HEADER CALCIUM-BINDING PROTEIN 30-JUL-93 2SAS
TITLE STRUCTURE OF A SARCOPLASMIC CALCIUM-BINDING PROTEIN FROM AMPHIOXUS
TITLE 2 REFINED AT 2.4 ANGSTROMS RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SARCOPLASMIC CALCIUM-BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BRANCHIOSTOMA LANCEOLATUM;
SOURCE 3 ORGANISM_COMMON: AMPHIOXUS;
SOURCE 4 ORGANISM_TAXID: 7740
KEYWDS CALCIUM-BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR W.J.COOK,Y.S.BABU,J.A.COX
REVDAT 6 14-AUG-19 2SAS 1 REMARK
REVDAT 5 17-JUL-19 2SAS 1 REMARK
REVDAT 4 24-FEB-09 2SAS 1 VERSN
REVDAT 3 01-APR-03 2SAS 1 JRNL
REVDAT 2 15-MAY-95 2SAS 1 JRNL
REVDAT 1 31-OCT-93 2SAS 0
JRNL AUTH W.J.COOK,L.C.JEFFREY,J.A.COX,S.VIJAY-KUMAR
JRNL TITL STRUCTURE OF A SARCOPLASMIC CALCIUM-BINDING PROTEIN FROM
JRNL TITL 2 AMPHIOXUS REFINED AT 2.4 A RESOLUTION.
JRNL REF J.MOL.BIOL. V. 229 461 1993
JRNL REFN ISSN 0022-2836
JRNL PMID 8429557
JRNL DOI 10.1006/JMBI.1993.1046
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH W.J.COOK,Y.S.BABU,J.A.COX
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY INVESTIGATION OF A
REMARK 1 TITL 2 SARCOPLASMIC CALCIUM-BINDING PROTEIN FROM AMPHIOXUS
REMARK 1 REF J.MOL.BIOL. V. 221 1071 1991
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 5.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1495
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 1
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.088 ; 1.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.683 ; 1.500
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.888 ; 1.500
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.677 ; 2.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2SAS 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_1000178612.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 41.20000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 41.20000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 29.80000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 40.65000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 29.80000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 40.65000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 41.20000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 29.80000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 40.65000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 41.20000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 29.80000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 40.65000
REMARK 290 SMTRY3 8 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: DIMERIC
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 59.60000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 41.20000
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 ARG A 37 CD - NE - CZ ANGL. DEV. = 8.7 DEGREES
REMARK 500 GLU A 40 CA - CB - CG ANGL. DEV. = 23.2 DEGREES
REMARK 500 ASP A 70 CB - CG - OD2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 LYS A 88 CA - CB - CG ANGL. DEV. = 14.1 DEGREES
REMARK 500 ASP A 119 CB - CG - OD1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 GLN A 128 CA - CB - CG ANGL. DEV. = 13.7 DEGREES
REMARK 500 LYS A 132 CA - CB - CG ANGL. DEV. = 15.3 DEGREES
REMARK 500 PHE A 134 N - CA - C ANGL. DEV. = -19.4 DEGREES
REMARK 500 TYR A 145 CB - CG - CD2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 TYR A 145 CB - CG - CD1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG A 160 NE - CZ - NH1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG A 160 NE - CZ - NH2 ANGL. DEV. = 8.9 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 LEU A 18 -45.82 -132.21
REMARK 500 LYS A 43 -126.97 37.22
