HEADER MOTOR PROTEIN/METAL-BINDING PROTEIN 16-FEB-05 2BKI
TITLE MYOSIN VI NUCLEOTIDE-FREE (MDINSERT2-IQ) CRYSTAL STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCONVENTIONAL MYOSIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DOMAIN LONG-S1, RESIDUES 1-858;
COMPND 5 SYNONYM: MYOSIN VI;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: CALMODULIN;
COMPND 9 CHAIN: B, D;
COMPND 10 SYNONYM: CAM;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 12 ORGANISM_COMMON: CHICKEN;
SOURCE 13 ORGANISM_TAXID: 9031;
SOURCE 14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 15 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS MOTOR PROTEIN-METAL-BINDING PROTEIN COMPLEX, COMPLEX (MOTOR PROTEIN-
KEYWDS 2 CALMODULIN), MYOSIN VI, REVERSE MYOSIN, CALMODULIN, IQ MOTIF, NON-
KEYWDS 3 CONVENTIONAL MYOSIN, NUCLEOTIDE-FREE CONFORMATION, MUSCLE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.MENETREY,A.BAHLOUL,C.YENGO,A.WELLS,C.MORRIS,H.L.SWEENEY,A.HOUDUSSE
REVDAT 4 13-DEC-23 2BKI 1 REMARK LINK
REVDAT 3 16-SEP-15 2BKI 1 COMPND SOURCE KEYWDS AUTHOR
REVDAT 3 2 1 JRNL REMARK VERSN DBREF
REVDAT 3 3 1 SEQADV FORMUL MASTER
REVDAT 2 24-FEB-09 2BKI 1 VERSN
REVDAT 1 07-JUN-05 2BKI 0
JRNL AUTH J.MENETREY,A.BAHLOUL,A.WELLS,C.YENGO,C.MORRIS,H.L.SWEENEY,
JRNL AUTH 2 A.HOUDUSSE
JRNL TITL THE STRUCTURE OF THE MYOSIN VI MOTOR REVEALS THE MECHANISM
JRNL TITL 2 OF DIRECTIONALITY REVERSAL
JRNL REF NATURE V. 435 779 2005
JRNL REFN ISSN 0028-0836
JRNL PMID 15944696
JRNL DOI 10.1038/NATURE03592
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 3 NUMBER OF REFLECTIONS : 36191
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) : 0.266
REMARK 3 R VALUE (WORKING SET) : 0.264
REMARK 3 FREE R VALUE : 0.304
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1948
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2389
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2930
REMARK 3 BIN FREE R VALUE SET COUNT : 118
REMARK 3 BIN FREE R VALUE : 0.3430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7991
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 9
REMARK 3 SOLVENT ATOMS : 49
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.74000
REMARK 3 B22 (A**2) : 2.65000
REMARK 3 B33 (A**2) : 0.10000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 1.125
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.430
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.339
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.988
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.860
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.809
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8138 ; 0.013 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 7293 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10997 ; 1.149 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16926 ; 2.037 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1042 ; 5.238 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1229 ; 0.064 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9247 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1662 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1835 ; 0.174 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 7914 ; 0.207 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 4801 ; 0.081 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 101 ; 0.173 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 8 ; 0.164 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 44 ; 0.226 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.202 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5197 ; 0.517 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8235 ; 0.965 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2941 ; 1.129 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2762 ; 1.987 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. CAM BOUND TO THE IQ MOTIF IS POORLY DEFINED IN THE
REMARK 3 DENSITY, ONLY POLY-ALA CHAINS HAVE BEEN MODELED FOR IT.
