HEADER MOTOR PROTEIN 29-AUG-16 5T45
TITLE CHICKEN SMOOTH MUSCLE MYOSIN MOTOR DOMAIN CO-CRYSTALLIZED WITH THE
TITLE 2 SPECIFIC CK-571 INHIBITOR, MGADP.BEFX FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYOSIN-11;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS MYOSIN INHIBITOR, MOTOR PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.SIRIGU,V.J.PLANELLES-HERRERO,J.HARTMAN,A.HOUDUSSE
REVDAT 6 17-JAN-24 5T45 1 LINK
REVDAT 5 06-SEP-17 5T45 1 REMARK
REVDAT 4 18-JAN-17 5T45 1 TITLE
REVDAT 3 14-DEC-16 5T45 1 JRNL
REVDAT 2 07-DEC-16 5T45 1
REVDAT 1 16-NOV-16 5T45 0
JRNL AUTH S.SIRIGU,J.J.HARTMAN,V.J.PLANELLES-HERRERO,V.ROPARS,
JRNL AUTH 2 S.CLANCY,X.WANG,G.CHUANG,X.QIAN,P.P.LU,E.BARRETT,K.RUDOLPH,
JRNL AUTH 3 C.ROYER,B.P.MORGAN,E.A.STURA,F.I.MALIK,A.M.HOUDUSSE
JRNL TITL HIGHLY SELECTIVE INHIBITION OF MYOSIN MOTORS PROVIDES THE
JRNL TITL 2 BASIS OF POTENTIAL THERAPEUTIC APPLICATION.
JRNL REF PROC. NATL. ACAD. SCI. V. 113 E7448 2016
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 27815532
JRNL DOI 10.1073/PNAS.1609342113
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.35
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 25175
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 + TEST SET) : 0.222
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1260
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 13
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.96
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2818
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2290
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2677
REMARK 3 BIN R VALUE (WORKING SET) : 0.2260
REMARK 3 BIN FREE R VALUE : 0.2940
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 141
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5604
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 96
REMARK 3 SOLVENT ATOMS : 83
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 72.89
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 64.51
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.62810
REMARK 3 B22 (A**2) : -8.79500
REMARK 3 B33 (A**2) : 7.16690
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.410
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 1.142
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.360
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 1.049
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.363
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.881
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 5823 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 7873 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2063 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 167 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 865 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 5823 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 766 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 6737 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.18
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.65
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 21.47
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -30.0199 32.9770 -15.2707
REMARK 3 T TENSOR
REMARK 3 T11: -0.2143 T22: 0.1734
REMARK 3 T33: -0.5006 T12: 0.0084
REMARK 3 T13: -0.0157 T23: -0.0314
REMARK 3 L TENSOR
REMARK 3 L11: 1.1726 L22: 1.7382
REMARK 3 L33: 0.9129 L12: 0.8180
REMARK 3 L13: -0.2510 L23: -0.4641
REMARK 3 S TENSOR
REMARK 3 S11: 0.0687 S12: 0.0492 S13: 0.0090
REMARK 3 S21: -0.0347 S22: -0.0569 S23: 0.1132
REMARK 3 S31: 0.1273 S32: -0.0953 S33: -0.0117
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5T45 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-AUG-16.
