HEADER CONTRACTILE PROTEIN 22-FEB-02 1L2O
TITLE SCALLOP MYOSIN S1-ADP-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 M.HIMMEL,S.GOURINATH,L.RESHETNIKOVA,Y.SHEN,G.SZENT-GYORGYI,C.COHEN
REVDAT 4 16-AUG-23 1L2O 1 REMARK SHEET LINK
REVDAT 3 24-FEB-09 1L2O 1 VERSN
REVDAT 2 01-APR-03 1L2O 1 JRNL
REVDAT 1 30-OCT-02 1L2O 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. 2.80 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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 54.16
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 37648249.680
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 72.0
REMARK 3 NUMBER OF REFLECTIONS : 29564
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) : 0.280
REMARK 3 FREE R VALUE : 0.327
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1516
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 24.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1584
REMARK 3 BIN R VALUE (WORKING SET) : 0.4960
REMARK 3 BIN FREE R VALUE : 0.5240
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 82
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.058
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8257
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 51
REMARK 3 SOLVENT ATOMS : 31
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 54.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 89.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.56000
REMARK 3 B22 (A**2) : 41.64000
REMARK 3 B33 (A**2) : -37.09000
REMARK 3 B12 (A**2) : 14.79000
REMARK 3 B13 (A**2) : 15.42000
REMARK 3 B23 (A**2) : 6.33000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.62
REMARK 3 ESD FROM SIGMAA (A) : 0.68
REMARK 3 LOW RESOLUTION CUTOFF (A) : 54.2
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.67
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.72
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.900
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 4.020
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) : 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 : FLAT MODEL
REMARK 3 KSOL : 0.29
REMARK 3 BSOL : 45.74
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 : CYP.PARAM
REMARK 3 PARAMETER FILE 5 : ADP.PARAM
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 : CYP.TOP
REMARK 3 TOPOLOGY FILE 5 : ADP.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 1L2O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-02.
REMARK 100 THE DEPOSITION ID IS D_1000015588.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-MAR-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 : X26C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
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 : 29564
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 55.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 74.4
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.03500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 24.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.15300
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1KK8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.28