REMARK 4
REMARK 4 2BKI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1290023002.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.96115
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38961
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.44000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
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: PDB ENTRY 1OE9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8-10% PEG 8000, 50MM MES PH 6.7, 150MM
REMARK 280 NH4.SO4, 3% ISO-PROPANOL, 3% TERT-BUTANOL
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 52.39050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 125.08350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 52.39050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 125.08350
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D
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 MET A 826
REMARK 465 TRP A 827
REMARK 465 LEU A 828
REMARK 465 CYS A 829
REMARK 465 LYS A 830
REMARK 465 ARG A 831
REMARK 465 ARG A 832
REMARK 465 HIS A 833
REMARK 465 LYS A 834
REMARK 465 PRO A 835
REMARK 465 ARG A 836
REMARK 465 ILE A 837
REMARK 465 ASP A 838
REMARK 465 GLY A 839
REMARK 465 LEU A 840
REMARK 465 VAL A 841
REMARK 465 LYS A 842
REMARK 465 VAL A 843
REMARK 465 GLY A 844
REMARK 465 THR A 845
REMARK 465 LEU A 846
REMARK 465 LYS A 847
REMARK 465 LYS A 848
REMARK 465 ARG A 849
REMARK 465 LEU A 850
REMARK 465 ASP A 851
REMARK 465 LYS A 852
REMARK 465 PHE A 853
REMARK 465 ASN A 854
REMARK 465 GLU A 855
REMARK 465 VAL A 856
REMARK 465 VAL A 857
REMARK 465 SER A 858
REMARK 465 MET B 0
REMARK 465 ALA B 1
REMARK 465 ASP B 2
REMARK 465 LYS B 148
REMARK 465 MET D 0
REMARK 465 ALA D 1
REMARK 465 ASP D 2
REMARK 465 GLN D 3
REMARK 465 LEU D 4
REMARK 465 THR D 5
REMARK 465 SER D 17
REMARK 465 LEU D 18
REMARK 465 PHE D 19
REMARK 465 ASP D 20
REMARK 465 LYS D 21
REMARK 465 ASP D 22
REMARK 465 GLY D 23
REMARK 465 ASP D 24
REMARK 465 GLY D 25
REMARK 465 THR D 26
REMARK 465 ILE D 27
REMARK 465 THR D 28
REMARK 465 THR D 29
REMARK 465 LYS D 30
REMARK 465 GLU D 31
REMARK 465 LEU D 32
REMARK 465 GLY D 33
REMARK 465 THR D 34
REMARK 465 VAL D 35
REMARK 465 MET D 36
REMARK 465 ARG D 37
REMARK 465 SER D 38
REMARK 465 LEU D 39
REMARK 465 GLY D 40
REMARK 465 GLN D 41
REMARK 465 ASN D 42
REMARK 465 ASN D 53
REMARK 465 GLU D 54
REMARK 465 VAL D 55
REMARK 465 ASP D 56
REMARK 465 ALA D 57
REMARK 465 ASP D 58
REMARK 465 GLY D 59
REMARK 465 ASN D 60
REMARK 465 GLY D 61
REMARK 465 THR D 62
REMARK 465 ILE D 63
REMARK 465 ASP D 64
REMARK 465 PHE D 65
REMARK 465 PRO D 66
REMARK 465 GLU D 67
REMARK 465 PHE D 68
REMARK 465 ARG D 126
REMARK 465 GLU D 127
REMARK 465 ALA D 128
REMARK 465 ASP D 129
REMARK 465 ILE D 130
REMARK 465 ASP D 131
REMARK 465 GLY D 132
REMARK 465 ASP D 133
REMARK 465 GLY D 134
REMARK 465 GLN D 135
REMARK 465 VAL D 136
REMARK 465 ASN D 137
REMARK 465 TYR D 138
REMARK 465 GLU D 139
REMARK 465 GLU D 140
REMARK 465 PHE D 141
REMARK 465 VAL D 142
REMARK 465 GLN D 143
REMARK 465 MET D 144
REMARK 465 MET D 145
REMARK 465 THR D 146
REMARK 465 ALA D 147
REMARK 465 LYS D 148
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 GLU A 2 CG CD OE1 OE2
REMARK 470 ASP A 3 CG OD1 OD2
REMARK 470 LYS A 105 CG CD CE NZ
REMARK 470 LYS A 162 CG CD CE NZ
REMARK 470 ILE A 178 CG1 CG2 CD1
REMARK 470 GLU A 414 CG CD OE1 OE2
REMARK 470 SER A 624 OG
REMARK 470 THR A 625 OG1 CG2
REMARK 470 ASN A 626 CG OD1 ND2
REMARK 470 ASN A 627 CG OD1 ND2
REMARK 470 ASN A 628 CG OD1 ND2
REMARK 470 LYS A 629 CG CD CE NZ
REMARK 470 ASP A 630 CG OD1 OD2
REMARK 470 THR A 631 OG1 CG2
REMARK 470 LYS A 632 CG CD CE NZ
REMARK 470 GLN A 633 CG CD OE1 NE2
REMARK 470 LYS A 634 CG CD CE NZ
REMARK 470 LYS A 637 CG CD CE NZ
REMARK 470 LEU A 638 CG CD1 CD2