REMARK 100 THE DEPOSITION ID IS D_1000223676.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-NOV-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978570
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS 10.9.4
REMARK 200 DATA SCALING SOFTWARE : XSCALE 10.90.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25175
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 7.180
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.8800
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) : 2.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 6.4.0
REMARK 200 STARTING MODEL: 1BR1
REMARK 200
REMARK 200 REMARK: PLATELET
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8K, 50 MM BICINE PH 8.2, 10% DMSO,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 36.47000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 101.08500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.47000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 101.08500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 GLN A 3
REMARK 465 LYS A 4
REMARK 465 PRO A 5
REMARK 465 LEU A 6
REMARK 465 SER A 7
REMARK 465 ASP A 8
REMARK 465 ASP A 9
REMARK 465 GLU A 10
REMARK 465 LYS A 11
REMARK 465 PHE A 12
REMARK 465 LEU A 13
REMARK 465 PHE A 14
REMARK 465 VAL A 15
REMARK 465 ASP A 16
REMARK 465 LYS A 17
REMARK 465 ASN A 18
REMARK 465 PHE A 19
REMARK 465 VAL A 20
REMARK 465 ASN A 21
REMARK 465 ASN A 22
REMARK 465 PRO A 23
REMARK 465 LEU A 24
REMARK 465 ALA A 25
REMARK 465 GLN A 26
REMARK 465 ALA A 27
REMARK 465 ASP A 28
REMARK 465 TRP A 29
REMARK 465 SER A 30
REMARK 465 ALA A 31
REMARK 465 LYS A 32
REMARK 465 HIS A 201
REMARK 465 LYS A 202
REMARK 465 GLY A 203
REMARK 465 LYS A 204
REMARK 465 ARG A 205
REMARK 465 THR A 206
REMARK 465 PRO A 207
REMARK 465 ALA A 208
REMARK 465 SER A 209
REMARK 465 LEU A 210
REMARK 465 LYS A 211
REMARK 465 VAL A 212
REMARK 465 HIS A 213
REMARK 465 LEU A 214
REMARK 465 PHE A 215
REMARK 465 GLN A 574
REMARK 465 LEU A 575
REMARK 465 LYS A 576
REMARK 465 VAL A 628
REMARK 465 ASP A 629
REMARK 465 ARG A 630
REMARK 465 ILE A 631
REMARK 465 VAL A 632
REMARK 465 GLY A 633
REMARK 465 LEU A 634
REMARK 465 ASP A 635
REMARK 465 GLN A 636
REMARK 465 MET A 637
REMARK 465 ALA A 638
REMARK 465 LYS A 639
REMARK 465 MET A 640
REMARK 465 THR A 641
REMARK 465 GLU A 642
REMARK 465 SER A 643
REMARK 465 SER A 644
REMARK 465 LEU A 645
REMARK 465 PRO A 646
REMARK 465 SER A 647
REMARK 465 ALA A 648
REMARK 465 SER A 649
REMARK 465 LYS A 650
REMARK 465 THR A 651
REMARK 465 LYS A 652
REMARK 465 LYS A 653
REMARK 465 GLY A 654
REMARK 465 MET A 655
REMARK 465 PHE A 656
REMARK 465 ARG A 788
REMARK 465 ASP A 789
REMARK 465 LEU A 790
REMARK 465 GLY A 791
REMARK 465 SER A 792
REMARK 465 ASP A 793
REMARK 465 TYR A 794
REMARK 465 LYS A 795
REMARK 465 ASP A 796
REMARK 465 ASP A 797
REMARK 465 ASP A 798
