HEADER CONTRACTILE PROTEIN 30-JAN-02 1KWO
TITLE SCALLOP MYOSIN S1-ATPGAMMAS-P-PDM IN THE ACTIN-DETACHED CONFORMATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYOSIN HEAVY CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SUBFRAGMENT 1(S1);
COMPND 5 OTHER_DETAILS: PAPAIN DIGESTED;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: MYOSIN REGULATORY LIGHT CHAIN;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: R-LC;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: MYOSIN ESSENTIAL LIGHT CHAIN;
COMPND 12 CHAIN: C;
COMPND 13 SYNONYM: E-LC
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARGOPECTEN IRRADIANS;
SOURCE 3 ORGANISM_TAXID: 31199;
SOURCE 4 TISSUE: MUSCLE;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: ARGOPECTEN IRRADIANS;
SOURCE 7 ORGANISM_TAXID: 31199;
SOURCE 8 TISSUE: MUSCLE;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: ARGOPECTEN IRRADIANS;
SOURCE 11 ORGANISM_TAXID: 31199;
SOURCE 12 TISSUE: MUSCLE
KEYWDS ACTIN-DETACHED, MYOSIN, MECHANICS OF MOTOR, CROSS LINKER, CONTRACTILE
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.M.HIMMEL,S.GOURINATH,L.RESHETNIKOVA,Y.SHEN,G.SZENT-GYORGYI,C.COHEN
REVDAT 3 16-AUG-23 1KWO 1 REMARK SHEET LINK
REVDAT 2 24-FEB-09 1KWO 1 VERSN
REVDAT 1 20-NOV-02 1KWO 0
JRNL AUTH D.M.HIMMEL,S.GOURINATH,L.RESHETNIKOVA,Y.SHEN,
JRNL AUTH 2 A.G.SZENT-GYORGYI,C.COHEN
JRNL TITL CRYSTALLOGRAPHIC FINDINGS ON THE INTERNALLY UNCOUPLED AND
JRNL TITL 2 NEAR-RIGOR STATES OF MYOSIN: FURTHER INSIGHTS INTO THE
JRNL TITL 3 MECHANICS OF THE MOTOR
JRNL REF PROC.NATL.ACAD.SCI.USA V. 99 12645 2002
JRNL REFN ISSN 0027-8424
JRNL PMID 12297624
JRNL DOI 10.1073/PNAS.202476799
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.HOUDUSSE,V.N.KALABOKIS,D.HIMMEL,A.G.SZENT-GYORGYI,C.COHEN
REMARK 1 TITL ATOMIC STRUCTURE OF SCALLOP MYOSIN SUBFRAGMENT S1 COMPLEXED
REMARK 1 TITL 2 WITH MGADP: A NOVEL CONFORMATION OF THE MYOSIN HEAD
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 97 459 1999
REMARK 1 REFN ISSN 0092-8674
REMARK 1 DOI 10.1016/S0092-8674(00)80756-4
REMARK 2
REMARK 2 RESOLUTION. 3.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 294029.200
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 78.8
REMARK 3 NUMBER OF REFLECTIONS : 13050
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.238
REMARK 3 FREE R VALUE : 0.328
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 631
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.013
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 12
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 9.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 128
REMARK 3 BIN R VALUE (WORKING SET) : 0.2560
REMARK 3 BIN FREE R VALUE : 0.2760
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 3
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.159
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8047
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 55
REMARK 3 SOLVENT ATOMS : 6
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.45000
REMARK 3 B22 (A**2) : 21.85000
REMARK 3 B33 (A**2) : -19.40000
REMARK 3 B12 (A**2) : 16.60000
REMARK 3 B13 (A**2) : 12.40000
REMARK 3 B23 (A**2) : 11.16000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.52
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : 40.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.69
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 4.410
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 9.560 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 14.540; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 10.830; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 15.980; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.20
REMARK 3 BSOL : 36.20
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER.PARAM
REMARK 3 PARAMETER FILE 4 : CNS_PP47
REMARK 3 PARAMETER FILE 5 : CNS_PP47
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : CNS_PP47
REMARK 3 TOPOLOGY FILE 5 : CNS_PP47
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KWO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JAN-02.
