 69 ILE D 430 THR D 434 5 5
HELIX 70 70 GLY E 27 SER E 32 1 6
HELIX 71 71 GLY E 51 ASP E 68 1 18
HELIX 72 72 THR E 79 ARG E 88 1 10
HELIX 73 73 SER E 89 GLY E 91 5 3
HELIX 74 74 ASP E 93 GLU E 100 1 8
HELIX 75 75 PHE E 121 ARG E 138 1 18
HELIX 76 76 SER E 146 VAL E 150 5 5
HELIX 77 77 ALA E 156 GLY E 175 1 20
HELIX 78 78 VAL E 196 SER E 201 1 6
HELIX 79 79 VAL E 267 CYS E 274 1 8
HELIX 80 80 GLY E 293 ASN E 308 1 16
HELIX 81 81 SER E 320 SER E 330 1 11
HELIX 82 82 ASP E 334 GLN E 341 1 8
HELIX 83 83 TYR E 350 ALA E 354 5 5
HELIX 84 84 GLY E 355 LYS E 371 1 17
HELIX 85 85 SER E 379 ARG E 385 1 7
HELIX 86 86 SER E 388 GLU E 406 1 19
HELIX 87 87 ARG E 488 GLY E 492 5 5
HELIX 88 88 GLY F 27 SER F 32 1 6
HELIX 89 89 GLY F 51 ASP F 68 1 18
HELIX 90 90 THR F 79 ARG F 88 1 10
HELIX 91 91 SER F 89 GLY F 91 5 3
HELIX 92 92 ASP F 93 GLU F 100 1 8
HELIX 93 93 GLY F 120 ARG F 138 1 19
HELIX 94 94 ALA F 156 GLY F 175 1 20
HELIX 95 95 VAL F 196 SER F 201 1 6
HELIX 96 96 VAL F 267 CYS F 274 1 8
HELIX 97 97 GLY F 293 ASN F 308 1 16
HELIX 98 98 ALA F 322 TRP F 331 1 10
HELIX 99 99 ASP F 334 GLN F 341 1 8
HELIX 100 100 TYR F 350 ALA F 354 5 5
HELIX 101 101 GLY F 355 ASP F 369 1 15
HELIX 102 102 SER F 379 ALA F 384 1 6
HELIX 103 103 SER F 388 GLU F 406 1 19
HELIX 104 104 ILE F 430 THR F 434 5 5
SHEET 1 A 2 LYS A 20 MET A 21 0
SHEET 2 A 2 LEU A 36 PRO A 37 -1 O LEU A 36 N MET A 21
SHEET 1 B 9 LEU A 103 ASP A 107 0
SHEET 2 B 9 GLY A 71 THR A 75 1 N GLY A 71 O PHE A 104
SHEET 3 B 9 ARG A 141 ASP A 145 1 O ASP A 145 N VAL A 74
SHEET 4 B 9 THR A 177 GLU A 183 1 O VAL A 179 N ILE A 144
SHEET 5 B 9 SER A 41 GLY A 46 1 N VAL A 44 O MET A 180
SHEET 6 B 9 ASN A 203 VAL A 210 1 O VAL A 205 N LEU A 43
SHEET 7 B 9 ARG A 217 LEU A 225 -1 O GLU A 221 N ILE A 206
SHEET 8 B 9 GLU A 234 THR A 240 -1 O PHE A 237 N ARG A 218
SHEET 9 B 9 GLY A 243 ILE A 246 -1 O ASN A 245 N THR A 238
SHEET 1 C 2 ARG A 262 VAL A 263 0
SHEET 2 C 2 PHE A 278 PHE A 279 -1 O PHE A 278 N VAL A 263
SHEET 1 D 8 LEU A 344 ILE A 346 0
SHEET 2 D 8 ALA A 312 ALA A 316 1 N ALA A 312 O LYS A 345
SHEET 3 D 8 ARG A 374 ASP A 378 1 O ALA A 376 N PHE A 315
SHEET 4 D 8 THR A 409 THR A 415 1 O THR A 409 N ILE A 375
SHEET 5 D 8 ILE A 283 GLY A 288 1 N ILE A 284 O PHE A 412
SHEET 6 D 8 THR A 436 LEU A 440 1 O ILE A 438 N LEU A 285
SHEET 7 D 8 GLU A 448 MET A 458 -1 O ASN A 454 N LEU A 439
