HEADER TRANSFERASE 10-JAN-00 1DSY
TITLE C2 DOMAIN FROM PROTEIN KINASE C (ALPHA) COMPLEXED WITH CA2+ AND
TITLE 2 PHOSPHATIDYLSERINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN KINASE C, ALPHA TYPE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CALCIUM/PHOSPHOLIPID BINDING DOMAIN;
COMPND 5 EC: 2.7.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET28C(+)
KEYWDS CALCIUM++, PHOSPHOLIPID BINDING PROTEIN, CALCIUM-BINDING PROTEIN,
KEYWDS 2 PHOSPHATIDYLSERINE, PROTEIN KINASE C, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.VERDAGUER,S.CORBALAN-GARCIA,W.F.OCHOA,I.FITA,J.C.GOMEZ-FERNANDEZ
REVDAT 4 07-FEB-24 1DSY 1 REMARK LINK
REVDAT 3 24-FEB-09 1DSY 1 VERSN
REVDAT 2 01-APR-03 1DSY 1 JRNL
REVDAT 1 26-JAN-00 1DSY 0
JRNL AUTH N.VERDAGUER,S.CORBALAN-GARCIA,W.F.OCHOA,I.FITA,
JRNL AUTH 2 J.C.GOMEZ-FERNANDEZ
JRNL TITL CA(2+) BRIDGES THE C2 MEMBRANE-BINDING DOMAIN OF PROTEIN
JRNL TITL 2 KINASE CALPHA DIRECTLY TO PHOSPHATIDYLSERINE.
JRNL REF EMBO J. V. 18 6329 1999
JRNL REFN ISSN 0261-4189
JRNL PMID 10562545
JRNL DOI 10.1093/EMBOJ/18.22.6329
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 18.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 5432
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 416
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1109
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 39
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 1.667
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DSY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JAN-00.
REMARK 100 THE DEPOSITION ID IS D_1000010338.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-FEB-99
REMARK 200 TEMPERATURE (KELVIN) : 293.0
REMARK 200 PH : 6.5
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 5610
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.09200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.28100
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: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8K, POTASSIUM PHOSPHATE, PH 6.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 61.13333
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 30.56667
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 30.56667
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 61.13333
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 HIS A 155
REMARK 465 GLY A 293
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 THR A 156 OG1 CG2
REMARK 470 GLU A 157 CG CD OE1 OE2
REMARK 470 ARG A 252 CG CD NE CZ NH1 NH2
REMARK 470 MET A 269 CG SD CE
REMARK 470 GLU A 292 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD2 ASP A 193 O4 PSF A 401 2.09
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 GLU A 171 N - CA - C ANGL. DEV. = -24.3 DEGREES
REMARK 500 LEU A 259 CA - CB - CG ANGL. DEV. = 16.8 DEGREES
REMARK 500 PRO A 291 C - N - CD ANGL. DEV. = -12.6 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 GLU A 157 141.74 160.87
REMARK 500 LYS A 158 -74.23 31.43
REMARK 500 ASP A 170 -88.75 -166.26
REMARK 500 GLU A 171 29.63 -173.23
REMARK 500 ARG A 178 -76.89 -92.29
REMARK 500 ASP A 193 78.14 -118.42
REMARK 500 SER A 260 145.49 -174.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PSF A 401
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 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET A 186 O
REMARK 620 2 ASP A 187 OD1 82.4
REMARK 620 3 ASP A 246 OD2 99.7 80.3
REMARK 620 4 ASP A 248 OD1 156.9 74.5 75.9
REMARK 620 5 ASP A 248 OD2 153.8 121.6 95.1 48.5
REMARK 620 6 ASP A 254 OD2 90.7 171.9 96.6 112.2 66.0
REMARK 620 7 HOH A 304 O 90.9 91.5 165.6 90.5 78.9 92.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 187 OD2
