HEADER CONTRACTILE PROTEIN/METAL BINDING 07-JUL-06 2IX7
TITLE STRUCTURE OF APO-CALMODULIN BOUND TO UNCONVENTIONAL MYOSIN V
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 2-146;
COMPND 5 SYNONYM: CAM;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: APO-CALMODULIN;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: MYOSIN-5A;
COMPND 10 CHAIN: C;
COMPND 11 FRAGMENT: RESIDUES 763-820;
COMPND 12 SYNONYM: MYOSIN VA, DILUTE MYOSIN HEAVY CHAIN, NON-MUSCLE;
COMPND 13 ENGINEERED: YES;
COMPND 14 OTHER_DETAILS: IQ MOTIFS
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGP1-2;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 12 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 13 ORGANISM_TAXID: 10090;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS CONTRACTILE PROTEIN/METAL BINDING, ACTIN-BINDING, UBL CONJUGATION,
KEYWDS 2 CA2+ REGULATION, MYOSIN, CALCIUM, IQ MOTIF, CALMODULIN, ACETYLATION,
KEYWDS 3 NUCLEOTIDE- BINDING, CONTRACTILE PROTEIN, COMPLEX, PHOSPHORYLATION,
KEYWDS 4 CALMODULIN-BINDING, METAL BINDING, METHYLATION, COILED COIL, ATP-
KEYWDS 5 BINDING, MOTOR PROTEIN, CONTRACTILE PROTEIN-METAL BINDING COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.HOUDUSSE,J.F.GAUCHER,S.MUI,E.KREMENTSOVA,K.M.TRYBUS,C.COHEN
REVDAT 7 13-DEC-23 2IX7 1 REMARK
REVDAT 6 08-NOV-23 2IX7 1 REMARK SSBOND LINK
REVDAT 5 27-FEB-19 2IX7 1 REMARK LINK
REVDAT 4 04-DEC-13 2IX7 1 SOURCE REMARK VERSN FORMUL
REVDAT 3 24-FEB-09 2IX7 1 VERSN
REVDAT 2 02-JAN-07 2IX7 1 JRNL
REVDAT 1 13-DEC-06 2IX7 0
JRNL AUTH A.HOUDUSSE,J.F.GAUCHER,E.KREMENTSOVA,S.MUI,K.M.TRYBUS,
JRNL AUTH 2 C.COHEN
JRNL TITL CRYSTAL STRUCTURE OF APO-CALMODULIN BOUND TO THE FIRST TWO
JRNL TITL 2 IQ MOTIFS OF MYOSIN V REVEALS ESSENTIAL RECOGNITION
JRNL TITL 3 FEATURES.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 103 19326 2006
JRNL REFN ISSN 0027-8424
JRNL PMID 17151196
JRNL DOI 10.1073/PNAS.0609436103
REMARK 2
REMARK 2 RESOLUTION. 2.50 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3356211.510
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 25977
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) : 0.216
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2570
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3860
REMARK 3 BIN R VALUE (WORKING SET) : 0.2700
REMARK 3 BIN FREE R VALUE : 0.3130
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 430
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.015
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2759
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 144
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 48.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.34000
REMARK 3 B22 (A**2) : 5.34000
REMARK 3 B33 (A**2) : -10.69000
REMARK 3 B12 (A**2) : 3.99000
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) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.26
REMARK 3 LOW RESOLUTION CUTOFF (A) : 6.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.36
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.32
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.850
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) : 4.080 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 5.590 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 6.580 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 8.490 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 57.09
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 : WATER.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED. THE STRUCTURE
REMARK 3 WAS FIRST SOLVED BY MIRAS AND THEN REFINED WITH A NON
REMARK 3 ISOMORPHOUS NATIVE DATA SET.
REMARK 4
REMARK 4 2IX7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-JUL-06.
REMARK 100 THE DEPOSITION ID IS D_1290029284.
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 : 5.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9134
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 : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25837
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 29.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : 0.25000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: PDB ENTRY 1WCD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 73.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION METHOD (4 C) PROTEIN
REMARK 280 SOLUTION; 10MG/ML IN 10MM IMIDAZOL PH7.0, 20MM NACL. RESERVOIR;
REMARK 280 1.8M SA, 50MM MES PH5.0, 5% MPD, 5MM EGTA, 2MM NAN3, PH 5.00,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.22667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 34.11333
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 34.11333
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 68.22667
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 TOTAL BURIED SURFACE AREA: 6660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.1 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 S SO4 B1148 LIES ON A SPECIAL POSITION.