REMARK 100 THE DEPOSITION ID IS D_1000015414.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-OCT-99
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.087
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14451
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.800
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.6
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 45.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.27400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1B7T
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 20000, MAGNESIUM CHLORIDE,
REMARK 280 ETHYLENE GLYCOL, TRIS HCL, ATPGAMMAS, PH 8.5, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 300 REMARK: MYOSIN-S1 CONSISTS OF THREE PEPTIDE CHAINS (HEAVY CHAIN,
REMARK 300 REGULATORY LIGHT CHAIN, ESSENTIAL LIGHT CHAIN), WHICH CAN ALSO BE
REMARK 300 DESCRIBED AS A HETEROTRIMER
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 52960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 ASN A 2
REMARK 465 ILE A 3
REMARK 465 ASP A 4
REMARK 465 GLN A 24
REMARK 465 THR A 25
REMARK 465 ALA A 26
REMARK 465 LYS A 201
REMARK 465 LYS A 202
REMARK 465 LYS A 203
REMARK 465 ASP A 204
REMARK 465 GLU A 205
REMARK 465 GLU A 206
REMARK 465 ALA A 207
REMARK 465 SER A 208
REMARK 465 ASP A 209
REMARK 465 THR A 407
REMARK 465 GLU A 408
REMARK 465 MET A 409
REMARK 465 THR A 563
REMARK 465 LYS A 564
REMARK 465 PRO A 565
REMARK 465 GLY A 566
REMARK 465 LYS A 567
REMARK 465 PRO A 568
REMARK 465 PRO A 625
REMARK 465 GLU A 626
REMARK 465 GLU A 627
REMARK 465 PRO A 628
REMARK 465 ALA A 629
REMARK 465 GLY A 630
REMARK 465 GLY A 631
REMARK 465 GLY A 632
REMARK 465 LYS A 633
REMARK 465 LYS A 634
REMARK 465 LYS A 635
REMARK 465 LYS A 636
REMARK 465 GLY A 637
REMARK 465 LYS A 638
REMARK 465 SER A 639
REMARK 465 SER A 640
REMARK 465 ALA A 641
REMARK 465 GLU A 698
REMARK 465 GLY A 699
REMARK 465 ILE A 700
REMARK 465 ARG A 701
REMARK 465 ILE A 702
REMARK 465 CYS A 703
REMARK 465 ALA A 727
REMARK 465 ILE A 728
REMARK 465 PRO A 729
REMARK 465 GLN A 730
REMARK 465 GLY A 731
REMARK 465 PHE A 732
REMARK 465 VAL A 733
REMARK 465 ALA B 1
REMARK 465 ASP B 2
REMARK 465 LYS B 3
REMARK 465 ALA B 4
REMARK 465 ALA B 5
REMARK 465 SER B 6
REMARK 465 GLY B 7
REMARK 465 VAL B 8
REMARK 465 LEU B 9
REMARK 465 THR B 10
REMARK 465 LYS B 11
REMARK 465 LEU B 12
REMARK 465 GLU B 155
REMARK 465 ALA B 156
REMARK 465 PRO C 1
REMARK 465 ASP C 155
REMARK 465 LYS C 156
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LEU A 13 CG CD1 CD2
REMARK 470 VAL A 15 CG1 CG2
REMARK 470 ASP A 16 CG OD1 OD2
REMARK 470 ARG A 17 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 18 CG CD CE NZ
REMARK 470 LYS A 19 CG CD CE NZ
REMARK 470 LEU A 20 CG CD1 CD2
REMARK 470 MET A 21 CG SD CE
REMARK 470 LYS A 22 CG CD CE NZ
REMARK 470 GLU A 23 CG CD OE1 OE2
REMARK 470 GLU A 39 CG CD OE1 OE2
REMARK 470 LYS A 40 CG CD CE NZ
REMARK 470 LYS A 84 CG CD CE NZ
REMARK 470 LEU A 118 CG CD1 CD2
REMARK 470 ARG A 128 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 144 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 145 CG CD CE NZ
REMARK 470 ILE A 148 CG1 CG2 CD1
REMARK 470 SER A 154 OG
REMARK 470 ASN A 162 CG OD1 ND2
REMARK 470 LYS A 210 CG CD CE NZ
REMARK 470 GLU A 212 CG CD OE1 OE2
REMARK 470 GLU A 216 CG CD OE1 OE2
REMARK 470 LYS A 233 CG CD CE NZ
REMARK 470 ILE A 284 CG1 CG2 CD1
REMARK 470 GLU A 295 CG CD OE1 OE2
REMARK 470 MET A 300 CG SD CE
REMARK 470 VAL A 319 CG1 CG2
REMARK 470 LEU A 330 CG CD1 CD2
REMARK 470 LYS A 364 CG CD CE NZ
REMARK 470 GLN A 365 CG CD OE1 NE2
REMARK 470 ARG A 366 CG CD NE CZ NH1 NH2
REMARK 470 PRO A 367 CG CD
REMARK 470 ARG A 368 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 369 CG CD OE1 OE2
REMARK 470 GLU A 370 CG CD OE1 OE2
REMARK 470 GLN A 371 CG CD OE1 NE2
REMARK 470 GLU A 373 CG CD OE1 OE2
REMARK 470 LEU A 386 CG CD1 CD2
REMARK 470 ASP A 393 CG OD1 OD2
REMARK 470 LEU A 395 CG CD1 CD2
REMARK 470 LYS A 396 CG CD CE NZ
REMARK 470 LYS A 402 CG CD CE NZ
REMARK 470 LYS A 404 CG CD CE NZ
REMARK 470 VAL A 405 CG1 CG2