REMARK 470 SER A 639 OG
REMARK 470 PHE A 640 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE A 789 CG1 CG2 CD1
REMARK 470 LYS A 809 CG CD CE NZ
REMARK 470 LYS A 811 CG CD CE NZ
REMARK 470 CYS A 817 SG
REMARK 470 ILE A 818 CG1 CG2 CD1
REMARK 470 LYS A 819 CG CD CE NZ
REMARK 470 LYS A 822 CG CD CE NZ
REMARK 470 THR A 823 OG1 CG2
REMARK 470 ARG A 825 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 3 CG CD OE1 NE2
REMARK 470 GLU B 7 CG CD OE1 OE2
REMARK 470 LYS B 30 CG CD CE NZ
REMARK 470 ARG B 74 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 75 CG CD CE NZ
REMARK 470 LYS B 77 CG CD CE NZ
REMARK 470 GLU B 83 CG CD OE1 OE2
REMARK 470 VAL B 91 CG1 CG2
REMARK 470 LYS B 94 CG CD CE NZ
REMARK 470 ARG B 106 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 115 CG CD CE NZ
REMARK 470 ASP B 118 CG OD1 OD2
REMARK 470 GLU B 119 CG CD OE1 OE2
REMARK 470 ILE B 125 CG1 CG2 CD1
REMARK 470 GLN B 135 CG CD OE1 NE2
REMARK 470 GLU D 6 CG CD OE1 OE2
REMARK 470 GLU D 7 CG CD OE1 OE2
REMARK 470 GLN D 8 CG CD OE1 NE2
REMARK 470 ILE D 9 CG1 CG2 CD1
REMARK 470 GLU D 11 CG CD OE1 OE2
REMARK 470 PHE D 12 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS D 13 CG CD CE NZ
REMARK 470 GLU D 14 CG CD OE1 OE2
REMARK 470 PHE D 16 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PRO D 43 CG CD
REMARK 470 THR D 44 OG1 CG2
REMARK 470 GLU D 45 CG CD OE1 OE2
REMARK 470 GLU D 47 CG CD OE1 OE2
REMARK 470 LEU D 48 CG CD1 CD2
REMARK 470 GLN D 49 CG CD OE1 NE2
REMARK 470 ASP D 50 CG OD1 OD2
REMARK 470 MET D 51 CG SD CE
REMARK 470 ILE D 52 CG1 CG2 CD1
REMARK 470 LEU D 69 CG CD1 CD2
REMARK 470 THR D 70 OG1 CG2
REMARK 470 MET D 71 CG SD CE
REMARK 470 MET D 72 CG SD CE
REMARK 470 ARG D 74 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 75 CG CD CE NZ
REMARK 470 MET D 76 CG SD CE
REMARK 470 LYS D 77 CG CD CE NZ
REMARK 470 ASP D 78 CG OD1 OD2
REMARK 470 THR D 79 OG1 CG2
REMARK 470 ASP D 80 CG OD1 OD2
REMARK 470 SER D 81 OG
REMARK 470 GLU D 82 CG CD OE1 OE2
REMARK 470 GLU D 83 CG CD OE1 OE2
REMARK 470 GLU D 84 CG CD OE1 OE2
REMARK 470 ILE D 85 CG1 CG2 CD1
REMARK 470 ARG D 86 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 87 CG CD OE1 OE2
REMARK 470 PHE D 89 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG D 90 CG CD NE CZ NH1 NH2
REMARK 470 VAL D 91 CG1 CG2
REMARK 470 PHE D 92 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP D 93 CG OD1 OD2
REMARK 470 LYS D 94 CG CD CE NZ
REMARK 470 ASP D 95 CG OD1 OD2
REMARK 470 ASN D 97 CG OD1 ND2
REMARK 470 TYR D 99 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE D 100 CG1 CG2 CD1
REMARK 470 SER D 101 OG
REMARK 470 GLU D 104 CG CD OE1 OE2
REMARK 470 LEU D 105 CG CD1 CD2
REMARK 470 ARG D 106 CG CD NE CZ NH1 NH2
REMARK 470 HIS D 107 CG ND1 CD2 CE1 NE2
REMARK 470 VAL D 108 CG1 CG2
REMARK 470 MET D 109 CG SD CE
REMARK 470 THR D 110 OG1 CG2
REMARK 470 ASN D 111 CG OD1 ND2
REMARK 470 LEU D 112 CG CD1 CD2
REMARK 470 GLU D 114 CG CD OE1 OE2
REMARK 470 LYS D 115 CG CD CE NZ
REMARK 470 LEU D 116 CG CD1 CD2
REMARK 470 THR D 117 OG1 CG2
REMARK 470 ASP D 118 CG OD1 OD2
REMARK 470 GLU D 119 CG CD OE1 OE2
REMARK 470 GLU D 120 CG CD OE1 OE2
REMARK 470 VAL D 121 CG1 CG2
REMARK 470 ASP D 122 CG OD1 OD2
REMARK 470 GLU D 123 CG CD OE1 OE2
REMARK 470 MET D 124 CG SD CE
REMARK 470 ILE D 125 CG1 CG2 CD1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU B 120 CD GLU B 120 OE2 0.067