SHEET 8 D 8 VAL A 443 ILE A 445 -1 N VAL A 443 O SER A 450
SHEET 1 E 9 LEU A 344 ILE A 346 0
SHEET 2 E 9 ALA A 312 ALA A 316 1 N ALA A 312 O LYS A 345
SHEET 3 E 9 ARG A 374 ASP A 378 1 O ALA A 376 N PHE A 315
SHEET 4 E 9 THR A 409 THR A 415 1 O THR A 409 N ILE A 375
SHEET 5 E 9 ILE A 283 GLY A 288 1 N ILE A 284 O PHE A 412
SHEET 6 E 9 THR A 436 LEU A 440 1 O ILE A 438 N LEU A 285
SHEET 7 E 9 GLU A 448 MET A 458 -1 O ASN A 454 N LEU A 439
SHEET 8 E 9 ARG A 468 ILE A 472 -1 O ARG A 468 N ILE A 453
SHEET 9 E 9 PRO A 477 SER A 482 -1 O ASP A 481 N GLU A 469
SHEET 1 F 2 LYS B 20 MET B 21 0
SHEET 2 F 2 LEU B 36 PRO B 37 -1 O LEU B 36 N MET B 21
SHEET 1 G 9 LEU B 103 ASP B 107 0
SHEET 2 G 9 GLY B 71 THR B 75 1 N GLY B 71 O PHE B 104
SHEET 3 G 9 ARG B 141 ASP B 145 1 O SER B 143 N VAL B 74
SHEET 4 G 9 THR B 177 GLU B 183 1 O THR B 181 N ILE B 144
SHEET 5 G 9 SER B 41 GLY B 46 1 N VAL B 44 O MET B 180
SHEET 6 G 9 ASN B 203 VAL B 210 1 O ASN B 203 N LEU B 43
SHEET 7 G 9 ARG B 217 LEU B 225 -1 O THR B 219 N ARG B 208
SHEET 8 G 9 GLU B 234 THR B 240 -1 O TYR B 235 N LEU B 220
SHEET 9 G 9 GLY B 243 ILE B 246 -1 O ASN B 245 N THR B 238
SHEET 1 H 2 ARG B 262 VAL B 263 0
SHEET 2 H 2 PHE B 278 PHE B 279 -1 O PHE B 278 N VAL B 263
SHEET 1 I 7 LEU B 344 ILE B 346 0
SHEET 2 I 7 ALA B 312 ALA B 316 1 N LEU B 314 O LYS B 345
SHEET 3 I 7 ARG B 374 ASP B 378 1 O ALA B 376 N PHE B 315
SHEET 4 I 7 THR B 409 THR B 415 1 O LEU B 411 N ILE B 375
SHEET 5 I 7 ILE B 283 GLY B 288 1 N ILE B 284 O GLY B 410
SHEET 6 I 7 THR B 436 LEU B 439 1 O THR B 436 N LEU B 285
SHEET 7 I 7 VAL B 455 LYS B 457 -1 O LYS B 457 N ILE B 437
SHEET 1 J 2 VAL B 443 GLU B 444 0
SHEET 2 J 2 MET B 449 SER B 450 -1 O SER B 450 N VAL B 443
SHEET 1 K 2 ARG B 468 ILE B 472 0
SHEET 2 K 2 PRO B 477 SER B 482 -1 O ASP B 481 N GLU B 469
SHEET 1 L 2 PHE B 486 GLU B 487 0
SHEET 2 L 2 THR B 495 ARG B 496 -1 O THR B 495 N GLU B 487
SHEET 1 M 2 LYS C 20 MET C 21 0
SHEET 2 M 2 LEU C 36 PRO C 37 -1 O LEU C 36 N MET C 21
SHEET 1 N 9 LEU C 103 ASP C 107 0
SHEET 2 N 9 GLY C 71 THR C 75 1 N GLY C 71 O PHE C 104
SHEET 3 N 9 ARG C 141 ASP C 145 1 O ASP C 145 N VAL C 74
SHEET 4 N 9 THR C 177 GLU C 183 1 O VAL C 179 N VAL C 142
SHEET 5 N 9 SER C 41 GLY C 46 1 N VAL C 44 O MET C 180
SHEET 6 N 9 ASN C 203 VAL C 210 1 O ASN C 203 N LEU C 43
SHEET 7 N 9 ARG C 217 LEU C 225 -1 O THR C 219 N ARG C 208