REMARK 470 VAL A 410 CG1 CG2
REMARK 470 LYS A 412 CG CD CE NZ
REMARK 470 GLN A 414 CG CD OE1 NE2
REMARK 470 GLN A 418 CG CD OE1 NE2
REMARK 470 LYS A 444 CG CD CE NZ
REMARK 470 LYS A 451 CG CD CE NZ
REMARK 470 TYR A 454 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 465 CG CD OE1 OE2
REMARK 470 ASN A 489 CG OD1 ND2
REMARK 470 PHE A 493 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 498 CG CD OE1 OE2
REMARK 470 GLU A 503 CG CD OE1 OE2
REMARK 470 ASP A 511 CG OD1 OD2
REMARK 470 PHE A 512 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET A 514 CG SD CE
REMARK 470 ILE A 523 CG1 CG2 CD1
REMARK 470 SER A 531 OG
REMARK 470 LEU A 533 CG CD1 CD2
REMARK 470 GLU A 534 CG CD OE1 OE2
REMARK 470 GLU A 536 CG CD OE1 OE2
REMARK 470 LYS A 541 CG CD CE NZ
REMARK 470 LYS A 545 CG CD CE NZ
REMARK 470 GLN A 548 CG CD OE1 NE2
REMARK 470 LYS A 550 CG CD CE NZ
REMARK 470 TYR A 552 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 MET A 556 CG SD CE
REMARK 470 PHE A 562 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR A 569 OG1 CG2
REMARK 470 ARG A 570 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 572 CG OD1 ND2
REMARK 470 GLN A 573 CG CD OE1 NE2
REMARK 470 HIS A 581 CG ND1 CD2 CE1 NE2
REMARK 470 ASP A 600 CG OD1 OD2
REMARK 470 ASN A 603 CG OD1 ND2
REMARK 470 ASN A 605 CG OD1 ND2
REMARK 470 LEU A 610 CG CD1 CD2
REMARK 470 LYS A 614 CG CD CE NZ
REMARK 470 PHE A 642 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN A 643 CG CD OE1 NE2
REMARK 470 GLU A 651 CG CD OE1 OE2
REMARK 470 LYS A 658 CG CD CE NZ
REMARK 470 ILE A 672 CG1 CG2 CD1
REMARK 470 LEU A 676 CG CD1 CD2
REMARK 470 LYS A 677 CG CD CE NZ
REMARK 470 HIS A 689 CG ND1 CD2 CE1 NE2
REMARK 470 GLN A 692 CG CD OE1 NE2
REMARK 470 GLU A 715 CG CD OE1 OE2
REMARK 470 LYS A 717 CG CD CE NZ
REMARK 470 ASP A 734 CG OD1 OD2
REMARK 470 LYS A 741 CG CD CE NZ
REMARK 470 LEU A 743 CG CD1 CD2
REMARK 470 GLU A 752 CG CD OE1 OE2
REMARK 470 LEU A 755 CG CD1 CD2
REMARK 470 LYS A 759 CG CD CE NZ
REMARK 470 LYS A 763 CG CD CE NZ
REMARK 470 GLU A 776 CG CD OE1 OE2
REMARK 470 LYS A 796 CG CD CE NZ
REMARK 470 LYS A 800 CG CD CE NZ
REMARK 470 ARG A 805 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 813 CG CD NE CZ NH1 NH2
REMARK 470 TYR A 830 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 832 CG CD CE NZ
REMARK 470 LYS A 834 CG CD CE NZ
REMARK 470 GLN B 16 CG CD OE1 NE2
REMARK 470 ILE B 17 CG1 CG2 CD1
REMARK 470 GLN B 18 CG CD OE1 NE2
REMARK 470 GLU B 19 CG CD OE1 OE2
REMARK 470 LYS B 21 CG CD CE NZ
REMARK 470 GLU B 22 CG CD OE1 OE2
REMARK 470 MET B 26 CG SD CE
REMARK 470 VAL B 29 CG1 CG2
REMARK 470 ARG B 31 CG CD NE CZ NH1 NH2
REMARK 470 VAL B 35 CG1 CG2
REMARK 470 LYS B 41 CG CD CE NZ
REMARK 470 GLU B 45 CG CD OE1 OE2
REMARK 470 GLN B 46 CG CD OE1 NE2
REMARK 470 LEU B 67 CG CD1 CD2
REMARK 470 PHE B 76 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 102 CG CD CE NZ
REMARK 470 LYS B 103 CG CD CE NZ
REMARK 470 GLU B 107 CG CD OE1 OE2
REMARK 470 LYS B 110 CG CD CE NZ
REMARK 470 ASN B 119 CG OD1 ND2
REMARK 470 LYS B 122 CG CD CE NZ
REMARK 470 MET B 127 CG SD CE
REMARK 470 GLU B 131 CG CD OE1 OE2
REMARK 470 LYS B 138 CG CD CE NZ
REMARK 470 LYS B 143 CG CD CE NZ
REMARK 470 GLU B 154 CG CD OE1 OE2
REMARK 470 ASP C 13 CG OD1 OD2
REMARK 470 PHE C 15 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG C 38 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 45 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 47 CG CD OE1 OE2
REMARK 470 LYS C 57 CG CD CE NZ
REMARK 470 LYS C 61 CG CD CE NZ
REMARK 470 PHE C 65 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU C 67 CG CD OE1 OE2
REMARK 470 PHE C 68 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU C 75 CG CD1 CD2
REMARK 470 ASP C 77 CG OD1 OD2
REMARK 470 GLN C 80 CG CD OE1 NE2
REMARK 470 ILE C 101 CG1 CG2 CD1
REMARK 470 LYS C 127 CG CD CE NZ
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 216 CB
REMARK 480 ILE B 43 CG1 CG2 CD1
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 SER B 44 N GLY B 48 2.02
