HEADER CALCIUM-BINDING PROTEIN 19-JAN-98 1A29
TITLE CALMODULIN COMPLEXED WITH TRIFLUOPERAZINE (1:2 COMPLEX)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 ORGAN: BRAIN;
SOURCE 6 CELLULAR_LOCATION: CYTOPLASM
KEYWDS CALCIUM-BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR ZS.BOCSKEI,V.HARMAT,B.G.VERTESSY,J.OVADI,G.NARAY-SZABO
REVDAT 4 02-AUG-23 1A29 1 REMARK LINK
REVDAT 3 24-FEB-09 1A29 1 VERSN
REVDAT 2 01-APR-03 1A29 1 JRNL
REVDAT 1 16-SEP-98 1A29 0
JRNL AUTH B.G.VERTESSY,V.HARMAT,Z.BOCSKEI,G.NARAY-SZABO,F.OROSZ,
JRNL AUTH 2 J.OVADI
JRNL TITL SIMULTANEOUS BINDING OF DRUGS WITH DIFFERENT CHEMICAL
JRNL TITL 2 STRUCTURES TO CA2+-CALMODULIN: CRYSTALLOGRAPHIC AND
JRNL TITL 3 SPECTROSCOPIC STUDIES.
JRNL REF BIOCHEMISTRY V. 37 15300 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9799490
JRNL DOI 10.1021/BI980795A
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH W.J.COOK,L.J.WALTER,M.R.WALTER
REMARK 1 TITL DRUG BINDING BY CALMODULIN: CRYSTAL STRUCTURE OF A
REMARK 1 TITL 2 CALMODULIN-TRIFLUOPERAZINE COMPLEX
REMARK 1 REF BIOCHEMISTRY V. 33 15259 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. 2.74 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.74
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 59.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.5
REMARK 3 NUMBER OF REFLECTIONS : 4768
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) : 0.197
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 230
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.017
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.74
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.82
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 57.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 233
REMARK 3 BIN R VALUE (WORKING SET) : 0.1661
REMARK 3 BIN FREE R VALUE : 0.3395
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 12
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.098
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1086
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 60
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -9.97500
REMARK 3 B22 (A**2) : -9.97500
REMARK 3 B33 (A**2) : -7.10100
REMARK 3 B12 (A**2) : -8.45400
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) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.12
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.40
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.080
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.100
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : GROUPED
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 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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : CA.PAR
REMARK 3 PARAMETER FILE 3 : TFP.PAR
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : CA.TOP
REMARK 3 TOPOLOGY FILE 3 : TFP.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1A29 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170303.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : FEB-95
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE(002)
REMARK 200 OPTICS : NORMAL FOCUS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : BIOTEX
REMARK 200 DATA SCALING SOFTWARE : BIOTEX
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17223
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.740
REMARK 200 RESOLUTION RANGE LOW (A) : 87.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 1.920
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : 0.07370