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 POLY-PEPTIDE CHAINS (HEAVY
REMARK 300 CHAIN, REGULATORY LIGHT CHAIN, ESSENTIAL LIGHT CHAIN), AND CAN THUS
REMARK 300 ALSO BE 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: 9770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 50580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -94.0 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 GLU A 23
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 LYS A 210
REMARK 465 LYS A 364
REMARK 465 GLN A 365
REMARK 465 ARG A 366
REMARK 465 PRO A 367
REMARK 465 ARG A 368
REMARK 465 GLU A 369
REMARK 465 GLU A 370
REMARK 465 LYS A 404
REMARK 465 VAL A 405
REMARK 465 GLY A 406
REMARK 465 PRO A 568
REMARK 465 THR A 569
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 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 TYR A 12 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A 13 CG CD1 CD2
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 39 CG CD OE1 OE2
REMARK 470 LYS A 40 CG CD CE NZ
REMARK 470 ASN A 162 CG OD1 ND2
REMARK 470 GLU A 295 CG CD OE1 OE2
REMARK 470 ASP A 393 CG OD1 OD2
REMARK 470 LYS A 396 CG CD CE NZ
REMARK 470 THR A 407 OG1 CG2
REMARK 470 GLU A 408 CG CD OE1 OE2
REMARK 470 VAL A 410 CG1 CG2
REMARK 470 LYS A 412 CG CD CE NZ
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 GLU A 498 CG CD OE1 OE2
REMARK 470 GLU A 503 CG CD OE1 OE2
REMARK 470 PHE A 509 CG CD1 CD2 CE1 CE2 CZ
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 LYS A 564 CG CD CE NZ
REMARK 470 LYS A 567 CG CD CE NZ
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 LYS A 614 CG CD CE NZ
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 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 LYS A 759 CG CD CE NZ
REMARK 470 GLU A 776 CG CD OE1 OE2
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 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 ARG B 31 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 41 CG CD CE NZ
REMARK 470 GLU B 45 CG CD OE1 OE2
REMARK 470 GLN B 99 CG CD OE1 NE2
REMARK 470 LYS B 103 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 ASP C 13 CG OD1 OD2
REMARK 470 ARG C 38 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 45 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 57 CG CD CE NZ
REMARK 470 LYS C 61 CG CD CE NZ
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 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 CB SER A 98 O HOH A 1021 1.54
REMARK 500 O TYR A 500 O ILE A 505 1.80
REMARK 500 OD1 ASP A 157 OH TYR A 192 1.97
REMARK 500 OD1 ASP A 134 CE LYS A 195 1.99
REMARK 500 OG1 THR A 183 O HOH A 1017 2.02
REMARK 500 CD LYS A 705 C13 PDM A 900 2.10
REMARK 500 OH TYR A 286 O ILE A 312 2.11
REMARK 500 O GLU B 135 N GLY B 137 2.13
REMARK 500 O LEU A 395 O HOH A 1005 2.15
REMARK 500 O ARG A 242 O HOH A 1003 2.15
REMARK 500 O ASP B 32 N PHE B 34 2.15
REMARK 500 CD LYS A 705 C12 PDM A 900 2.15
REMARK 500 O ASN A 281 O HOH A 1018 2.17
REMARK 500 CE LYS A 705 C12 PDM A 900 2.18
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 ASP A 7 N - CA - C ANGL. DEV. = 16.5 DEGREES