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 23 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 54 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP A 269 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 308 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 336 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 421 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP A 433 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP A 540 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 573 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 574 CB - CG - OD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP A 599 CB - CG - OD2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ASP A 656 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 724 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 730 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP B 133 CB - CG - OD2 ANGL. DEV. = 5.6 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 ASP A 3 73.22 170.25
REMARK 500 LYS A 37 27.13 47.41
REMARK 500 ALA A 91 -121.27 62.19
REMARK 500 LYS A 105 -8.66 70.41
REMARK 500 GLU A 152 -168.57 -77.62
REMARK 500 GLN A 176 104.31 66.10
REMARK 500 GLU A 241 -5.19 69.86
REMARK 500 ASN A 244 -176.91 -66.70
REMARK 500 LEU A 310 -31.05 -136.48
REMARK 500 ASN A 504 103.50 -2.25
REMARK 500 LEU A 522 -27.14 80.84
REMARK 500 ASN A 533 0.51 -68.15
REMARK 500 LYS A 552 -71.07 -69.42
REMARK 500 ASP A 553 65.29 -113.45
REMARK 500 LYS A 562 32.14 -88.28
REMARK 500 ASP A 599 35.31 -146.79
REMARK 500 GLU A 611 55.59 -107.01
REMARK 500 THR A 631 -86.71 -102.81
REMARK 500 LYS A 632 -59.84 60.01
REMARK 500 ASN B 42 71.63 -154.62
REMARK 500 ALA B 46 -47.06 -176.65
REMARK 500 ASP B 56 97.85 -62.05
REMARK 500 ASN B 60 -36.67 -176.64
REMARK 500 GLU D 47 33.20 -91.95
REMARK 500 MET D 51 -74.43 -61.65
REMARK 500 ASP D 78 60.52 -104.12
REMARK 500 SER D 81 -178.30 -69.21
REMARK 500 ASP D 95 -86.30 -134.35
REMARK 500 ASN D 97 55.50 -157.13
REMARK 500 ILE D 100 46.99 -154.13
REMARK 500 SER D 101 174.08 60.83
REMARK 500 ARG D 106 -44.60 -175.03
REMARK 500 MET D 124 -63.15 -157.51
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 CA B1148 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 20 OD1
REMARK 620 2 ASP B 22 OD1 83.0
REMARK 620 3 ASP B 24 OD1 80.0 64.7
REMARK 620 4 THR B 26 O 75.0 146.3 86.3
REMARK 620 5 GLU B 31 OE1 148.2 124.7 123.6 84.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1149 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 56 OD2
REMARK 620 2 ASN B 60 OD1 59.5
REMARK 620 3 THR B 62 O 90.6 89.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1150 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 93 OD1
REMARK 620 2 ASP B 95 OD1 78.3
REMARK 620 3 ASN B 97 OD1 115.6 84.4
REMARK 620 4 ASN B 97 ND2 109.1 46.0 40.4
REMARK 620 5 TYR B 99 O 79.6 157.4 100.8 140.8
REMARK 620 6 GLU B 104 OE2 81.4 104.5 162.4 141.2 77.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1151 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 129 OD1
REMARK 620 2 ASP B 131 OD2 141.4
REMARK 620 3 ASP B 131 OD1 106.9 39.7
REMARK 620 4 ASP B 133 OD1 112.6 68.3 54.9
REMARK 620 5 GLN B 135 O 68.8 149.7 152.0 100.1
REMARK 620 6 GLU B 140 OE2 114.8 53.9 80.8 122.1 126.8
REMARK 620 7 GLU B 140 OE1 97.8 91.4 122.1 149.2 85.7 41.4
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1826
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1148
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1149
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1151
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2BKH RELATED DB: PDB
REMARK 900 MYOSIN VI NUCLEOTIDE-FREE (MDINSERT2) CRYSTAL STRUCTURE
REMARK 900 RELATED ID: 1AHR RELATED DB: PDB
REMARK 900 CALMODULIN MUTANT WITH A TWO RESIDUE DELETION IN THE CENTRAL HELIX
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE AUTHORS STATE THAT THE ORIGINAL SEQUENCE (UNIPROT
REMARK 999 Q29122) OF MYOSIN VI FROM PIG WAS MOST LIKELY
REMARK 999 INCORRECT BECAUSE THE CHANGES THAT ARE IN THEIR CLONE
REMARK 999 (LYS DELETION AND THE 6 MUTATIONS) ARE CONSERVED ACROSS
REMARK 999 THE MYOSIN VI FAMILY.