REMARK 465 ASP A 799
REMARK 465 LYS A 800
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 41 CE NZ
REMARK 470 LYS A 53 CG CD CE NZ
REMARK 470 GLN A 62 CG CD OE1 NE2
REMARK 470 LYS A 66 CG CD CE NZ
REMARK 470 LYS A 67 CD CE NZ
REMARK 470 LYS A 77 CD CE NZ
REMARK 470 LYS A 82 NZ
REMARK 470 LYS A 136 CG CD CE NZ
REMARK 470 LYS A 145 CD CE NZ
REMARK 470 LYS A 189 CD CE NZ
REMARK 470 LYS A 408 CE NZ
REMARK 470 LYS A 448 CD CE NZ
REMARK 470 LYS A 452 CG CD CE NZ
REMARK 470 THR A 453 OG1 CG2
REMARK 470 ARG A 455 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 511 CG CD OE1 OE2
REMARK 470 ASN A 533 CG OD1 ND2
REMARK 470 GLU A 543 CG CD OE1 OE2
REMARK 470 LYS A 549 CG CD CE NZ
REMARK 470 LYS A 573 CG CD CE NZ
REMARK 470 LYS A 619 CD CE NZ
REMARK 470 LYS A 626 CE NZ
REMARK 470 ARG A 731 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 732 CD OE1 NE2
REMARK 470 GLU A 735 CG CD OE1 OE2
REMARK 470 ILE A 736 CG1 CG2 CD1
REMARK 470 LYS A 744 CG CD CE NZ
REMARK 470 LYS A 758 CG CD CE NZ
REMARK 470 GLU A 787 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS A 53 78.16 -159.20
REMARK 500 GLN A 62 3.79 -61.64
REMARK 500 LEU A 271 69.13 39.69
REMARK 500 THR A 286 -164.23 -75.91
REMARK 500 ALA A 297 135.48 -37.72
REMARK 500 ASN A 364 -15.40 -153.06
REMARK 500 SER A 476 -159.46 -81.40
REMARK 500 ASP A 516 122.34 -36.41
REMARK 500 GLU A 529 -102.67 -75.41
REMARK 500 ARG A 530 105.89 30.74
REMARK 500 THR A 532 -155.85 -147.61
REMARK 500 ASN A 533 -108.11 63.45
REMARK 500 SER A 572 -174.33 -69.90
REMARK 500 THR A 673 -71.30 -58.18
REMARK 500 LYS A 691 42.80 72.84
REMARK 500 SER A 772 -28.30 -142.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1083 DISTANCE = 6.72 ANGSTROMS
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 902 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 184 OG1
REMARK 620 2 SER A 246 OG 83.4
REMARK 620 3 ADP A 904 O1B 94.4 151.3
REMARK 620 4 HOH A1004 O 76.8 71.2 80.4
REMARK 620 5 HOH A1021 O 118.1 81.7 123.4 147.6
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 52E A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BEF A 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP A 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 906
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 907
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN A 908
DBREF 5T45 A 1 800 PDB 5T45 5T45 1 800
SEQRES 1 A 800 MET ALA GLN LYS PRO LEU SER ASP ASP GLU LYS PHE LEU
SEQRES 2 A 800 PHE VAL ASP LYS ASN PHE VAL ASN ASN PRO LEU ALA GLN
SEQRES 3 A 800 ALA ASP TRP SER ALA LYS LYS LEU VAL TRP VAL PRO SER
SEQRES 4 A 800 GLU LYS HIS GLY PHE GLU ALA ALA SER ILE LYS GLU GLU
SEQRES 5 A 800 LYS GLY ASP GLU VAL THR VAL GLU LEU GLN GLU ASN GLY
SEQRES 6 A 800 LYS LYS VAL THR LEU SER LYS ASP ASP ILE GLN LYS MET
SEQRES 7 A 800 ASN PRO PRO LYS PHE SER LYS VAL GLU ASP MET ALA GLU