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.74
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.09200
REMARK 200 R SYM FOR SHELL (I) : 0.20500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.840
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.851
REMARK 200 STARTING MODEL: PDB ENTRY 1LIN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED BY SITTING
REMARK 280 DROP TECHNIQUE IN THE COLD ROOM (8 DEGREES C +/- 2 DEGREES C) BY
REMARK 280 MIXING 4 MICROLITERS OF 1 MM PROTEIN CONTAINING 1.2-1.5 MM TFP
REMARK 280 IN 5 MM CACL2 WITH 4 MICROLITERS OF THE RESERVOIR SOLUTION (1 ML
REMARK 280 10 MM SODIUM CACODYLATE/HCL BUFFER, PH 5.2-5.6 WITH 10 MM CACL2,
REMARK 280 25-30 % (W/V) POLYETHYLENE GLYCOL 6000), CRYSTAL GROWTH TOOK 2-3
REMARK 280 WEEKS., PH 5.0
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 118.38000
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 59.19000
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 59.19000
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 118.38000
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 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 ALA A 1
REMARK 465 ASP A 2
REMARK 465 ALA A 147
REMARK 465 LYS A 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 6 CG CD OE1 OE2
REMARK 470 GLU A 7 CG CD OE1 OE2
REMARK 470 ASN A 53 CG OD1 ND2
REMARK 470 ARG A 74 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 75 CG CD CE NZ
REMARK 470 MET A 76 CG SD CE
REMARK 470 LYS A 77 CG CD CE NZ
REMARK 470 ASP A 78 CG OD1 OD2
REMARK 470 THR A 79 OG1 CG2
REMARK 470 ASP A 80 CG OD1 OD2
REMARK 470 GLU A 84 CG CD OE1 OE2
REMARK 470 GLU A 87 CG CD OE1 OE2
REMARK 470 LYS A 94 CG CD CE NZ
REMARK 470 LYS A 115 CG CD CE NZ
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 ASN A 42 79.24 -152.45
REMARK 500 ASP A 78 -175.89 -68.35
REMARK 500 THR A 79 -29.91 73.12
REMARK 500 SER A 81 66.34 79.40
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 A 149 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 20 OD1
REMARK 620 2 ASP A 22 OD1 77.0
REMARK 620 3 ASP A 24 OD1 76.0 75.7
REMARK 620 4 THR A 26 O 84.6 154.2 82.5
REMARK 620 5 GLU A 31 OE1 120.5 128.2 151.5 76.8
REMARK 620 6 GLU A 31 OE2 101.5 72.5 147.7 129.7 56.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 150 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 56 OD1
REMARK 620 2 ASP A 58 OD1 72.9
REMARK 620 3 ASN A 60 OD1 85.2 76.9
REMARK 620 4 THR A 62 O 75.4 141.7 79.5
REMARK 620 5 GLU A 67 OE1 112.8 121.8 156.4 90.2
REMARK 620 6 GLU A 67 OE2 61.9 84.1 145.8 99.5 56.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 151 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 93 OD1
REMARK 620 2 ASP A 95 OD1 79.1
REMARK 620 3 ASP A 95 OD2 118.1 39.9
REMARK 620 4 ASN A 97 OD1 81.4 74.2 74.1
REMARK 620 5 TYR A 99 O 83.9 155.1 146.4 85.5
REMARK 620 6 GLU A 104 OE1 95.5 123.7 122.8 161.2 75.7
REMARK 620 7 GLU A 104 OE2 108.9 72.9 69.4 142.6 130.4 55.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 152 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 129 OD1
REMARK 620 2 ASP A 131 OD1 77.7
REMARK 620 3 ASP A 133 OD1 87.6 83.3
REMARK 620 4 GLN A 135 O 85.8 154.7 76.9
REMARK 620 5 GLU A 140 OE1 112.7 123.7 148.2 80.3
REMARK 620 6 GLU A 140 OE2 85.6 71.0 154.3 127.2 55.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 149
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 151
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 152