DBREF 2BKI A 1 858 UNP Q29122 Q29122_PIG 1 858
DBREF 2BKI B 0 0 PDB 2BKI 2BKI 0 0
DBREF 2BKI B 1 148 UNP P62149 CALM_CHICK 1 148
DBREF 2BKI D 0 0 PDB 2BKI 2BKI 0 0
DBREF 2BKI D 1 148 UNP P62149 CALM_CHICK 1 148
SEQRES 1 A 858 MET GLU ASP GLY LYS PRO VAL TRP ALA PRO HIS PRO THR
SEQRES 2 A 858 ASP GLY PHE GLN VAL GLY ASN ILE VAL ASP ILE GLY PRO
SEQRES 3 A 858 ASP SER LEU THR ILE GLU PRO LEU ASN GLN LYS GLY LYS
SEQRES 4 A 858 THR PHE LEU ALA LEU ILE ASN GLN VAL PHE PRO ALA GLU
SEQRES 5 A 858 GLU ASP SER LYS LYS ASP VAL GLU ASP ASN CYS SER LEU
SEQRES 6 A 858 MET TYR LEU ASN GLU ALA THR LEU LEU HIS ASN ILE LYS
SEQRES 7 A 858 VAL ARG TYR SER LYS ASP ARG ILE TYR THR TYR VAL ALA
SEQRES 8 A 858 ASN ILE LEU ILE ALA VAL ASN PRO TYR PHE ASP ILE PRO
SEQRES 9 A 858 LYS ILE TYR SER SER GLU THR ILE LYS SER TYR GLN GLY
SEQRES 10 A 858 LYS SER LEU GLY THR MET PRO PRO HIS VAL PHE ALA ILE
SEQRES 11 A 858 ALA ASP LYS ALA PHE ARG ASP MET LYS VAL LEU LYS LEU
SEQRES 12 A 858 SER GLN SER ILE ILE VAL SER GLY GLU SER GLY ALA GLY
SEQRES 13 A 858 LYS THR GLU ASN THR LYS PHE VAL LEU ARG TYR LEU THR
SEQRES 14 A 858 GLU SER TYR GLY THR GLY GLN ASP ILE ASP ASP ARG ILE
SEQRES 15 A 858 VAL GLU ALA ASN PRO LEU LEU GLU ALA PHE GLY ASN ALA
SEQRES 16 A 858 LYS THR VAL ARG ASN ASN ASN SER SER ARG PHE GLY LYS
SEQRES 17 A 858 PHE VAL GLU ILE HIS PHE ASN GLU LYS SER SER VAL VAL
SEQRES 18 A 858 GLY GLY PHE VAL SER HIS TYR LEU LEU GLU LYS SER ARG
SEQRES 19 A 858 ILE CYS VAL GLN GLY LYS GLU GLU ARG ASN TYR HIS ILE
SEQRES 20 A 858 PHE TYR ARG LEU CYS ALA GLY ALA SER GLU ASP ILE ARG
SEQRES 21 A 858 GLU ARG LEU HIS LEU SER SER PRO ASP ASN PHE ARG TYR
SEQRES 22 A 858 LEU ASN ARG GLY CYS THR ARG TYR PHE ALA ASN LYS GLU
SEQRES 23 A 858 THR ASP LYS GLN ILE LEU GLN ASN ARG LYS SER PRO GLU
SEQRES 24 A 858 TYR LEU LYS ALA GLY SER LEU LYS ASP PRO LEU LEU ASP
SEQRES 25 A 858 ASP HIS GLY ASP PHE ILE ARG MET CYS THR ALA MET LYS
SEQRES 26 A 858 LYS ILE GLY LEU ASP ASP GLU GLU LYS LEU ASP LEU PHE
SEQRES 27 A 858 ARG VAL VAL ALA GLY VAL LEU HIS LEU GLY ASN ILE ASP
SEQRES 28 A 858 PHE GLU GLU ALA GLY SER THR SER GLY GLY CYS ASN LEU
SEQRES 29 A 858 LYS ASN LYS SER THR GLN ALA LEU GLU TYR CYS ALA GLU
SEQRES 30 A 858 LEU LEU GLY LEU ASP GLN ASP ASP LEU ARG VAL SER LEU
SEQRES 31 A 858 THR THR ARG VAL MET LEU THR THR ALA GLY GLY ALA LYS
SEQRES 32 A 858 GLY THR VAL ILE LYS VAL PRO LEU LYS VAL GLU GLN ALA
SEQRES 33 A 858 ASN ASN ALA ARG ASP ALA LEU ALA LYS THR VAL TYR SER
SEQRES 34 A 858 HIS LEU PHE ASP HIS VAL VAL ASN ARG VAL ASN GLN CYS
SEQRES 35 A 858 PHE PRO PHE GLU THR SER SER TYR PHE ILE GLY VAL LEU
SEQRES 36 A 858 ASP ILE ALA GLY PHE GLU TYR PHE GLU HIS ASN SER PHE
SEQRES 37 A 858 GLU GLN PHE CYS ILE ASN TYR CYS ASN GLU LYS LEU GLN
SEQRES 38 A 858 GLN PHE PHE ASN GLU ARG ILE LEU LYS GLU GLU GLN GLU