REMARK 500 OD1 ASP B 32 O PHE B 34 2.14
REMARK 500 NE2 GLN A 812 OD1 ASP B 118 2.18
REMARK 500 OG SER B 36 OD2 ASP B 39 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LYS A 22 N - CA - C ANGL. DEV. = 20.3 DEGREES
REMARK 500 GLU A 216 N - CA - C ANGL. DEV. = -20.3 DEGREES
REMARK 500 PRO A 304 C - N - CA ANGL. DEV. = 14.9 DEGREES
REMARK 500 PRO A 304 C - N - CD ANGL. DEV. = -15.5 DEGREES
REMARK 500 GLY A 307 N - CA - C ANGL. DEV. = -16.4 DEGREES
REMARK 500 ASP A 320 N - CA - C ANGL. DEV. = 19.2 DEGREES
REMARK 500 PRO A 367 N - CA - CB ANGL. DEV. = 7.9 DEGREES
REMARK 500 GLU A 369 N - CA - C ANGL. DEV. = -16.3 DEGREES
REMARK 500 PHE A 539 CA - CB - CG ANGL. DEV. = 18.7 DEGREES
REMARK 500 PHE A 539 CB - CG - CD1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 PRO A 575 C - N - CA ANGL. DEV. = 12.9 DEGREES
REMARK 500 THR A 644 N - CA - C ANGL. DEV. = 23.4 DEGREES
REMARK 500 SER A 646 N - CA - C ANGL. DEV. = -24.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 6 -135.17 -105.80
REMARK 500 ASP A 7 68.91 -166.06
REMARK 500 PRO A 8 -87.98 -56.07
REMARK 500 ASP A 9 60.30 -151.74
REMARK 500 GLN A 11 -5.21 -45.75
REMARK 500 TYR A 12 -31.96 -136.09
REMARK 500 LEU A 13 41.23 -97.75
REMARK 500 ASP A 16 138.55 -36.52
REMARK 500 ARG A 17 -161.85 53.22
REMARK 500 LYS A 18 51.29 -97.10
REMARK 500 LEU A 20 24.71 -75.87
REMARK 500 LYS A 22 -73.04 -67.77
REMARK 500 LYS A 31 -68.06 -124.95
REMARK 500 ASP A 38 111.95 -170.36
REMARK 500 LYS A 40 -98.00 -78.51
REMARK 500 SER A 50 143.83 -179.92
REMARK 500 LYS A 52 52.79 -118.38
REMARK 500 ASP A 54 29.50 -76.84
REMARK 500 GLU A 55 72.16 -155.23
REMARK 500 ALA A 62 -83.81 -64.61
REMARK 500 ARG A 67 -164.05 -100.05
REMARK 500 PRO A 80 12.24 -62.91
REMARK 500 PHE A 82 23.89 -68.51
REMARK 500 GLU A 86 -78.73 -95.39
REMARK 500 MET A 88 -25.86 -30.63
REMARK 500 ASN A 102 -73.03 -76.76
REMARK 500 SER A 116 82.82 36.35
REMARK 500 PHE A 119 -159.47 -108.60
REMARK 500 CYS A 120 39.57 -152.60
REMARK 500 ILE A 121 137.06 -34.07
REMARK 500 ARG A 127 83.46 -179.89
REMARK 500 ARG A 128 113.48 -25.43
REMARK 500 ILE A 131 48.01 -77.16
REMARK 500 ARG A 144 -157.02 -77.75
REMARK 500 HIS A 151 147.18 -173.22
REMARK 500 PHE A 153 -78.10 -27.27
REMARK 500 GLU A 168 -157.36 -126.05
REMARK 500 CYS A 172 70.32 -151.00
REMARK 500 GLU A 177 -147.27 -94.89
REMARK 500 THR A 183 44.67 -72.42
REMARK 500 GLU A 184 -40.24 -149.56
REMARK 500 LYS A 195 -7.16 -49.36
REMARK 500 VAL A 196 -90.18 -108.91
REMARK 500 ALA A 197 88.18 -69.36
REMARK 500 LYS A 211 -84.91 -68.00
REMARK 500 GLU A 216 -68.77 -144.37
REMARK 500 ASP A 217 -2.74 -58.80
REMARK 500 ALA A 222 37.17 -74.88
REMARK 500 VAL A 225 -80.08 -72.90
REMARK 500 TYR A 229 -30.46 -146.69
REMARK 500
REMARK 500 THIS ENTRY HAS 198 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 903 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 183 OG1
REMARK 620 2 SER A 241 OG 103.7
REMARK 620 3 AGS A 999 O2G 99.0 53.8
REMARK 620 4 AGS A 999 O1B 57.4 127.8 79.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 902 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 28 O
REMARK 620 2 ASP B 28 OD1 90.3
REMARK 620 3 ASP B 30 OD2 114.1 155.4
REMARK 620 4 ARG B 31 N 60.9 114.8 81.9
REMARK 620 5 ASP B 32 OD1 175.2 94.4 61.2 116.0
REMARK 620 6 ASP B 32 N 112.7 91.9 81.9 57.7 66.3
REMARK 620 7 PHE B 34 O 137.1 54.6 101.9 151.0 47.3 94.1
REMARK 620 8 ASP B 39 OD1 101.0 106.8 67.0 133.8 78.5 141.4 71.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 19 O
REMARK 620 2 ASP C 19 OD1 76.1
REMARK 620 3 ASP C 22 O 94.1 167.0
REMARK 620 4 ASP C 22 OD1 68.7 109.6 73.9
REMARK 620 5 GLY C 23 O 55.8 89.0 78.3 114.6
REMARK 620 6 ASP C 25 OD2 109.9 55.4 122.3 163.5 74.4
REMARK 620 7 ALA C 27 O 119.1 54.1 138.9 95.1 139.5 70.9
REMARK 620 8 HOH C 903 O 163.6 114.8 76.6 95.5 133.1 86.6 64.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AGS A 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PDM A 900
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1B7T RELATED DB: PDB
REMARK 900 1B7T CONTAINS THE SAME PROTEIN COMPLEXED WITH MGADP.