SHEET 8 N 9 GLU C 234 THR C 240 -1 O TYR C 235 N LEU C 220
SHEET 9 N 9 GLY C 243 ILE C 246 -1 O GLY C 243 N THR C 240
SHEET 1 O 2 ARG C 262 VAL C 263 0
SHEET 2 O 2 PHE C 278 PHE C 279 -1 O PHE C 278 N VAL C 263
SHEET 1 P 9 LEU C 344 ILE C 346 0
SHEET 2 P 9 ALA C 312 ALA C 316 1 N LEU C 314 O LYS C 345
SHEET 3 P 9 ARG C 374 ASP C 378 1 O ALA C 376 N PHE C 315
SHEET 4 P 9 THR C 409 THR C 415 1 O LEU C 411 N ILE C 375
SHEET 5 P 9 ILE C 283 GLY C 288 1 N ILE C 284 O PHE C 412
SHEET 6 P 9 THR C 436 ILE C 445 1 O LEU C 440 N THR C 287
SHEET 7 P 9 GLU C 448 MET C 458 -1 O ASN C 454 N LEU C 439
SHEET 8 P 9 ARG C 468 ILE C 472 -1 O ARG C 468 N ILE C 453
SHEET 9 P 9 PRO C 477 SER C 482 -1 O ASP C 481 N GLU C 469
SHEET 1 Q 2 PHE C 486 GLU C 487 0
SHEET 2 Q 2 THR C 495 ARG C 496 -1 O THR C 495 N GLU C 487
SHEET 1 R 2 LYS D 20 MET D 21 0
SHEET 2 R 2 LEU D 36 PRO D 37 -1 O LEU D 36 N MET D 21
SHEET 1 S 9 LEU D 103 ASP D 107 0
SHEET 2 S 9 GLY D 71 THR D 75 1 N PHE D 73 O PHE D 104
SHEET 3 S 9 ARG D 141 ASP D 145 1 O ASP D 145 N VAL D 74
SHEET 4 S 9 THR D 177 GLU D 183 1 O THR D 181 N ILE D 144
SHEET 5 S 9 SER D 41 GLY D 46 1 N THR D 42 O MET D 180
SHEET 6 S 9 ASN D 203 VAL D 210 1 O ASN D 203 N LEU D 43
SHEET 7 S 9 ARG D 217 LEU D 225 -1 O THR D 219 N ARG D 208
SHEET 8 S 9 GLU D 234 THR D 240 -1 O TYR D 235 N LEU D 220
SHEET 9 S 9 GLY D 243 ILE D 246 -1 O ASN D 245 N THR D 238
SHEET 1 T 2 ARG D 262 VAL D 263 0
SHEET 2 T 2 PHE D 278 PHE D 279 -1 O PHE D 278 N VAL D 263
SHEET 1 U 9 LEU D 344 ILE D 346 0
SHEET 2 U 9 ALA D 312 ALA D 316 1 N LEU D 314 O LYS D 345
SHEET 3 U 9 ARG D 374 ASP D 378 1 O ALA D 376 N PHE D 315
SHEET 4 U 9 THR D 409 THR D 415 1 O LEU D 411 N ILE D 377
SHEET 5 U 9 ILE D 283 GLY D 288 1 N ALA D 286 O PHE D 412
SHEET 6 U 9 THR D 436 GLU D 444 1 O LEU D 440 N THR D 287
SHEET 7 U 9 MET D 449 MET D 458 -1 O ASN D 454 N LEU D 439
SHEET 8 U 9 ARG D 468 ILE D 472 -1 O ARG D 468 N ILE D 453
SHEET 9 U 9 PRO D 477 SER D 482 -1 O ASP D 478 N MET D 471
SHEET 1 V 2 LYS E 20 MET E 21 0
SHEET 2 V 2 LEU E 36 PRO E 37 -1 O LEU E 36 N MET E 21
SHEET 1 W 9 LEU E 103 ASP E 107 0
SHEET 2 W 9 GLY E 71 THR E 75 1 N PHE E 73 O LEU E 106
SHEET 3 W 9 ARG E 141 ASP E 145 1 O ARG E 141 N VAL E 72
SHEET 4 W 9 THR E 177 GLU E 183 1 O VAL E 179 N ILE E 144
SHEET 5 W 9 SER E 41 GLY E 46 1 N VAL E 44 O MET E 180
SHEET 6 W 9 ASN E 203 VAL E 210 1 O VAL E 205 N LEU E 43