REMARK 500 PRO A 8 C - N - CA ANGL. DEV. = -11.8 DEGREES
REMARK 500 ALA A 14 N - CA - C ANGL. DEV. = 16.9 DEGREES
REMARK 500 LEU A 111 N - CA - C ANGL. DEV. = -18.8 DEGREES
REMARK 500 THR A 407 N - CA - C ANGL. DEV. = -21.1 DEGREES
REMARK 500 GLU A 503 CA - C - N ANGL. DEV. = -12.7 DEGREES
REMARK 500 ILE A 510 CB - CA - C ANGL. DEV. = -14.7 DEGREES
REMARK 500 PHE A 539 CB - CA - C ANGL. DEV. = -12.7 DEGREES
REMARK 500 PHE A 539 CB - CG - CD1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 PRO A 601 C - N - CA ANGL. DEV. = 13.3 DEGREES
REMARK 500 HIS A 664 N - CA - C ANGL. DEV. = -16.2 DEGREES
REMARK 500 GLY A 695 O - C - N ANGL. DEV. = 11.5 DEGREES
REMARK 500 PRO A 725 N - CA - C ANGL. DEV. = 17.2 DEGREES
REMARK 500 GLY A 765 N - CA - C ANGL. DEV. = -16.7 DEGREES
REMARK 500 ASP B 97 N - CA - C ANGL. DEV. = -18.1 DEGREES
REMARK 500 ASP B 118 N - CA - C ANGL. DEV. = -17.1 DEGREES
REMARK 500 GLY B 150 N - CA - C ANGL. DEV. = 18.5 DEGREES
REMARK 500 SER B 151 N - CA - C ANGL. DEV. = 23.1 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 -152.94 -105.47
REMARK 500 ASP A 7 88.29 -174.72
REMARK 500 PRO A 8 -75.43 -77.00
REMARK 500 GLN A 11 -94.74 -36.99
REMARK 500 TYR A 12 44.35 -102.27
REMARK 500 LEU A 13 -35.67 -139.42
REMARK 500 VAL A 15 -62.81 -147.82
REMARK 500 LEU A 20 -71.57 -136.61
REMARK 500 LYS A 52 32.69 -157.29
REMARK 500 ASP A 54 46.21 -70.62
REMARK 500 GLU A 55 47.68 -148.08
REMARK 500 ILE A 56 105.21 -57.19
REMARK 500 ALA A 62 -77.40 -59.52
REMARK 500 LYS A 71 -11.97 -49.86
REMARK 500 ASP A 73 1.73 -63.14
REMARK 500 LYS A 84 54.39 39.84
REMARK 500 ASP A 87 73.14 -161.82
REMARK 500 MET A 88 3.84 -46.02
REMARK 500 LEU A 94 47.23 -96.10
REMARK 500 TYR A 101 -80.96 -60.76
REMARK 500 ASN A 102 -16.79 -37.54
REMARK 500 SER A 116 88.71 -69.33
REMARK 500 LEU A 118 27.03 -69.77
REMARK 500 TYR A 126 32.26 73.48
REMARK 500 PRO A 130 37.96 -89.34
REMARK 500 LYS A 145 -17.40 -44.33
REMARK 500 HIS A 151 124.33 172.99
REMARK 500 LEU A 152 -51.08 -24.56
REMARK 500 PHE A 153 -73.30 -40.48
REMARK 500 ASN A 158 -23.79 -37.62
REMARK 500 ARG A 167 79.88 39.99
REMARK 500 GLU A 177 -154.09 -85.95
REMARK 500 ALA A 180 -73.45 -73.31
REMARK 500 LYS A 182 -80.38 -38.30
REMARK 500 THR A 183 34.10 -61.71
REMARK 500 GLU A 184 -68.54 -132.74
REMARK 500 LEU A 193 -14.21 -43.83
REMARK 500 CYS A 198 167.63 -43.27
REMARK 500 ALA A 222 28.84 -71.58
REMARK 500 ASN A 239 67.38 -115.37
REMARK 500 PRO A 253 9.41 -58.20
REMARK 500 GLU A 263 90.70 -160.29
REMARK 500 HIS A 283 -66.18 -20.94
REMARK 500 ILE A 284 -71.51 -29.29
REMARK 500 PHE A 285 -51.11 -29.82
REMARK 500 ASN A 291 35.24 79.17
REMARK 500 ILE A 293 77.26 -118.35
REMARK 500 GLU A 295 21.37 -65.64
REMARK 500 PRO A 304 84.32 -49.96
REMARK 500 ASN A 313 47.91 -82.98
REMARK 500
REMARK 500 THIS ENTRY HAS 147 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 77.2
REMARK 620 3 ADP A 999 O2B 76.4 147.2
REMARK 620 4 ADP A 999 O3B 127.0 155.5 55.3
REMARK 620 5 HOH A1016 O 114.3 68.0 106.2 100.2
REMARK 620 6 HOH A1017 O 59.0 105.7 76.6 87.2 172.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 902 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 28 OD1