REMARK 900 RELATED ID: 1KK8 RELATED DB: PDB
REMARK 900 1KK8 CONTAINS THE SAME PROTEIN, COMPLEXED WITH S1-ADP-BEFX.
DBREF 1KWO A 1 835 UNP P24733 MYS_AEQIR 1 835
DBREF 1KWO B 1 156 UNP P13543 MLR_AEQIR 1 156
DBREF 1KWO C 1 156 UNP P07291 MLE_AEQIR 1 156
SEQRES 1 A 835 MET ASN ILE ASP PHE SER ASP PRO ASP PHE GLN TYR LEU
SEQRES 2 A 835 ALA VAL ASP ARG LYS LYS LEU MET LYS GLU GLN THR ALA
SEQRES 3 A 835 ALA PHE ASP GLY LYS LYS ASN CYS TRP VAL PRO ASP GLU
SEQRES 4 A 835 LYS GLU GLY PHE ALA SER ALA GLU ILE GLN SER SER LYS
SEQRES 5 A 835 GLY ASP GLU ILE THR VAL LYS ILE VAL ALA ASP SER SER
SEQRES 6 A 835 THR ARG THR VAL LYS LYS ASP ASP ILE GLN SER MET ASN
SEQRES 7 A 835 PRO PRO LYS PHE GLU LYS LEU GLU ASP MET ALA ASN MET
SEQRES 8 A 835 THR TYR LEU ASN GLU ALA SER VAL LEU TYR ASN LEU ARG
SEQRES 9 A 835 SER ARG TYR THR SER GLY LEU ILE TYR THR TYR SER GLY
SEQRES 10 A 835 LEU PHE CYS ILE ALA VAL ASN PRO TYR ARG ARG LEU PRO
SEQRES 11 A 835 ILE TYR THR ASP SER VAL ILE ALA LYS TYR ARG GLY LYS
SEQRES 12 A 835 ARG LYS THR GLU ILE PRO PRO HIS LEU PHE SER VAL ALA
SEQRES 13 A 835 ASP ASN ALA TYR GLN ASN MET VAL THR ASP ARG GLU ASN
SEQRES 14 A 835 GLN SER CYS LEU ILE THR GLY GLU SER GLY ALA GLY LYS
SEQRES 15 A 835 THR GLU ASN THR LYS LYS VAL ILE MET TYR LEU ALA LYS
SEQRES 16 A 835 VAL ALA CYS ALA VAL LYS LYS LYS ASP GLU GLU ALA SER
SEQRES 17 A 835 ASP LYS LYS GLU GLY SER LEU GLU ASP GLN ILE ILE GLN
SEQRES 18 A 835 ALA ASN PRO VAL LEU GLU ALA TYR GLY ASN ALA LYS THR
SEQRES 19 A 835 THR ARG ASN ASN ASN SER SER ARG PHE GLY LYS PHE ILE
SEQRES 20 A 835 ARG ILE HIS PHE GLY PRO THR GLY LYS ILE ALA GLY ALA
SEQRES 21 A 835 ASP ILE GLU THR TYR LEU LEU GLU LYS SER ARG VAL THR
SEQRES 22 A 835 TYR GLN GLN SER ALA GLU ARG ASN TYR HIS ILE PHE TYR
SEQRES 23 A 835 GLN ILE CYS SER ASN ALA ILE PRO GLU LEU ASN ASP VAL
SEQRES 24 A 835 MET LEU VAL THR PRO ASP SER GLY LEU TYR SER PHE ILE
SEQRES 25 A 835 ASN GLN GLY CYS LEU THR VAL ASP ASN ILE ASP ASP VAL
SEQRES 26 A 835 GLU GLU PHE LYS LEU CYS ASP GLU ALA PHE ASP ILE LEU
SEQRES 27 A 835 GLY PHE THR LYS GLU GLU LYS GLN SER MET PHE LYS CYS
SEQRES 28 A 835 THR ALA SER ILE LEU HIS MET GLY GLU MET LYS PHE LYS
SEQRES 29 A 835 GLN ARG PRO ARG GLU GLU GLN ALA GLU SER ASP GLY THR
SEQRES 30 A 835 ALA GLU ALA GLU LYS VAL ALA PHE LEU CYS GLY ILE ASN
SEQRES 31 A 835 ALA GLY ASP LEU LEU LYS ALA LEU LEU LYS PRO LYS VAL
SEQRES 32 A 835 LYS VAL GLY THR GLU MET VAL THR LYS GLY GLN ASN MET
SEQRES 33 A 835 ASN GLN VAL VAL ASN SER VAL GLY ALA LEU ALA LYS SER
SEQRES 34 A 835 LEU TYR ASP ARG MET PHE ASN TRP LEU VAL ARG ARG VAL
SEQRES 35 A 835 ASN LYS THR LEU ASP THR LYS ALA LYS ARG ASN TYR TYR
SEQRES 36 A 835 ILE GLY VAL LEU ASP ILE ALA GLY PHE GLU ILE PHE ASP