SHEET 7 W 9 ARG E 217 LEU E 225 -1 O THR E 219 N ARG E 208
SHEET 8 W 9 GLU E 234 THR E 240 -1 O TYR E 235 N LEU E 220
SHEET 9 W 9 GLY E 243 ILE E 246 -1 O GLY E 243 N THR E 240
SHEET 1 X 2 ARG E 262 VAL E 263 0
SHEET 2 X 2 PHE E 278 PHE E 279 -1 O PHE E 278 N VAL E 263
SHEET 1 Y 9 LEU E 344 ILE E 346 0
SHEET 2 Y 9 ALA E 312 ALA E 316 1 N ALA E 312 O LYS E 345
SHEET 3 Y 9 ARG E 374 ASP E 378 1 O ALA E 376 N PHE E 315
SHEET 4 Y 9 THR E 409 THR E 415 1 O LEU E 411 N ILE E 375
SHEET 5 Y 9 ILE E 283 GLY E 288 1 N ILE E 284 O PHE E 412
SHEET 6 Y 9 THR E 436 GLU E 444 1 O LEU E 440 N THR E 287
SHEET 7 Y 9 MET E 449 MET E 458 -1 O ASN E 454 N LEU E 439
SHEET 8 Y 9 ARG E 468 ILE E 472 -1 O ARG E 468 N ILE E 453
SHEET 9 Y 9 PRO E 477 ILE E 479 -1 O ASP E 478 N MET E 471
SHEET 1 Z 2 LYS F 20 MET F 21 0
SHEET 2 Z 2 LEU F 36 PRO F 37 -1 O LEU F 36 N MET F 21
SHEET 1 AA 9 LEU F 103 ASP F 107 0
SHEET 2 AA 9 GLY F 71 THR F 75 1 N PHE F 73 O LEU F 106
SHEET 3 AA 9 ARG F 141 ASP F 145 1 O ASP F 145 N VAL F 74
SHEET 4 AA 9 THR F 177 GLU F 183 1 O VAL F 179 N ILE F 144
SHEET 5 AA 9 SER F 41 GLY F 46 1 N VAL F 44 O MET F 180
SHEET 6 AA 9 ASN F 203 VAL F 210 1 O VAL F 205 N LEU F 43
SHEET 7 AA 9 ARG F 217 LEU F 225 -1 O GLU F 221 N ILE F 206
SHEET 8 AA 9 TYR F 235 THR F 240 -1 O TYR F 235 N LEU F 220
SHEET 9 AA 9 GLY F 243 ILE F 246 -1 O GLY F 243 N THR F 240
SHEET 1 AB 2 ARG F 262 VAL F 263 0
SHEET 2 AB 2 PHE F 278 PHE F 279 -1 O PHE F 278 N VAL F 263
SHEET 1 AC 9 LEU F 344 ILE F 346 0
SHEET 2 AC 9 ALA F 312 ALA F 316 1 N ALA F 312 O LYS F 345
SHEET 3 AC 9 ARG F 374 ASP F 378 1 O ALA F 376 N PHE F 315
SHEET 4 AC 9 THR F 409 THR F 415 1 O LEU F 411 N ILE F 375
SHEET 5 AC 9 ILE F 283 GLY F 288 1 N ILE F 284 O PHE F 412
SHEET 6 AC 9 THR F 436 ILE F 445 1 O ILE F 438 N LEU F 285
SHEET 7 AC 9 GLU F 448 LYS F 457 -1 O ASN F 454 N LEU F 439
SHEET 8 AC 9 ILE F 467 SER F 473 -1 O ARG F 468 N ILE F 453
SHEET 9 AC 9 GLY F 476 SER F 482 -1 O GLY F 476 N SER F 473
SHEET 1 AD 2 PHE F 486 GLU F 487 0
SHEET 2 AD 2 THR F 495 ARG F 496 -1 O THR F 495 N GLU F 487
LINK C ILE A 430 N SEP A 431 1555 1555 1.32
LINK C SEP A 431 N ALA A 432 1555 1555 1.33
LINK C ILE B 430 N SEP B 431 1555 1555 1.32
LINK C SEP B 431 N ALA B 432 1555 1555 1.33
LINK C ILE C 430 N SEP C 431 1555 1555 1.31
LINK C SEP C 431 N ALA C 432 1555 1555 1.33