REMARK 620 2 ASP B 30 OD2 147.8
REMARK 620 3 ASP B 30 OD1 111.8 47.3
REMARK 620 4 ARG B 31 N 97.0 101.2 79.5
REMARK 620 5 ASP B 32 N 99.7 112.2 133.8 63.2
REMARK 620 6 ASP B 32 OD1 92.5 74.2 104.1 167.8 107.6
REMARK 620 7 PHE B 34 O 47.5 115.8 120.8 142.4 105.5 45.3
REMARK 620 8 ASP B 39 OD2 63.6 84.2 64.0 124.4 161.2 66.9 57.4
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 OD1
REMARK 620 2 ASP C 19 O 66.5
REMARK 620 3 ASP C 22 OD1 116.7 54.4
REMARK 620 4 GLY C 23 O 70.7 56.1 92.0
REMARK 620 5 ASP C 25 OD2 67.7 114.9 156.0 66.5
REMARK 620 6 ASP C 25 OD1 111.3 121.3 116.9 67.8 46.4
REMARK 620 7 ALA C 27 O 61.3 101.8 108.7 132.0 94.1 129.6
REMARK 620 8 HOH C 502 O 151.0 142.0 91.6 116.8 89.0 54.9 105.6
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 B 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 PDM A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 999
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 1L2O A 1 835 UNP P24733 MYS_AEQIR 1 835
DBREF 1L2O B 1 156 UNP P13543 MLR_AEQIR 1 156
DBREF 1L2O 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 PDM A 900 21
HET ADP A 999 27
HET MG B 902 1
HET CA C 501 1
HETNAM MG MAGNESIUM ION
HETNAM PDM 4-[4-(2,5-DIOXO-PYRROLIDIN-1-YL)-PHENYLAMINO]-4-
HETNAM 2 PDM HYDROXY-BUTYRIC ACID
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM CA CALCIUM ION
HETSYN PDM PARA-PHENYL DIMALEMIDE
FORMUL 4 MG 2(MG 2+)
FORMUL 5 PDM C14 H16 N2 O5
FORMUL 6 ADP C10 H15 N5 O10 P2
FORMUL 8 CA CA 2+
FORMUL 9 HOH *31(H2 O)
HELIX 1 1 PRO A 79 GLU A 83 5 5
HELIX 2 2 ASN A 95 SER A 109 1 15
HELIX 3 3 THR A 133 ARG A 141 1 9
HELIX 4 4 HIS A 151 ARG A 167 1 17
HELIX 5 5 GLY A 181 ALA A 197 1 17
HELIX 6 6 SER A 214 ALA A 222 1 9
HELIX 7 7 ASN A 223 GLY A 230 1 8
HELIX 8 8 GLU A 268 TYR A 274 5 7
HELIX 9 9 TYR A 282 CYS A 289 1 8
HELIX 10 10 ILE A 293 GLU A 295 5 3
HELIX 11 11 LEU A 296 LEU A 301 1 6
HELIX 12 12 ASP A 323 LEU A 338 1 16
HELIX 13 13 THR A 341 MET A 361 1 21
HELIX 14 14 GLU A 379 CYS A 387 1 9
HELIX 15 15 ASN A 390 LEU A 398 1 9
HELIX 16 16 ASN A 415 LEU A 446 1 32
HELIX 17 17 SER A 471 GLU A 498 1 28
HELIX 18 18 GLY A 513 LYS A 525 1 13
HELIX 19 19 GLY A 528 GLU A 536 1 9
HELIX 20 20 ASP A 543 ASP A 549 1 7
HELIX 21 21 LEU A 551 MET A 556 1 6
HELIX 22 22 GLY A 593 LYS A 599 1 7
HELIX 23 23 ASN A 603 ALA A 612 1 10
HELIX 24 24 GLU A 615 PHE A 622 1 8
HELIX 25 25 SER A 646 TYR A 661 1 16
HELIX 26 26 ASP A 683 GLN A 692 1 10
HELIX 27 27 TYR A 713 SER A 721 1 9
HELIX 28 28 GLY A 735 LEU A 746 1 12
HELIX 29 29 GLY A 765 ALA A 797 1 33
HELIX 30 30 TYR A 798 ASN A 814 1 17
HELIX 31 31 ASN A 814 ASN A 823 1 10
HELIX 32 32 TRP A 824 VAL A 833 1 10
HELIX 33 33 GLN B 16 ASP B 28 1 13
HELIX 34 34 SER B 36 LEU B 47 1 12
HELIX 35 35 ASP B 52 LYS B 61 1 10
HELIX 36 36 ASN B 68 LYS B 79 1 12
HELIX 37 37 SER B 85 MET B 95 1 11
HELIX 38 38 ASN B 105 ASN B 115 1 11
HELIX 39 39 ASN B 121 LYS B 130 1 10
HELIX 40 40 ASP B 140 LYS B 149 1 10
HELIX 41 41 SER C 4 ASP C 19 1 16
HELIX 42 42 PHE C 20 GLY C 23 5 4
HELIX 43 43 PHE C 31 VAL C 36 1 6
HELIX 44 44 CYS C 37 GLY C 41 5 5
HELIX 45 45 ARG C 45 GLY C 53 1 9
HELIX 46 46 PRO C 64 CYS C 78 1 15