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 30 CG CD CE NZ
REMARK 470 LYS A 77 CG CD CE NZ
REMARK 470 GLU A 119 CG CD OE1 OE2
REMARK 470 LYS B 21 CG CD CE NZ
REMARK 470 ASP B 133 CG OD1 OD2
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 21 -34.54 -39.61
REMARK 500 ASN A 42 74.19 -113.43
REMARK 500 GLU A 54 25.44 -73.60
REMARK 500 VAL A 55 -23.90 -159.77
REMARK 500 ASP A 56 45.96 -109.70
REMARK 500 ASP A 93 78.21 -107.28
REMARK 500 LYS A 94 -76.13 -25.20
REMARK 500 LYS A 115 118.08 -27.41
REMARK 500 ARG B 74 -67.69 -91.23
REMARK 500 ASP B 78 46.86 -155.54
REMARK 500 ASP B 80 172.31 -59.70
REMARK 500 SER B 81 156.30 178.23
REMARK 500 ASN B 111 -39.86 -131.85
REMARK 500 ASP C 764 158.13 177.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1147
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1148
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1149
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1257
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1258
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYS C 1259
DBREF 2IX7 A 2 146 UNP P62204 CALM_MOUSE 2 146
DBREF 2IX7 B 2 146 UNP P62204 CALM_MOUSE 2 146
DBREF 2IX7 C 763 820 UNP Q99104 MYO5A_MOUSE 763 820
SEQRES 1 A 145 ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS GLU
SEQRES 2 A 145 ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR ILE
SEQRES 3 A 145 THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU GLY
SEQRES 4 A 145 GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE ASN
SEQRES 5 A 145 GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE PRO
SEQRES 6 A 145 GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP THR
SEQRES 7 A 145 ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL PHE
SEQRES 8 A 145 ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU LEU
SEQRES 9 A 145 ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR ASP
SEQRES 10 A 145 GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE ASP
SEQRES 11 A 145 GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN MET
SEQRES 12 A 145 MET THR
SEQRES 1 B 145 ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS GLU
SEQRES 2 B 145 ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR ILE
SEQRES 3 B 145 THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU GLY
SEQRES 4 B 145 GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE ASN
SEQRES 5 B 145 GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE PRO
SEQRES 6 B 145 GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP THR
SEQRES 7 B 145 ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL PHE
SEQRES 8 B 145 ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU LEU
SEQRES 9 B 145 ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR ASP
SEQRES 10 B 145 GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE ASP
SEQRES 11 B 145 GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN MET
SEQRES 12 B 145 MET THR
SEQRES 1 C 58 ALA ASP LYS LEU ARG ALA ALA CYS ILE ARG ILE GLN LYS
SEQRES 2 C 58 THR ILE ARG GLY TRP LEU LEU ARG LYS ARG TYR LEU CYS
SEQRES 3 C 58 MET GLN ARG ALA ALA ILE THR VAL GLN ARG TYR VAL ARG
SEQRES 4 C 58 GLY TYR GLN ALA ARG CYS TYR ALA LYS PHE LEU ARG ARG
SEQRES 5 C 58 THR LYS ALA ALA THR THR
HET SO4 B1147 5
HET SO4 B1148 5
HET SO4 B1149 5
HET CYS C1259 7
HET SO4 C1257 5
HET SO4 C1258 5
HETNAM SO4 SULFATE ION
HETNAM CYS CYSTEINE
FORMUL 4 SO4 5(O4 S 2-)
FORMUL 7 CYS C3 H7 N O2 S
FORMUL 10 HOH *144(H2 O)
HELIX 1 1 THR A 5 ASP A 20 1 16
HELIX 2 2 GLU A 31 LEU A 39 1 9
HELIX 3 3 THR A 44 GLU A 54 1 11
HELIX 4 4 PHE A 65 ASP A 78 1 14
HELIX 5 5 SER A 81 VAL A 91 1 11
HELIX 6 6 ALA A 102 LEU A 112 1 11
HELIX 7 7 THR A 117 ALA A 128 1 12
HELIX 8 8 ASN A 137 MET A 145 1 9
HELIX 9 9 THR B 5 PHE B 19 1 15
HELIX 10 10 GLU B 31 LEU B 39 1 9
HELIX 11 11 THR B 44 VAL B 55 1 12
HELIX 12 12 PHE B 65 MET B 76 1 12
HELIX 13 13 SER B 81 VAL B 91 1 11
HELIX 14 14 ALA B 102 THR B 110 1 9
HELIX 15 15 THR B 117 GLU B 127 1 11
HELIX 16 16 TYR B 138 THR B 146 1 9
HELIX 17 17 ASP C 764 THR C 819 1 56
SHEET 1 AA 2 THR A 26 THR A 28 0
SHEET 2 AA 2 THR A 62 ASP A 64 -1 O ILE A 63 N ILE A 27
SHEET 1 AB 2 ILE A 100 SER A 101 0
SHEET 2 AB 2 GLN A 135 VAL A 136 -1 N VAL A 136 O ILE A 100
SHEET 1 BA 2 THR B 26 THR B 28 0
SHEET 2 BA 2 THR B 62 ASP B 64 -1 O ILE B 63 N ILE B 27
SHEET 1 BB 2 TYR B 99 SER B 101 0
SHEET 2 BB 2 GLN B 135 ASN B 137 -1 O VAL B 136 N ILE B 100
SSBOND 1 CYS C 788 CYS C 1259 1555 1555 2.04
SITE 1 AC1 5 GLY B 61 THR B 62 HOH B2051 ASP C 764
SITE 2 AC1 5 LYS C 765
SITE 1 AC2 2 ASP B 131 GLY B 132
SITE 1 AC3 4 ARG B 106 HIS B 107 THR B 110 HOH B2082
SITE 1 AC4 3 LYS C 810 ARG C 813 HOH C2030
SITE 1 AC5 1 ARG C 814
SITE 1 AC6 2 CYS C 788 ARG C 791
CRYST1 112.000 112.000 102.340 90.00 90.00 120.00 P 32 2 1 12
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 0.008929 0.005155 0.000000 0.00000
SCALE2 0.000000 0.010310 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009771 0.00000
(ATOM LINES ARE NOT SHOWN.)
END