SEQRES 8 A 800 LEU THR CYS LEU ASN GLU ALA SER VAL LEU HIS ASN LEU
SEQRES 9 A 800 ARG GLU ARG TYR PHE SER GLY LEU ILE TYR THR TYR SER
SEQRES 10 A 800 GLY LEU PHE CYS VAL VAL ILE ASN PRO TYR LYS GLN LEU
SEQRES 11 A 800 PRO ILE TYR SER GLU LYS ILE ILE ASP MET TYR LYS GLY
SEQRES 12 A 800 LYS LYS ARG HIS GLU MET PRO PRO HIS ILE TYR ALA ILE
SEQRES 13 A 800 ALA ASP THR ALA TYR ARG SER MET LEU GLN ASP ARG GLU
SEQRES 14 A 800 ASP GLN SER ILE LEU CYS THR GLY GLU SER GLY ALA GLY
SEQRES 15 A 800 LYS THR GLU ASN THR LYS LYS VAL ILE GLN TYR LEU ALA
SEQRES 16 A 800 VAL VAL ALA SER SER HIS LYS GLY LYS ARG THR PRO ALA
SEQRES 17 A 800 SER LEU LYS VAL HIS LEU PHE PRO TYR GLY GLU LEU GLU
SEQRES 18 A 800 LYS GLN LEU LEU GLN ALA ASN PRO ILE LEU GLU ALA PHE
SEQRES 19 A 800 GLY ASN ALA LYS THR VAL LYS ASN ASP ASN SER SER ARG
SEQRES 20 A 800 PHE GLY LYS PHE ILE ARG ILE ASN PHE ASP VAL THR GLY
SEQRES 21 A 800 TYR ILE VAL GLY ALA ASN ILE GLU THR TYR LEU LEU GLU
SEQRES 22 A 800 LYS SER ARG ALA ILE ARG GLN ALA LYS ASP GLU ARG THR
SEQRES 23 A 800 PHE HIS ILE PHE TYR TYR LEU ILE ALA GLY ALA SER GLU
SEQRES 24 A 800 GLN MET ARG ASN ASP LEU LEU LEU GLU GLY PHE ASN ASN
SEQRES 25 A 800 TYR THR PHE LEU SER ASN GLY HIS VAL PRO ILE PRO ALA
SEQRES 26 A 800 GLN GLN ASP ASP GLU MET PHE GLN GLU THR LEU GLU ALA
SEQRES 27 A 800 MET THR ILE MET GLY PHE THR GLU GLU GLU GLN THR SER
SEQRES 28 A 800 ILE LEU ARG VAL VAL SER SER VAL LEU GLN LEU GLY ASN
SEQRES 29 A 800 ILE VAL PHE LYS LYS GLU ARG ASN THR ASP GLN ALA SER
SEQRES 30 A 800 MET PRO ASP ASN THR ALA ALA GLN LYS VAL CYS HIS LEU
SEQRES 31 A 800 MET GLY ILE ASN VAL THR ASP PHE THR ARG SER ILE LEU
SEQRES 32 A 800 THR PRO ARG ILE LYS VAL GLY ARG ASP VAL VAL GLN LYS
SEQRES 33 A 800 ALA GLN THR LYS GLU GLN ALA ASP PHE ALA ILE GLU ALA
SEQRES 34 A 800 LEU ALA LYS ALA LYS PHE GLU ARG LEU PHE ARG TRP ILE
SEQRES 35 A 800 LEU THR ARG VAL ASN LYS ALA LEU ASP LYS THR LYS ARG
SEQRES 36 A 800 GLN GLY ALA SER PHE LEU GLY ILE LEU ASP ILE ALA GLY
SEQRES 37 A 800 PHE GLU ILE PHE GLU ILE ASN SER PHE GLU GLN LEU CYS
SEQRES 38 A 800 ILE ASN TYR THR ASN GLU LYS LEU GLN GLN LEU PHE ASN
SEQRES 39 A 800 HIS THR MET PHE ILE LEU GLU GLN GLU GLU TYR GLN ARG
SEQRES 40 A 800 GLU GLY ILE GLU TRP ASN PHE ILE ASP PHE GLY LEU ASP
SEQRES 41 A 800 LEU GLN PRO CYS ILE GLU LEU ILE GLU ARG PRO THR ASN
SEQRES 42 A 800 PRO PRO GLY VAL LEU ALA LEU LEU ASP GLU GLU CYS TRP
SEQRES 43 A 800 PHE PRO LYS ALA THR ASP THR SER PHE VAL GLU LYS LEU
SEQRES 44 A 800 ILE GLN GLU GLN GLY ASN HIS ALA LYS PHE GLN LYS SER
SEQRES 45 A 800 LYS GLN LEU LYS ASP LYS THR GLU PHE CYS ILE LEU HIS
SEQRES 46 A 800 TYR ALA GLY LYS VAL THR TYR ASN ALA SER ALA TRP LEU
SEQRES 47 A 800 THR LYS ASN MET ASP PRO LEU ASN ASP ASN VAL THR SER
SEQRES 48 A 800 LEU LEU ASN GLN SER SER ASP LYS PHE VAL ALA ASP LEU