SEQRES 39 A 858 LEU TYR GLN LYS GLU GLY LEU GLY VAL ASN GLU VAL HIS
SEQRES 40 A 858 TYR VAL ASP ASN GLN ASP CYS ILE ASP LEU ILE GLU ALA
SEQRES 41 A 858 ARG LEU VAL GLY ILE LEU ASP ILE LEU ASP GLU GLU ASN
SEQRES 42 A 858 ARG LEU PRO GLN PRO SER ASP GLN HIS PHE THR SER ALA
SEQRES 43 A 858 VAL HIS GLN LYS HIS LYS ASP HIS PHE ARG LEU SER ILE
SEQRES 44 A 858 PRO ARG LYS SER LYS LEU ALA ILE HIS ARG ASN ILE ARG
SEQRES 45 A 858 ASP ASP GLU GLY PHE ILE ILE ARG HIS PHE ALA GLY ALA
SEQRES 46 A 858 VAL CYS TYR GLU THR THR GLN PHE VAL GLU LYS ASN ASN
SEQRES 47 A 858 ASP ALA LEU HIS MET SER LEU GLU SER LEU ILE CYS GLU
SEQRES 48 A 858 SER ARG ASP LYS PHE ILE ARG GLU LEU PHE GLU SER SER
SEQRES 49 A 858 THR ASN ASN ASN LYS ASP THR LYS GLN LYS ALA GLY LYS
SEQRES 50 A 858 LEU SER PHE ILE SER VAL GLY ASN LYS PHE LYS THR GLN
SEQRES 51 A 858 LEU ASN LEU LEU LEU ASP LYS LEU ARG SER THR GLY ALA
SEQRES 52 A 858 SER PHE ILE ARG CYS ILE LYS PRO ASN LEU LYS MET THR
SEQRES 53 A 858 SER HIS HIS PHE GLU GLY ALA GLN ILE LEU SER GLN LEU
SEQRES 54 A 858 GLN CYS SER GLY MET VAL SER VAL LEU ASP LEU MET GLN
SEQRES 55 A 858 GLY GLY PHE PRO SER ARG ALA SER PHE HIS GLU LEU TYR
SEQRES 56 A 858 ASN MET TYR LYS LYS TYR MET PRO ASP LYS LEU ALA ARG
SEQRES 57 A 858 LEU ASP PRO ARG LEU PHE CYS LYS ALA LEU PHE LYS ALA
SEQRES 58 A 858 LEU GLY LEU ASN GLU ILE ASP TYR LYS PHE GLY LEU THR
SEQRES 59 A 858 LYS VAL PHE PHE ARG PRO GLY LYS PHE ALA GLU PHE ASP
SEQRES 60 A 858 GLN ILE MET LYS SER ASP PRO ASP HIS LEU ALA GLU LEU
SEQRES 61 A 858 VAL LYS ARG VAL ASN HIS TRP LEU ILE CYS SER ARG TRP
SEQRES 62 A 858 LYS LYS VAL GLN TRP CYS SER LEU SER VAL ILE LYS LEU
SEQRES 63 A 858 LYS ASN LYS ILE LYS TYR ARG ALA GLU ALA CYS ILE LYS
SEQRES 64 A 858 MET GLN LYS THR ILE ARG MET TRP LEU CYS LYS ARG ARG
SEQRES 65 A 858 HIS LYS PRO ARG ILE ASP GLY LEU VAL LYS VAL GLY THR
SEQRES 66 A 858 LEU LYS LYS ARG LEU ASP LYS PHE ASN GLU VAL VAL SER
SEQRES 1 B 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 B 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 B 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 B 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 B 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 B 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 B 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 B 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 B 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 B 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 B 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 B 149 GLN MET MET THR ALA LYS