SEQRES 37 A 835 PHE ASN SER PHE GLU GLN LEU CYS ILE ASN TYR THR ASN
SEQRES 38 A 835 GLU ARG LEU GLN GLN PHE PHE ASN HIS HIS MET PHE ILE
SEQRES 39 A 835 LEU GLU GLN GLU GLU TYR LYS LYS GLU GLY ILE ALA TRP
SEQRES 40 A 835 GLU PHE ILE ASP PHE GLY MET ASP LEU GLN MET CYS ILE
SEQRES 41 A 835 ASP LEU ILE GLU LYS PRO MET GLY ILE LEU SER ILE LEU
SEQRES 42 A 835 GLU GLU GLU CYS MET PHE PRO LYS ALA ASP ASP LYS SER
SEQRES 43 A 835 PHE GLN ASP LYS LEU TYR GLN ASN HIS MET GLY LYS ASN
SEQRES 44 A 835 ARG MET PHE THR LYS PRO GLY LYS PRO THR ARG PRO ASN
SEQRES 45 A 835 GLN GLY PRO ALA HIS PHE GLU LEU HIS HIS TYR ALA GLY
SEQRES 46 A 835 ASN VAL PRO TYR SER ILE THR GLY TRP LEU GLU LYS ASN
SEQRES 47 A 835 LYS ASP PRO ILE ASN GLU ASN VAL VAL ALA LEU LEU GLY
SEQRES 48 A 835 ALA SER LYS GLU PRO LEU VAL ALA GLU LEU PHE LYS ALA
SEQRES 49 A 835 PRO GLU GLU PRO ALA GLY GLY GLY LYS LYS LYS LYS GLY
SEQRES 50 A 835 LYS SER SER ALA PHE GLN THR ILE SER ALA VAL HIS ARG
SEQRES 51 A 835 GLU SER LEU ASN LYS LEU MET LYS ASN LEU TYR SER THR
SEQRES 52 A 835 HIS PRO HIS PHE VAL ARG CYS ILE ILE PRO ASN GLU LEU
SEQRES 53 A 835 LYS GLN PRO GLY LEU VAL ASP ALA GLU LEU VAL LEU HIS
SEQRES 54 A 835 GLN LEU GLN CYS ASN GLY VAL LEU GLU GLY ILE ARG ILE
SEQRES 55 A 835 CYS ARG LYS GLY PHE PRO SER ARG LEU ILE TYR SER GLU
SEQRES 56 A 835 PHE LYS GLN ARG TYR SER ILE LEU ALA PRO ASN ALA ILE
SEQRES 57 A 835 PRO GLN GLY PHE VAL ASP GLY LYS THR VAL SER GLU LYS
SEQRES 58 A 835 ILE LEU ALA GLY LEU GLN MET ASP PRO ALA GLU TYR ARG
SEQRES 59 A 835 LEU GLY THR THR LYS VAL PHE PHE LYS ALA GLY VAL LEU
SEQRES 60 A 835 GLY ASN LEU GLU GLU MET ARG ASP GLU ARG LEU SER LYS
SEQRES 61 A 835 ILE ILE SER MET PHE GLN ALA HIS ILE ARG GLY TYR LEU
SEQRES 62 A 835 ILE ARG LYS ALA TYR LYS LYS LEU GLN ASP GLN ARG ILE
SEQRES 63 A 835 GLY LEU SER VAL ILE GLN ARG ASN ILE ARG LYS TRP LEU
SEQRES 64 A 835 VAL LEU ARG ASN TRP GLN TRP TRP LYS LEU TYR SER LYS
SEQRES 65 A 835 VAL LYS PRO
SEQRES 1 B 156 ALA ASP LYS ALA ALA SER GLY VAL LEU THR LYS LEU PRO
SEQRES 2 B 156 GLN LYS GLN ILE GLN GLU MET LYS GLU ALA PHE SER MET
SEQRES 3 B 156 ILE ASP VAL ASP ARG ASP GLY PHE VAL SER LYS GLU ASP
SEQRES 4 B 156 ILE LYS ALA ILE SER GLU GLN LEU GLY ARG ALA PRO ASP
SEQRES 5 B 156 ASP LYS GLU LEU THR ALA MET LEU LYS GLU ALA PRO GLY
SEQRES 6 B 156 PRO LEU ASN PHE THR MET PHE LEU SER ILE PHE SER ASP
SEQRES 7 B 156 LYS LEU SER GLY THR ASP SER GLU GLU THR ILE ARG ASN
SEQRES 8 B 156 ALA PHE ALA MET PHE ASP GLU GLN GLU THR LYS LYS LEU
SEQRES 9 B 156 ASN ILE GLU TYR ILE LYS ASP LEU LEU GLU ASN MET GLY
SEQRES 10 B 156 ASP ASN PHE ASN LYS ASP GLU MET ARG MET THR PHE LYS
SEQRES 11 B 156 GLU ALA PRO VAL GLU GLY GLY LYS PHE ASP TYR VAL LYS