SEQRES 49 A 800 TRP LYS ASP VAL ASP ARG ILE VAL GLY LEU ASP GLN MET
SEQRES 50 A 800 ALA LYS MET THR GLU SER SER LEU PRO SER ALA SER LYS
SEQRES 51 A 800 THR LYS LYS GLY MET PHE ARG THR VAL GLY GLN LEU TYR
SEQRES 52 A 800 LYS GLU GLN LEU THR LYS LEU MET THR THR LEU ARG ASN
SEQRES 53 A 800 THR ASN PRO ASN PHE VAL ARG CYS ILE ILE PRO ASN HIS
SEQRES 54 A 800 GLU LYS ARG ALA GLY LYS LEU ASP ALA HIS LEU VAL LEU
SEQRES 55 A 800 GLU GLN LEU ARG CYS ASN GLY VAL LEU GLU GLY ILE ARG
SEQRES 56 A 800 ILE CYS ARG GLN GLY PHE PRO ASN ARG ILE VAL PHE GLN
SEQRES 57 A 800 GLU PHE ARG GLN ARG TYR GLU ILE LEU ALA ALA ASN ALA
SEQRES 58 A 800 ILE PRO LYS GLY PHE MET ASP GLY LYS GLN ALA CYS ILE
SEQRES 59 A 800 LEU MET ILE LYS ALA LEU GLU LEU ASP PRO ASN LEU TYR
SEQRES 60 A 800 ARG ILE GLY GLN SER LYS ILE PHE PHE ARG THR GLY VAL
SEQRES 61 A 800 LEU ALA HIS LEU GLU GLU GLU ARG ASP LEU GLY SER ASP
SEQRES 62 A 800 TYR LYS ASP ASP ASP ASP LYS
HET 52E A 901 35
HET MG A 902 1
HET BEF A 903 4
HET ADP A 904 27
HET GOL A 905 6
HET GOL A 906 6
HET GOL A 907 6
HET BCN A 908 11
HETNAM 52E 4-{[(2-CHLORO-3-FLUOROBENZYL)CARBAMOYL](METHYL)AMINO}-
HETNAM 2 52E 3,4-DIDEOXY-5-O-(ISOQUINOLIN-3-YLCARBAMOYL)-D-ERYTHRO-
HETNAM 3 52E PENTITOL
HETNAM MG MAGNESIUM ION
HETNAM BEF BERYLLIUM TRIFLUORIDE ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM GOL GLYCEROL
HETNAM BCN BICINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 52E C24 H26 CL F N4 O5
FORMUL 3 MG MG 2+
FORMUL 4 BEF BE F3 1-
FORMUL 5 ADP C10 H15 N5 O10 P2
FORMUL 6 GOL 3(C3 H8 O3)
FORMUL 9 BCN C6 H13 N O4
FORMUL 10 HOH *83(H2 O)
HELIX 1 AA1 ASP A 73 ILE A 75 5 3
HELIX 2 AA2 PRO A 80 SER A 84 5 5
HELIX 3 AA3 ASP A 88 LEU A 92 5 5
HELIX 4 AA4 ASN A 96 SER A 110 1 15
HELIX 5 AA5 LEU A 130 TYR A 133 5 4
HELIX 6 AA6 SER A 134 TYR A 141 1 8
HELIX 7 AA7 HIS A 152 ARG A 168 1 17
HELIX 8 AA8 GLY A 182 ALA A 198 1 17
HELIX 9 AA9 GLY A 218 LEU A 225 1 8
HELIX 10 AB1 GLN A 226 GLY A 235 1 10
HELIX 11 AB2 GLU A 273 ILE A 278 5 6
HELIX 12 AB3 PHE A 287 ALA A 297 1 11
HELIX 13 AB4 SER A 298 LEU A 305 1 8
HELIX 14 AB5 GLY A 309 TYR A 313 5 5
HELIX 15 AB6 GLN A 327 MET A 342 1 16
HELIX 16 AB7 THR A 345 GLY A 363 1 19
HELIX 17 AB8 ASN A 381 GLY A 392 1 12
HELIX 18 AB9 ASN A 394 THR A 404 1 11
HELIX 19 AC1 THR A 419 ASP A 451 1 33
HELIX 20 AC2 SER A 476 GLY A 509 1 34
HELIX 21 AC3 ASP A 516 ASP A 520 5 5
HELIX 22 AC4 LEU A 521 GLU A 529 1 9
HELIX 23 AC5 GLY A 536 CYS A 545 1 10
HELIX 24 AC6 THR A 551 GLY A 564 1 14
HELIX 25 AC7 ALA A 596 ASP A 603 1 8
HELIX 26 AC8 ASN A 606 GLN A 615 1 10
HELIX 27 AC9 ASP A 618 TRP A 625 1 8
HELIX 28 AD1 THR A 658 ASN A 676 1 19
HELIX 29 AD2 ASP A 697 GLY A 709 1 13
HELIX 30 AD3 GLY A 709 GLY A 720 1 12
HELIX 31 AD4 PHE A 727 TYR A 734 1 8
HELIX 32 AD5 ASP A 748 LEU A 760 1 13
HELIX 33 AD6 GLY A 779 GLU A 785 1 7
SHEET 1 AA1 4 LEU A 34 SER A 39 0