SEQRES 1 D 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 D 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 D 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 D 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 D 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 D 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 D 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 D 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 D 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 D 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 D 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 D 149 GLN MET MET THR ALA LYS
HET SO4 A1826 5
HET CA B1148 1
HET CA B1149 1
HET CA B1150 1
HET CA B1151 1
HETNAM SO4 SULFATE ION
HETNAM CA CALCIUM ION
FORMUL 4 SO4 O4 S 2-
FORMUL 5 CA 4(CA 2+)
FORMUL 9 HOH *49(H2 O)
HELIX 1 1 ASN A 46 VAL A 48 5 3
HELIX 2 2 ASN A 62 LEU A 65 5 4
HELIX 3 3 ASN A 69 SER A 82 1 14
HELIX 4 4 SER A 108 GLN A 116 1 9
HELIX 5 5 HIS A 126 LEU A 141 1 16
HELIX 6 6 GLY A 156 GLY A 173 1 18
HELIX 7 7 ASP A 177 ALA A 185 1 9
HELIX 8 8 ALA A 185 GLY A 193 1 9
HELIX 9 9 LYS A 232 CYS A 236 5 5
HELIX 10 10 TYR A 245 ALA A 255 1 11
HELIX 11 11 SER A 256 LEU A 263 1 8
HELIX 12 12 SER A 267 ASN A 270 5 4
HELIX 13 13 PHE A 271 ARG A 276 1 6
HELIX 14 14 ASN A 284 ILE A 291 1 8
HELIX 15 15 LEU A 292 LYS A 296 5 5
HELIX 16 16 SER A 297 ALA A 303 1 7
HELIX 17 17 ASP A 312 GLY A 328 1 17
HELIX 18 18 ASP A 330 ILE A 350 1 21
HELIX 19 19 SER A 368 LEU A 379 1 12
HELIX 20 20 ASP A 382 LEU A 390 1 9
HELIX 21 21 LYS A 412 GLN A 441 1 30
HELIX 22 22 SER A 467 GLU A 499 1 33
HELIX 23 23 ASN A 511 ALA A 520 1 10
HELIX 24 24 GLY A 524 ASN A 533 1 10
HELIX 25 25 SER A 539 HIS A 551 1 13
HELIX 26 26 ILE A 559 SER A 563 5 5
HELIX 27 27 GLN A 592 ASN A 597 1 6
HELIX 28 28 HIS A 602 GLU A 611 1 10
HELIX 29 29 ASP A 614 PHE A 621 1 8
HELIX 30 30 GLU A 622 LYS A 629 1 8
HELIX 31 31 LYS A 632 LEU A 638 1 7
HELIX 32 32 SER A 642 SER A 660 1 19
HELIX 33 33 GLU A 681 SER A 692 1 12
HELIX 34 34 GLY A 693 GLY A 703 1 11
HELIX 35 35 PHE A 711 LYS A 719 1 9
HELIX 36 36 LYS A 720 MET A 722 5 3
HELIX 37 37 PRO A 723 LEU A 729 1 7
HELIX 38 38 ASP A 730 GLY A 743 1 14
HELIX 39 39 LYS A 762 ASP A 773 1 12
HELIX 40 40 ASP A 773 ARG A 783 1 11
HELIX 41 41 VAL A 784 CYS A 817 1 34
HELIX 42 42 THR B 5 ASP B 20 1 16
HELIX 43 43 THR B 28 LEU B 39 1 12
HELIX 44 44 ALA B 46 ASP B 56 1 11
HELIX 45 45 ASP B 64 ALA B 73 1 10
HELIX 46 46 THR B 79 ASP B 93 1 15
HELIX 47 47 SER B 101 GLY B 113 1 13
HELIX 48 48 THR B 117 ASP B 129 1 13
HELIX 49 49 TYR B 138 ALA B 147 1 10
HELIX 50 50 GLU D 6 PHE D 16 1 11
HELIX 51 51 GLU D 45 GLN D 49 5 5
HELIX 52 52 THR D 70 ASP D 78 1 9
HELIX 53 53 SER D 81 ARG D 90 1 10
HELIX 54 54 ARG D 106 LEU D 112 1 7
HELIX 55 55 THR D 117 GLU D 123 1 7
SHEET 1 AA 5 PHE A 41 LEU A 44 0
SHEET 2 AA 5 SER A 28 PRO A 33 -1 O LEU A 29 N ALA A 43
SHEET 3 AA 5 GLY A 15 ASP A 23 -1 O ASN A 20 N GLU A 32