SEQRES 12 B 156 PHE THR ALA MET ILE LYS GLY SER GLY GLU GLU GLU ALA
SEQRES 1 C 156 PRO LYS LEU SER GLN ASP GLU ILE ASP ASP LEU LYS ASP
SEQRES 2 C 156 VAL PHE GLU LEU PHE ASP PHE TRP ASP GLY ARG ASP GLY
SEQRES 3 C 156 ALA VAL ASP ALA PHE LYS LEU GLY ASP VAL CYS ARG CYS
SEQRES 4 C 156 LEU GLY ILE ASN PRO ARG ASN GLU ASP VAL PHE ALA VAL
SEQRES 5 C 156 GLY GLY THR HIS LYS MET GLY GLU LYS SER LEU PRO PHE
SEQRES 6 C 156 GLU GLU PHE LEU PRO ALA TYR GLU GLY LEU MET ASP CYS
SEQRES 7 C 156 GLU GLN GLY THR PHE ALA ASP TYR MET GLU ALA PHE LYS
SEQRES 8 C 156 THR PHE ASP ARG GLU GLY GLN GLY PHE ILE SER GLY ALA
SEQRES 9 C 156 GLU LEU ARG HIS VAL LEU THR ALA LEU GLY GLU ARG LEU
SEQRES 10 C 156 SER ASP GLU ASP VAL ASP GLU ILE ILE LYS LEU THR ASP
SEQRES 11 C 156 LEU GLN GLU ASP LEU GLU GLY ASN VAL LYS TYR GLU ASP
SEQRES 12 C 156 PHE VAL LYS LYS VAL MET ALA GLY PRO TYR PRO ASP LYS
HET MG A 903 1
HET AGS A 999 31
HET PDM A 900 21
HET CA C 501 1
HET MG C 902 1
HETNAM MG MAGNESIUM ION
HETNAM AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER
HETNAM PDM 4-[4-(2,5-DIOXO-PYRROLIDIN-1-YL)-PHENYLAMINO]-4-
HETNAM 2 PDM HYDROXY-BUTYRIC ACID
HETNAM CA CALCIUM ION
HETSYN AGS ATP-GAMMA-S; ADENOSINE 5'-(3-THIOTRIPHOSPHATE);
HETSYN 2 AGS ADENOSINE 5'-(GAMMA-THIOTRIPHOSPHATE); ADENOSINE-5'-
HETSYN 3 AGS DIPHOSPHATE MONOTHIOPHOSPHATE
HETSYN PDM PARA-PHENYL DIMALEMIDE
FORMUL 4 MG 2(MG 2+)
FORMUL 5 AGS C10 H16 N5 O12 P3 S
FORMUL 6 PDM C14 H16 N2 O5
FORMUL 7 CA CA 2+
FORMUL 9 HOH *6(H2 O)
HELIX 1 1 ASP A 87 MET A 91 5 5
HELIX 2 2 ALA A 97 THR A 108 1 12
HELIX 3 3 THR A 133 TYR A 140 1 8
HELIX 4 4 HIS A 151 THR A 165 1 15
HELIX 5 5 GLU A 184 VAL A 196 1 13
HELIX 6 6 ASN A 223 GLY A 230 1 8
HELIX 7 7 GLU A 268 TYR A 274 5 7
HELIX 8 8 HIS A 283 CYS A 289 1 7
HELIX 9 10 ASP A 323 PHE A 340 1 18
HELIX 10 11 THR A 341 GLY A 359 1 19
HELIX 11 12 THR A 377 GLY A 388 1 12
HELIX 12 13 ASN A 390 LYS A 400 1 11
HELIX 13 14 MET A 416 LEU A 446 1 31
HELIX 14 15 SER A 471 MET A 492 1 22
HELIX 15 17 CYS A 519 LYS A 525 1 7
HELIX 16 19 ASP A 543 GLN A 553 1 11
HELIX 17 20 LEU A 595 LYS A 599 5 5
HELIX 18 22 GLU A 615 PHE A 622 1 8
HELIX 19 23 VAL A 648 TYR A 661 1 14
HELIX 20 25 SER A 714 GLN A 718 5 5
HELIX 21 26 TYR A 720 ALA A 724 5 5
HELIX 22 27 GLY A 735 LEU A 746 1 12
HELIX 23 28 VAL A 766 LYS A 799 1 34
HELIX 24 29 LYS A 799 ARG A 816 1 18
HELIX 25 30 TRP A 818 ASN A 823 1 6
HELIX 26 31 TRP A 824 VAL A 833 1 10
HELIX 27 32 GLN B 14 ASP B 28 1 15
HELIX 28 34 ASP B 52 ALA B 58 1 7
HELIX 29 35 SER B 74 LYS B 79 1 6
HELIX 30 36 SER B 85 ALA B 94 1 10
HELIX 31 37 ASN B 105 ASN B 115 1 11
HELIX 32 38 ASN B 121 LYS B 130 1 10
HELIX 33 39 ASP B 140 LYS B 149 1 10
HELIX 34 40 SER C 4 ASP C 22 1 19