LINK C ILE D 430 N SEP D 431 1555 1555 1.33
LINK C SEP D 431 N ALA D 432 1555 1555 1.33
LINK C ILE E 430 N SEP E 431 1555 1555 1.32
LINK C SEP E 431 N ALA E 432 1555 1555 1.33
LINK C ILE F 430 N SEP F 431 1555 1555 1.32
LINK C SEP F 431 N ALA F 432 1555 1555 1.33
LINK OG1 THR A 53 MG MG A 701 1555 1555 2.47
LINK OE2 GLU A 78 MG MG A 701 1555 1555 2.55
LINK OG1 THR A 295 MG MG A 801 1555 1555 2.33
LINK OE1 GLU A 318 MG MG A 801 1555 1555 2.81
LINK OG1 THR A 415 MG MG A 802 1555 1555 2.90
LINK MG MG A 701 O2G ATP A 903 1555 1555 2.29
LINK MG MG A 701 O3G ATP A 903 1555 1555 1.99
LINK MG MG A 801 O2G ATP A 901 1555 1555 2.25
LINK MG MG A 801 O3B ATP A 901 1555 1555 2.77
LINK MG MG A 802 O1G ATP A 901 1555 1555 2.05
LINK MG MG A 802 O3B ATP A 901 1555 1555 2.12
LINK O1G ATP A 903 MG MG B 527 1555 1555 2.01
LINK OG1 THR B 295 MG MG B 801 1555 1555 2.30
LINK OE1 GLU B 318 MG MG B 801 1555 1555 2.75
LINK MG MG B 701 O1G ATP B 903 1555 1555 2.02
LINK MG MG B 801 O2G ATP B 901 1555 1555 2.32
LINK OE2 GLU C 78 MG MG C 520 1555 1555 2.01
LINK OG1 THR C 295 MG MG C 801 1555 1555 2.44
LINK MG MG C 520 O2G ATP C 903 1555 1555 2.03
LINK MG MG C 520 O3G ATP C 903 1555 1555 2.13
LINK MG MG C 801 O2G ATP C 901 1555 1555 2.18
LINK MG MG C 801 O3B ATP C 901 1555 1555 2.44
LINK OG1 THR D 53 MG MG D 702 1555 1555 2.69
LINK OE2 GLU D 78 MG MG D 702 1555 1555 2.07
LINK OG1 THR D 295 MG MG D 802 1555 1555 2.42
LINK MG MG D 701 O1G ATP D 903 1555 1555 2.17
LINK MG MG D 701 O3B ATP D 903 1555 1555 2.67
LINK MG MG D 702 O2G ATP D 903 1555 1555 2.03
LINK MG MG D 702 O3G ATP D 903 1555 1555 2.93
LINK MG MG D 802 O2G ATP D 901 1555 1555 2.25
LINK MG MG D 802 O3A ATP D 901 1555 1555 2.62
LINK MG MG D 802 O3B ATP D 901 1555 1555 2.45
LINK OG1 THR E 53 MG MG E 702 1555 1555 2.37
LINK OD2 ASP E 145 MG MG E 702 1555 1555 2.71
LINK OG1 THR E 295 MG MG E 801 1555 1555 2.02
LINK MG MG E 701 O1G ATP E 903 1555 1555 2.03
LINK MG MG E 701 O2B ATP E 903 1555 1555 2.80
LINK MG MG E 701 O3B ATP E 903 1555 1555 2.87
LINK MG MG E 702 O2G ATP E 903 1555 1555 2.09
LINK MG MG E 702 O3B ATP E 903 1555 1555 2.91
LINK MG MG E 801 O2G ATP E 901 1555 1555 2.00
LINK N GLY F 49 MG MG F 702 1555 1555 2.56
LINK OG1 THR F 53 MG MG F 701 1555 1555 2.04
LINK OG1 THR F 295 MG MG F 802 1555 1555 2.34
LINK OE1 GLU F 318 MG MG F 802 1555 1555 2.70
LINK OG1 THR F 415 MG MG F 801 1555 1555 2.42