SHEET 2 AA1 4 GLY A 43 LYS A 53 -1 O ALA A 47 N VAL A 35
SHEET 3 AA1 4 GLU A 56 LEU A 61 -1 O THR A 58 N GLU A 51
SHEET 4 AA1 4 LYS A 67 SER A 71 -1 O VAL A 68 N VAL A 59
SHEET 1 AA2 7 TYR A 114 TYR A 116 0
SHEET 2 AA2 7 CYS A 121 ILE A 124 -1 O VAL A 122 N THR A 115
SHEET 3 AA2 7 ASN A 678 ILE A 685 1 O ILE A 685 N VAL A 123
SHEET 4 AA2 7 GLN A 171 THR A 176 1 N LEU A 174 O ASN A 680
SHEET 5 AA2 7 SER A 459 ASP A 465 1 O GLY A 462 N GLN A 171
SHEET 6 AA2 7 GLY A 249 PHE A 256 -1 N LYS A 250 O ASP A 465
SHEET 7 AA2 7 ILE A 262 TYR A 270 -1 O ASN A 266 N ARG A 253
SHEET 1 AA3 2 ASN A 236 ALA A 237 0
SHEET 2 AA3 2 SER A 245 SER A 246 -1 O SER A 245 N ALA A 237
SHEET 1 AA4 2 LYS A 368 LYS A 369 0
SHEET 2 AA4 2 ALA A 376 SER A 377 -1 O SER A 377 N LYS A 368
SHEET 1 AA5 2 ARG A 406 LYS A 408 0
SHEET 2 AA5 2 VAL A 413 GLN A 415 -1 O VAL A 414 N ILE A 407
SHEET 1 AA6 3 PHE A 569 GLN A 570 0
SHEET 2 AA6 3 GLU A 580 HIS A 585 -1 O CYS A 582 N GLN A 570
SHEET 3 AA6 3 GLY A 588 ASN A 593 -1 O TYR A 592 N PHE A 581
SHEET 1 AA7 3 ASN A 723 VAL A 726 0
SHEET 2 AA7 3 LYS A 773 PHE A 776 -1 O ILE A 774 N ILE A 725
SHEET 3 AA7 3 TYR A 767 ILE A 769 -1 N ARG A 768 O PHE A 775
LINK OG1 THR A 184 MG MG A 902 1555 1555 1.95
LINK OG SER A 246 MG MG A 902 1555 1555 2.35
LINK MG MG A 902 O1B ADP A 904 1555 1555 1.95
LINK MG MG A 902 O HOH A1004 1555 1555 2.22
LINK MG MG A 902 O HOH A1021 1555 1555 2.82
CISPEP 1 PRO A 216 TYR A 217 0 -2.46
CISPEP 2 GLY A 410 ARG A 411 0 1.03
SITE 1 AC1 20 MET A 89 LEU A 95 SER A 117 GLY A 118
SITE 2 AC1 20 LEU A 119 PHE A 120 PHE A 493 MET A 497
SITE 3 AC1 20 GLU A 501 PHE A 517 GLY A 709 VAL A 710
SITE 4 AC1 20 GLU A 712 GLY A 713 ILE A 714 CYS A 717
SITE 5 AC1 20 PRO A 722 ARG A 724 HOH A1001 HOH A1044
SITE 1 AC2 7 THR A 184 SER A 246 ASP A 465 BEF A 903
SITE 2 AC2 7 ADP A 904 HOH A1004 HOH A1021
SITE 1 AC3 9 SER A 179 LYS A 183 ASN A 242 SER A 245
SITE 2 AC3 9 SER A 246 MG A 902 ADP A 904 HOH A1004
SITE 3 AC3 9 HOH A1061
SITE 1 AC4 18 ILE A 113 ASN A 125 PRO A 126 LYS A 128
SITE 2 AC4 18 TYR A 133 GLU A 178 SER A 179 GLY A 180
SITE 3 AC4 18 ALA A 181 GLY A 182 LYS A 183 THR A 184
SITE 4 AC4 18 GLU A 185 ASN A 242 MG A 902 BEF A 903
SITE 5 AC4 18 HOH A1004 HOH A1008
SITE 1 AC5 6 ARG A 247 PHE A 248 GLY A 249 LEU A 271
SITE 2 AC5 6 GLU A 273 ILE A 466
SITE 1 AC6 5 TYR A 161 VAL A 197 THR A 259 TYR A 261
SITE 2 AC6 5 HOH A1028
SITE 1 AC7 4 TYR A 586 ARG A 706 GLU A 712 ARG A 715
SITE 1 AC8 8 PHE A 251 GLU A 268 TYR A 270 ASN A 394
SITE 2 AC8 8 GLN A 666 LYS A 669 LEU A 670 THR A 673
CRYST1 72.940 202.170 67.020 90.00 90.00 90.00 P 21 21 2 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013710 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004946 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014921 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