REMARK 620 2 ASP A 187 OD1 48.2
REMARK 620 3 ASP A 193 OD2 77.3 123.0
REMARK 620 4 ASP A 246 OD1 77.4 92.6 90.2
REMARK 620 5 ASP A 246 OD2 76.8 60.1 129.9 42.5
REMARK 620 6 TRP A 247 O 156.8 152.1 84.9 88.0 104.4
REMARK 620 7 ASP A 248 OD1 119.2 72.1 162.9 97.5 62.8 80.2
REMARK 620 8 PSF A 401 O4 77.3 94.6 52.1 138.4 152.2 103.3 123.7
REMARK 620 9 PSF A 401 O3 79.5 50.2 113.1 142.4 103.3 121.7 68.9 61.8
REMARK 620 N 1 2 3 4 5 6 7 8
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PSF A 401
DBREF 1DSY A 155 293 UNP P05696 KPCA_RAT 155 293
SEQRES 1 A 139 HIS THR GLU LYS ARG GLY ARG ILE TYR LEU LYS ALA GLU
SEQRES 2 A 139 VAL THR ASP GLU LYS LEU HIS VAL THR VAL ARG ASP ALA
SEQRES 3 A 139 LYS ASN LEU ILE PRO MET ASP PRO ASN GLY LEU SER ASP
SEQRES 4 A 139 PRO TYR VAL LYS LEU LYS LEU ILE PRO ASP PRO LYS ASN
SEQRES 5 A 139 GLU SER LYS GLN LYS THR LYS THR ILE ARG SER THR LEU
SEQRES 6 A 139 ASN PRO GLN TRP ASN GLU SER PHE THR PHE LYS LEU LYS
SEQRES 7 A 139 PRO SER ASP LYS ASP ARG ARG LEU SER VAL GLU ILE TRP
SEQRES 8 A 139 ASP TRP ASP ARG THR THR ARG ASN ASP PHE MET GLY SER
SEQRES 9 A 139 LEU SER PHE GLY VAL SER GLU LEU MET LYS MET PRO ALA
SEQRES 10 A 139 SER GLY TRP TYR LYS LEU LEU ASN GLN GLU GLU GLY GLU
SEQRES 11 A 139 TYR TYR ASN VAL PRO ILE PRO GLU GLY
HET CA A 501 1
HET CA A 502 1
HET PO4 A 601 5
HET PSF A 401 25
HETNAM CA CALCIUM ION
HETNAM PO4 PHOSPHATE ION
HETNAM PSF 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE
HETSYN PSF PHOSPHATIDYLSERINE
FORMUL 2 CA 2(CA 2+)
FORMUL 4 PO4 O4 P 3-
FORMUL 5 PSF C18 H34 N O10 P
FORMUL 6 HOH *39(H2 O)
HELIX 1 1 LYS A 232 LYS A 236 5 5
HELIX 2 2 VAL A 263 MET A 269 1 7
HELIX 3 3 ASN A 279 GLU A 284 1 6
SHEET 1 A 5 GLN A 222 LYS A 230 0
SHEET 2 A 5 LYS A 172 LYS A 181 -1 N LEU A 173 O PHE A 229
SHEET 3 A 5 ARG A 161 VAL A 168 -1 O ARG A 161 N LYS A 181
SHEET 4 A 5 ALA A 271 LYS A 276 -1 N ALA A 271 O ALA A 166
SHEET 5 A 5 VAL A 288 ILE A 290 -1 O VAL A 288 N LYS A 276
SHEET 1 B 4 GLN A 210 LYS A 211 0
SHEET 2 B 4 PRO A 194 ILE A 201 -1 N LEU A 198 O GLN A 210
SHEET 3 B 4 ARG A 239 ASP A 246 -1 O ARG A 239 N ILE A 201
SHEET 4 B 4 ASP A 254 GLY A 262 -1 O ASP A 254 N ASP A 246
LINK O MET A 186 CA CA A 501 1555 1555 2.24
LINK OD1 ASP A 187 CA CA A 501 1555 1555 2.35
LINK OD2 ASP A 187 CA CA A 502 1555 1555 2.68
LINK OD1 ASP A 187 CA CA A 502 1555 1555 2.68
LINK OD2 ASP A 193 CA CA A 502 1555 1555 2.54
LINK OD2 ASP A 246 CA CA A 501 1555 1555 2.29
LINK OD1 ASP A 246 CA CA A 502 1555 1555 2.57
LINK OD2 ASP A 246 CA CA A 502 1555 1555 3.23
LINK O TRP A 247 CA CA A 502 1555 1555 2.34
LINK OD1 ASP A 248 CA CA A 501 1555 1555 2.61
LINK OD2 ASP A 248 CA CA A 501 1555 1555 2.71
LINK OD1 ASP A 248 CA CA A 502 1555 1555 2.43
LINK OD2 ASP A 254 CA CA A 501 1555 1555 2.41
LINK O HOH A 304 CA CA A 501 1555 1555 3.15
LINK O4 PSF A 401 CA CA A 502 1555 1555 2.17
LINK O3 PSF A 401 CA CA A 502 1555 1555 2.49
CISPEP 1 ILE A 201 PRO A 202 0 -0.60
SITE 1 AC1 5 MET A 186 ASP A 187 ASP A 246 ASP A 248
SITE 2 AC1 5 ASP A 254
SITE 1 AC2 6 ASP A 187 ASP A 193 ASP A 246 TRP A 247
SITE 2 AC2 6 ASP A 248 PSF A 401
SITE 1 AC3 6 TYR A 195 LYS A 197 LYS A 209 LYS A 211
SITE 2 AC3 6 ASN A 253 HOH A 316
SITE 1 AC4 16 ASP A 187 PRO A 188 ASN A 189 ASP A 193
SITE 2 AC4 16 ASP A 203 GLU A 207 SER A 208 ARG A 216
SITE 3 AC4 16 ARG A 238 TRP A 247 ASP A 248 ARG A 249
SITE 4 AC4 16 THR A 250 THR A 251 HOH A 335 CA A 502
CRYST1 58.800 58.800 91.700 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 0.017007 0.009819 0.000000 0.00000
SCALE2 0.000000 0.019638 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010905 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