LINK MG MG F 701 O2G ATP F 903 1555 1555 2.06
LINK MG MG F 701 O3B ATP F 903 1555 1555 2.49
LINK MG MG F 702 O1G ATP F 903 1555 1555 2.06
LINK MG MG F 702 O3G ATP F 903 1555 1555 2.61
LINK MG MG F 702 O3B ATP F 903 1555 1555 2.78
LINK MG MG F 801 O1G ATP F 901 1555 1555 2.04
LINK MG MG F 802 O2G ATP F 901 1555 1555 2.15
SITE 1 AC1 20 THR A 290 GLY A 291 THR A 292 GLY A 293
SITE 2 AC1 20 LYS A 294 THR A 295 LEU A 296 TRP A 331
SITE 3 AC1 20 ARG A 451 ILE A 472 MG A 801 MG A 802
SITE 4 AC1 20 LYS B 457 MET B 458 ARG B 459 GLY B 460
SITE 5 AC1 20 SER B 461 TRP B 462 HIS B 463 LYS B 465
SITE 1 AC2 20 GLY A 49 THR A 50 GLY A 51 LYS A 52
SITE 2 AC2 20 THR A 53 LEU A 54 SER A 89 PHE A 90
SITE 3 AC2 20 ARG A 218 ILE A 239 THR A 240 ASP A 241
SITE 4 AC2 20 MG A 701 LYS B 224 LEU B 225 ARG B 226
SITE 5 AC2 20 THR B 228 SER B 229 HIS B 230 MG B 527
SITE 1 AC3 5 THR A 295 GLU A 318 ASP A 378 MG A 802
SITE 2 AC3 5 ATP A 901
SITE 1 AC4 5 THR A 290 LYS A 294 THR A 415 MG A 801
SITE 2 AC4 5 ATP A 901
SITE 1 AC5 4 THR A 53 GLU A 78 ATP A 903 ARG B 226
SITE 1 AC6 3 ATP A 903 PHE B 199 LYS B 224
SITE 1 AC7 19 THR B 290 GLY B 291 THR B 292 GLY B 293
SITE 2 AC7 19 LYS B 294 THR B 295 LEU B 296 SER B 330
SITE 3 AC7 19 TRP B 331 ARG B 451 ILE B 472 MG B 801
SITE 4 AC7 19 LYS C 457 MET C 458 ARG C 459 SER C 461
SITE 5 AC7 19 TRP C 462 HIS C 463 LYS C 465
SITE 1 AC8 19 GLY B 49 THR B 50 GLY B 51 LYS B 52
SITE 2 AC8 19 THR B 53 LEU B 54 SER B 89 PHE B 90
SITE 3 AC8 19 ASP B 145 ARG B 218 ILE B 239 ASP B 241
SITE 4 AC8 19 MG B 701 LYS C 224 LEU C 225 ARG C 226
SITE 5 AC8 19 THR C 228 SER C 229 HIS C 230
SITE 1 AC9 4 THR B 295 GLU B 318 GLU B 319 ATP B 901
SITE 1 BC1 4 LYS B 52 ATP B 903 PHE C 199 LYS C 224
SITE 1 BC2 19 THR C 290 GLY C 291 THR C 292 GLY C 293
SITE 2 BC2 19 LYS C 294 THR C 295 LEU C 296 SER C 330
SITE 3 BC2 19 TRP C 331 ARG C 451 ILE C 472 MG C 801
SITE 4 BC2 19 LYS D 457 MET D 458 ARG D 459 SER D 461
SITE 5 BC2 19 TRP D 462 HIS D 463 HOH D 525
SITE 1 BC3 17 GLY C 49 THR C 50 GLY C 51 LYS C 52
SITE 2 BC3 17 THR C 53 LEU C 54 SER C 89 PHE C 90
SITE 3 BC3 17 ARG C 218 ILE C 239 ASP C 241 MG C 520
SITE 4 BC3 17 LYS D 224 ARG D 226 THR D 228 SER D 229
SITE 5 BC3 17 HIS D 230
SITE 1 BC4 3 THR C 295 GLU C 318 ATP C 901
SITE 1 BC5 4 THR C 53 GLU C 78 ATP C 903 ARG D 226
SITE 1 BC6 19 THR D 290 GLY D 291 THR D 292 GLY D 293