HELIX 35 43 PRO C 64 GLU C 73 1 10
HELIX 36 44 THR C 82 THR C 92 1 11
HELIX 37 45 GLY C 103 LEU C 110 1 8
HELIX 38 46 SER C 118 ASP C 130 1 13
HELIX 39 47 LYS C 140 GLY C 151 1 12
SHEET 1 A 3 ASN A 33 ASP A 38 0
SHEET 2 A 3 GLY A 42 SER A 51 -1 O ALA A 44 N VAL A 36
SHEET 3 A 3 ILE A 56 ILE A 60 -1 O THR A 57 N SER A 50
SHEET 1 B 2 ALA A 122 VAL A 123 0
SHEET 2 B 2 CYS A 670 ILE A 671 1 O ILE A 671 N ALA A 122
SHEET 1 C 3 GLN A 170 LEU A 173 0
SHEET 2 C 3 ARG A 248 GLY A 252 -1 N ILE A 249 O ILE A 456
SHEET 3 C 3 LYS A 256 ASP A 261 -1 O GLY A 259 N HIS A 250
SHEET 1 D 2 ASN A 231 ALA A 232 0
SHEET 2 D 2 SER A 240 SER A 241 -1 O SER A 240 N ALA A 232
SHEET 1 E 1 SER A 709 ILE A 712 0
SHEET 1 F 1 VAL B 134 GLU B 135 0
SHEET 1 G 2 VAL C 28 ASP C 29 0
SHEET 2 G 2 SER C 62 LEU C 63 -1 O LEU C 63 N VAL C 28
SHEET 1 H 1 ASN C 138 VAL C 139 0
LINK OG1 THR A 183 O1B AGS A 999 1555 1555 1.99
LINK SG CYS A 693 CP9 PDM A 900 1555 1555 1.86
LINK NZ LYS A 705 C13 PDM A 900 1555 1555 1.37
LINK OG1 THR A 183 MG MG A 903 1555 1555 1.95
LINK OG SER A 241 MG MG A 903 1555 1555 2.36
LINK MG MG A 903 O2G AGS A 999 1555 1555 2.78
LINK MG MG A 903 O1B AGS A 999 1555 1555 2.18
LINK O ASP B 28 MG MG C 902 1555 1555 3.11
LINK OD1 ASP B 28 MG MG C 902 1555 1555 1.72
LINK OD2 ASP B 30 MG MG C 902 1555 1555 2.56
LINK N ARG B 31 MG MG C 902 1555 1555 2.72
LINK OD1 ASP B 32 MG MG C 902 1555 1555 2.17
LINK N ASP B 32 MG MG C 902 1555 1555 2.83
LINK O PHE B 34 MG MG C 902 1555 1555 2.90
LINK OD1 ASP B 39 MG MG C 902 1555 1555 2.38
LINK O ASP C 19 CA CA C 501 1555 1555 2.69
LINK OD1 ASP C 19 CA CA C 501 1555 1555 2.36
LINK O ASP C 22 CA CA C 501 1555 1555 2.76
LINK OD1 ASP C 22 CA CA C 501 1555 1555 2.04
LINK O GLY C 23 CA CA C 501 1555 1555 2.17
LINK OD2 ASP C 25 CA CA C 501 1555 1555 2.41
LINK O ALA C 27 CA CA C 501 1555 1555 2.67
LINK CA CA C 501 O HOH C 903 1555 1555 2.77
SITE 1 AC1 6 ASP C 19 ASP C 22 GLY C 23 ASP C 25
SITE 2 AC1 6 ALA C 27 HOH C 903
SITE 1 AC2 7 ASP B 28 VAL B 29 ASP B 30 ARG B 31
SITE 2 AC2 7 ASP B 32 PHE B 34 ASP B 39
SITE 1 AC3 3 THR A 183 SER A 241 AGS A 999
SITE 1 AC4 18 ASN A 124 PRO A 125 TYR A 126 TYR A 132
SITE 2 AC4 18 GLU A 177 SER A 178 GLY A 179 ALA A 180
SITE 3 AC4 18 GLY A 181 LYS A 182 THR A 183 GLU A 184
SITE 4 AC4 18 ASN A 185 ASN A 237 ASN A 239 SER A 241
SITE 5 AC4 18 ALA A 462 MG A 903
SITE 1 AC5 5 TYR A 583 ALA A 584 GLN A 692 CYS A 693
SITE 2 AC5 5 LYS A 705
CRYST1 51.816 57.028 151.708 95.16 96.45 100.93 P 1 1
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 0.019299 0.003725 0.002624 0.00000
SCALE2 0.000000 0.017859 0.002049 0.00000
SCALE3 0.000000 0.000000 0.006677 0.00000
(ATOM LINES ARE NOT SHOWN.)
END