HELIX 47 47 THR C 82 LYS C 91 1 10
HELIX 48 48 THR C 92 ASP C 94 5 3
HELIX 49 49 GLY C 103 LEU C 113 1 11
HELIX 50 50 SER C 118 THR C 129 1 12
HELIX 51 51 TYR C 141 GLY C 151 1 11
SHEET 1 A 5 SER A 65 VAL A 69 0
SHEET 2 A 5 ILE A 56 ILE A 60 -1 N VAL A 58 O ARG A 67
SHEET 3 A 5 GLY A 42 SER A 50 -1 N GLU A 47 O LYS A 59
SHEET 4 A 5 ASN A 33 ASP A 38 -1 N ASP A 38 O GLY A 42
SHEET 5 A 5 GLN A 75 SER A 76 -1 O GLN A 75 N TRP A 35
SHEET 1 B 5 ALA A 122 VAL A 123 0
SHEET 2 B 5 THR A 663 ILE A 671 1 O ILE A 671 N ALA A 122
SHEET 3 B 5 ASN A 169 THR A 175 1 N THR A 175 O VAL A 668
SHEET 4 B 5 LEU A 459 ASP A 460 1 O LEU A 459 N ILE A 174
SHEET 5 B 5 LYS A 245 PHE A 246 -1 N LYS A 245 O ASP A 460
SHEET 1 C 2 ASN A 231 THR A 234 0
SHEET 2 C 2 ASN A 237 SER A 241 -1 O ASN A 237 N THR A 234
SHEET 1 D 2 ILE A 257 ASP A 261 0
SHEET 2 D 2 ARG A 248 PHE A 251 -1 N HIS A 250 O GLY A 259
SHEET 1 E 2 PHE A 578 HIS A 582 0
SHEET 2 E 2 GLY A 585 TYR A 589 -1 O TYR A 589 N PHE A 578
SHEET 1 F 2 ARG A 710 ILE A 712 0
SHEET 2 F 2 TYR A 753 ARG A 754 -1 N ARG A 754 O PHE A 761
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 2 PHE C 100 SER C 102 0
SHEET 2 H 2 ASN C 138 LYS C 140 -1
LINK SG CYS A 693 CP9 PDM A 900 1555 1555 1.81
LINK NZ LYS A 705 C13 PDM A 900 1555 1555 1.45
LINK CE LYS A 705 C13 PDM A 900 1555 1555 1.98
LINK OG1 THR A 183 MG MG A 903 1555 1555 2.02
LINK OG SER A 241 MG MG A 903 1555 1555 2.41
LINK MG MG A 903 O2B ADP A 999 1555 1555 1.91
LINK MG MG A 903 O3B ADP A 999 1555 1555 2.98
LINK MG MG A 903 O HOH A1016 1555 1555 2.08
LINK MG MG A 903 O HOH A1017 1555 1555 2.09
LINK OD1 ASP B 28 MG MG B 902 1555 1555 2.34
LINK OD2 ASP B 30 MG MG B 902 1555 1555 2.93
LINK OD1 ASP B 30 MG MG B 902 1555 1555 2.50
LINK N ARG B 31 MG MG B 902 1555 1555 2.79
LINK N ASP B 32 MG MG B 902 1555 1555 2.07
LINK OD1 ASP B 32 MG MG B 902 1555 1555 1.90
LINK O PHE B 34 MG MG B 902 1555 1555 3.13
LINK OD2 ASP B 39 MG MG B 902 1555 1555 2.49
LINK OD1 ASP C 19 CA CA C 501 1555 1555 2.25
LINK O ASP C 19 CA CA C 501 1555 1555 2.97
LINK OD1 ASP C 22 CA CA C 501 1555 1555 2.25
LINK O GLY C 23 CA CA C 501 1555 1555 2.61
LINK OD2 ASP C 25 CA CA C 501 1555 1555 2.01
LINK OD1 ASP C 25 CA CA C 501 1555 1555 3.01
LINK O ALA C 27 CA CA C 501 1555 1555 2.26
LINK CA CA C 501 O HOH C 502 1555 1555 2.63
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 502
SITE 1 AC2 6 ASP B 28 ASP B 30 ARG B 31 ASP B 32
SITE 2 AC2 6 PHE B 34 ASP B 39
SITE 1 AC3 5 THR A 183 SER A 241 ADP A 999 HOH A1016
SITE 2 AC3 5 HOH A1017
SITE 1 AC4 5 GLN A 485 TYR A 583 GLN A 692 CYS A 693
SITE 2 AC4 5 LYS A 705
SITE 1 AC5 18 ASN A 124 PRO A 125 TYR A 126 ARG A 127
SITE 2 AC5 18 TYR A 132 GLY A 179 ALA A 180 GLY A 181
SITE 3 AC5 18 LYS A 182 THR A 183 GLU A 184 ASN A 237
SITE 4 AC5 18 ASN A 239 MG A 903 HOH A1016 HOH A1017
SITE 5 AC5 18 HOH A1022 HOH A1023
CRYST1 51.800 57.000 150.500 95.60 96.30 101.50 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 0.019305 0.003928 0.002633 0.00000
SCALE2 0.000000 0.017903 0.002213 0.00000
SCALE3 0.000000 0.000000 0.006736 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