SHEET 4 AA 5 VAL A 7 HIS A 11 -1 O VAL A 7 N GLY A 19
SHEET 5 AA 5 PHE A 49 PRO A 50 -1 O PHE A 49 N TRP A 8
SHEET 1 AB 7 TYR A 87 VAL A 90 0
SHEET 2 AB 7 ILE A 93 VAL A 97 -1 O ILE A 93 N VAL A 90
SHEET 3 AB 7 GLY A 662 ILE A 669 1 O PHE A 665 N LEU A 94
SHEET 4 AB 7 GLN A 145 SER A 150 1 O SER A 146 N SER A 664
SHEET 5 AB 7 TYR A 450 ASP A 456 1 O PHE A 451 N GLN A 145
SHEET 6 AB 7 GLY A 207 PHE A 214 -1 O LYS A 208 N ASP A 456
SHEET 7 AB 7 VAL A 220 TYR A 228 -1 N VAL A 221 O HIS A 213
SHEET 1 AC 2 ASN A 194 ALA A 195 0
SHEET 2 AC 2 SER A 203 SER A 204 -1 O SER A 203 N ALA A 195
SHEET 1 AD 2 PHE A 352 GLU A 354 0
SHEET 2 AD 2 CYS A 362 LEU A 364 -1 O ASN A 363 N GLU A 353
SHEET 1 AE 2 THR A 392 LEU A 396 0
SHEET 2 AE 2 VAL A 406 PRO A 410 -1 O ILE A 407 N MET A 395
SHEET 1 AF 3 LEU A 557 SER A 558 0
SHEET 2 AF 3 GLY A 576 ARG A 580 -1 O ILE A 578 N SER A 558
SHEET 3 AF 3 ALA A 585 GLU A 589 -1 O VAL A 586 N ILE A 579
SHEET 1 AG 3 SER A 707 SER A 710 0
SHEET 2 AG 3 LYS A 755 PHE A 758 -1 O VAL A 756 N ALA A 709
SHEET 3 AG 3 TYR A 749 PHE A 751 -1 O LYS A 750 N PHE A 757
SHEET 1 BA 2 TYR B 99 ILE B 100 0
SHEET 2 BA 2 VAL B 136 ASN B 137 -1 O VAL B 136 N ILE B 100
LINK OD1 ASP B 20 CA CA B1148 1555 1555 2.61
LINK OD1 ASP B 22 CA CA B1148 1555 1555 2.47
LINK OD1 ASP B 24 CA CA B1148 1555 1555 2.46
LINK O THR B 26 CA CA B1148 1555 1555 2.36
LINK OE1 GLU B 31 CA CA B1148 1555 1555 3.32
LINK OD2 ASP B 56 CA CA B1149 1555 1555 2.88
LINK OD1 ASN B 60 CA CA B1149 1555 1555 3.24
LINK O THR B 62 CA CA B1149 1555 1555 2.60
LINK OD1 ASP B 93 CA CA B1150 1555 1555 2.54
LINK OD1 ASP B 95 CA CA B1150 1555 1555 3.16
LINK OD1 ASN B 97 CA CA B1150 1555 1555 3.10
LINK ND2 ASN B 97 CA CA B1150 1555 1555 3.36
LINK O TYR B 99 CA CA B1150 1555 1555 2.22
LINK OE2 GLU B 104 CA CA B1150 1555 1555 2.48
LINK OD1 ASP B 129 CA CA B1151 1555 1555 2.39
LINK OD2 ASP B 131 CA CA B1151 1555 1555 3.31
LINK OD1 ASP B 131 CA CA B1151 1555 1555 2.96
LINK OD1 ASP B 133 CA CA B1151 1555 1555 3.02
LINK O GLN B 135 CA CA B1151 1555 1555 2.37
LINK OE2 GLU B 140 CA CA B1151 1555 1555 3.32
LINK OE1 GLU B 140 CA CA B1151 1555 1555 2.86
SITE 1 AC1 6 GLU A 152 GLY A 154 ALA A 155 GLY A 156
SITE 2 AC1 6 LYS A 157 THR A 158
SITE 1 AC2 5 ASP B 20 ASP B 22 ASP B 24 THR B 26
SITE 2 AC2 5 GLU B 31
SITE 1 AC3 4 ASP B 56 ASN B 60 THR B 62 GLU B 67
SITE 1 AC4 5 ASP B 93 ASP B 95 ASN B 97 TYR B 99
SITE 2 AC4 5 GLU B 104
SITE 1 AC5 5 ASP B 129 ASP B 131 ASP B 133 GLN B 135
SITE 2 AC5 5 GLU B 140
CRYST1 104.781 250.167 67.274 90.00 90.00 90.00 P 21 21 2 8
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 0.009544 0.000000 0.000000 0.00000
SCALE2 0.000000 0.003997 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014865 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