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TFP A 153
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TFP A 154
DBREF 1A29 A 1 148 UNP P62157 CALM_BOVIN 1 148
SEQRES 1 A 148 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS
SEQRES 2 A 148 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR
SEQRES 3 A 148 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU
SEQRES 4 A 148 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE
SEQRES 5 A 148 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE
SEQRES 6 A 148 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP
SEQRES 7 A 148 THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL
SEQRES 8 A 148 PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU
SEQRES 9 A 148 LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR
SEQRES 10 A 148 ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE
SEQRES 11 A 148 ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN
SEQRES 12 A 148 MET MET THR ALA LYS
HET CA A 149 1
HET CA A 150 1
HET CA A 151 1
HET CA A 152 1
HET TFP A 153 28
HET TFP A 154 28
HETNAM CA CALCIUM ION
HETNAM TFP 10-[3-(4-METHYL-PIPERAZIN-1-YL)-PROPYL]-2-
HETNAM 2 TFP TRIFLUOROMETHYL-10H-PHENOTHIAZINE
FORMUL 2 CA 4(CA 2+)
FORMUL 6 TFP 2(C21 H24 F3 N3 S)
HELIX 1 1 GLU A 6 PHE A 19 1 14
HELIX 2 2 THR A 29 SER A 38 1 10
HELIX 3 3 GLU A 45 VAL A 55 1 11
HELIX 4 4 PHE A 65 ALA A 73 1 9
HELIX 5 5 GLU A 82 PHE A 92 1 11
HELIX 6 6 ALA A 102 LEU A 112 1 11
HELIX 7 7 ASP A 118 ALA A 128 1 11
HELIX 8 8 TYR A 138 MET A 144 1 7
SHEET 1 A 2 TYR A 99 ILE A 100 0
SHEET 2 A 2 VAL A 136 ASN A 137 -1 O VAL A 136 N ILE A 100
LINK OD1 ASP A 20 CA CA A 149 1555 1555 2.29
LINK OD1 ASP A 22 CA CA A 149 1555 1555 2.29
LINK OD1 ASP A 24 CA CA A 149 1555 1555 2.29
LINK O THR A 26 CA CA A 149 1555 1555 2.28
LINK OE1 GLU A 31 CA CA A 149 1555 1555 2.33
LINK OE2 GLU A 31 CA CA A 149 1555 1555 2.29
LINK OD1 ASP A 56 CA CA A 150 1555 1555 2.30
LINK OD1 ASP A 58 CA CA A 150 1555 1555 2.30
LINK OD1 ASN A 60 CA CA A 150 1555 1555 2.30
LINK O THR A 62 CA CA A 150 1555 1555 2.32
LINK OE1 GLU A 67 CA CA A 150 1555 1555 2.29
LINK OE2 GLU A 67 CA CA A 150 1555 1555 2.31
LINK OD1 ASP A 93 CA CA A 151 1555 1555 2.28
LINK OD1 ASP A 95 CA CA A 151 1555 1555 2.30
LINK OD2 ASP A 95 CA CA A 151 1555 1555 3.37
LINK OD1 ASN A 97 CA CA A 151 1555 1555 2.31
LINK O TYR A 99 CA CA A 151 1555 1555 2.31
LINK OE1 GLU A 104 CA CA A 151 1555 1555 2.32
LINK OE2 GLU A 104 CA CA A 151 1555 1555 2.32
LINK OD1 ASP A 129 CA CA A 152 1555 1555 2.31
LINK OD1 ASP A 131 CA CA A 152 1555 1555 2.30
LINK OD1 ASP A 133 CA CA A 152 1555 1555 2.30
LINK O GLN A 135 CA CA A 152 1555 1555 2.30
LINK OE1 GLU A 140 CA CA A 152 1555 1555 2.33
LINK OE2 GLU A 140 CA CA A 152 1555 1555 2.35
SITE 1 AC1 5 ASP A 20 ASP A 22 ASP A 24 THR A 26
SITE 2 AC1 5 GLU A 31
SITE 1 AC2 5 ASP A 56 ASP A 58 ASN A 60 THR A 62
SITE 2 AC2 5 GLU A 67
SITE 1 AC3 5 ASP A 93 ASP A 95 ASN A 97 TYR A 99
SITE 2 AC3 5 GLU A 104
SITE 1 AC4 5 ASP A 129 ASP A 131 ASP A 133 GLN A 135
SITE 2 AC4 5 GLU A 140
SITE 1 AC5 8 ILE A 100 LEU A 105 MET A 124 GLU A 127
SITE 2 AC5 8 VAL A 136 PHE A 141 MET A 144 TFP A 154
SITE 1 AC6 8 GLU A 11 GLU A 14 ALA A 15 MET A 109
SITE 2 AC6 8 GLU A 114 LEU A 116 GLU A 120 TFP A 153
CRYST1 40.750 40.750 177.570 90.00 90.00 120.00 P 32 2 1 6
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 0.024540 0.014168 0.000000 0.00000
SCALE2 0.000000 0.028336 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005632 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