SITE 2 BC6 19 LYS D 294 THR D 295 LEU D 296 SER D 330
SITE 3 BC6 19 TRP D 331 ARG D 451 ILE D 472 MG D 802
SITE 4 BC6 19 LYS E 457 MET E 458 ARG E 459 SER E 461
SITE 5 BC6 19 TRP E 462 HIS E 463 LYS E 465
SITE 1 BC7 21 GLY D 49 THR D 50 GLY D 51 LYS D 52
SITE 2 BC7 21 THR D 53 LEU D 54 GLU D 78 SER D 89
SITE 3 BC7 21 PHE D 90 ARG D 218 ILE D 239 THR D 240
SITE 4 BC7 21 ASP D 241 MG D 701 MG D 702 LYS E 224
SITE 5 BC7 21 LEU E 225 ARG E 226 THR E 228 SER E 229
SITE 6 BC7 21 HIS E 230
SITE 1 BC8 3 THR D 295 GLU D 319 ATP D 901
SITE 1 BC9 2 LYS D 52 ATP D 903
SITE 1 CC1 4 THR D 53 GLU D 78 ASP D 145 ATP D 903
SITE 1 CC2 19 THR E 290 GLY E 291 THR E 292 GLY E 293
SITE 2 CC2 19 LYS E 294 THR E 295 LEU E 296 SER E 330
SITE 3 CC2 19 TRP E 331 ARG E 451 ILE E 472 MG E 801
SITE 4 CC2 19 LYS F 457 MET F 458 ARG F 459 SER F 461
SITE 5 CC2 19 TRP F 462 HIS F 463 LYS F 465
SITE 1 CC3 21 GLY E 49 THR E 50 GLY E 51 LYS E 52
SITE 2 CC3 21 THR E 53 LEU E 54 GLU E 78 SER E 89
SITE 3 CC3 21 PHE E 90 ILE E 239 ASP E 241 MG E 701
SITE 4 CC3 21 MG E 702 LEU F 223 LYS F 224 LEU F 225
SITE 5 CC3 21 ARG F 226 THR F 228 SER F 229 HIS F 230
SITE 6 CC3 21 LYS F 232
SITE 1 CC4 4 THR E 295 GLU E 318 GLU E 319 ATP E 901
SITE 1 CC5 4 GLY E 49 LYS E 52 ATP E 903 LYS F 224
SITE 1 CC6 5 LYS E 52 THR E 53 ASP E 145 THR E 181
SITE 2 CC6 5 ATP E 903
SITE 1 CC7 19 LYS A 457 MET A 458 ARG A 459 SER A 461
SITE 2 CC7 19 TRP A 462 HIS A 463 LYS A 465 THR F 290
SITE 3 CC7 19 GLY F 291 THR F 292 GLY F 293 LYS F 294
SITE 4 CC7 19 THR F 295 LEU F 296 TRP F 331 ARG F 451
SITE 5 CC7 19 ILE F 472 MG F 801 MG F 802
SITE 1 CC8 19 LYS A 224 ARG A 226 THR A 228 HIS A 230
SITE 2 CC8 19 LYS A 232 GLY F 49 THR F 50 GLY F 51
SITE 3 CC8 19 LYS F 52 THR F 53 LEU F 54 GLU F 78
SITE 4 CC8 19 SER F 89 PHE F 90 ILE F 239 ASP F 241
SITE 5 CC8 19 HOH F 531 MG F 701 MG F 702
SITE 1 CC9 3 THR F 53 ASP F 145 ATP F 903
SITE 1 DC1 4 LYS A 224 SER F 48 GLY F 49 ATP F 903
SITE 1 DC2 3 THR F 295 GLU F 318 ATP F 901
SITE 1 DC3 6 ALA A 432 THR F 290 LYS F 294 GLU F 318
SITE 2 DC3 6 THR F 415 ATP F 901
CRYST1 132.370 135.110 204.500 90.00 90.00 90.00 P 21 21 21 24
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 0.007555 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007401 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004890 0.00000
(ATOM LINES ARE NOT SHOWN.)
END