REMARK 500 ASP A 75 22.86 47.88
REMARK 500 THR A 92 43.44 -143.17
REMARK 500 ALA A 97 -8.95 -56.82
REMARK 500 LYS A 132 -67.68 -90.39
REMARK 500 PHE A 134 109.23 161.87
REMARK 500 GLN A 135 41.70 -68.78
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 186 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 19 OD1
REMARK 620 2 SER A 25 O 79.9
REMARK 620 3 ASN A 21 OD1 84.1 151.6
REMARK 620 4 ASP A 30 OD1 87.5 128.5 73.5
REMARK 620 5 ASP A 30 OD2 108.7 82.5 125.0 54.8
REMARK 620 6 ASP A 23 OD1 82.1 78.3 76.4 149.0 155.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 187 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 81 OE2
REMARK 620 2 ASP A 70 OD1 87.0
REMARK 620 3 ASN A 72 OD1 75.7 81.0
REMARK 620 4 ASP A 74 OD1 146.5 83.5 71.0
REMARK 620 5 VAL A 76 O 116.7 79.6 156.2 93.1
REMARK 620 6 GLU A 81 OE1 45.1 108.3 117.8 165.8 81.6
REMARK 620 7 HOH A 189 O 101.7 170.1 96.7 86.7 100.0 81.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 188 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 119 OD1
REMARK 620 2 ILE A 121 O 83.3
REMARK 620 3 SER A 117 OG 71.3 154.5
REMARK 620 4 GLU A 126 OE1 150.9 80.3 123.2
REMARK 620 5 GLU A 126 OE2 142.4 132.8 72.4 53.7
REMARK 620 6 ASP A 115 OD1 85.1 84.3 92.2 116.7 105.8
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: EF1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: EF2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: EF3
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 186
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 187
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 188
DBREF 2SAS A 1 185 UNP P04570 SCP2_BRALA 1 185
SEQRES 1 A 185 GLY LEU ASN ASP PHE GLN LYS GLN LYS ILE LYS PHE THR
SEQRES 2 A 185 PHE ASP PHE PHE LEU ASP MET ASN HIS ASP GLY SER ILE
SEQRES 3 A 185 GLN ASP ASN ASP PHE GLU ASP MET MET THR ARG TYR LYS
SEQRES 4 A 185 GLU VAL ASN LYS GLY SER LEU SER ASP ALA ASP TYR LYS
SEQRES 5 A 185 SER MET GLN ALA SER LEU GLU ASP GLU TRP ARG ASP LEU
SEQRES 6 A 185 LYS GLY ARG ALA ASP ILE ASN LYS ASP ASP VAL VAL SER
SEQRES 7 A 185 TRP GLU GLU TYR LEU ALA MET TRP GLU LYS THR ILE ALA
SEQRES 8 A 185 THR CYS LYS SER VAL ALA ASP LEU PRO ALA TRP CYS GLN
SEQRES 9 A 185 ASN ARG ILE PRO PHE LEU PHE LYS GLY MET ASP VAL SER
SEQRES 10 A 185 GLY ASP GLY ILE VAL ASP LEU GLU GLU PHE GLN ASN TYR
SEQRES 11 A 185 CYS LYS ASN PHE GLN LEU GLN CYS ALA ASP VAL PRO ALA
SEQRES 12 A 185 VAL TYR ASN VAL ILE THR ASP GLY GLY LYS VAL THR PHE
SEQRES 13 A 185 ASP LEU ASN ARG TYR LYS GLU LEU TYR TYR ARG LEU LEU
SEQRES 14 A 185 THR SER PRO ALA ALA ASP ALA GLY ASN THR LEU MET GLY
SEQRES 15 A 185 GLN LYS PRO
HET CA A 186 1
HET CA A 187 1
HET CA A 188 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 3(CA 2+)
FORMUL 5 HOH *(H2 O)
HELIX 1 A ASP A 4 LEU A 18 1 15
HELIX 2 B ASP A 28 ASN A 42 1 15
HELIX 3 C ASP A 48 ALA A 69 1 22
HELIX 4 D TRP A 79 ALA A 91 1 13
HELIX 5 E CYS A 103 MET A 114 1 12
HELIX 6 F LEU A 124 LYS A 132 1 9
HELIX 7 G VAL A 141 ILE A 148 1 8
HELIX 8 H LEU A 158 THR A 170 1 13
HELIX 9 I ALA A 176 MET A 181 5 6
SHEET 1 A 2 SER A 25 GLN A 27 0
SHEET 2 A 2 VAL A 76 SER A 78 -1
SSBOND 1 CYS A 131 CYS A 138 1555 1555 2.03
LINK CA CA A 186 OD1 ASP A 19 1555 1555 2.20
LINK CA CA A 186 O SER A 25 1555 1555 2.11
LINK CA CA A 186 OD1 ASN A 21 1555 1555 2.37
LINK CA CA A 186 OD1 ASP A 30 1555 1555 2.44
LINK CA CA A 186 OD2 ASP A 30 1555 1555 2.36
LINK CA CA A 186 OD1 ASP A 23 1555 1555 2.30
LINK CA CA A 187 OE2 GLU A 81 1555 1555 3.07
LINK CA CA A 187 OD1 ASP A 70 1555 1555 1.94
LINK CA CA A 187 OD1 ASN A 72 1555 1555 2.80
LINK CA CA A 187 OD1 ASP A 74 1555 1555 2.25
LINK CA CA A 187 O VAL A 76 1555 1555 2.32
LINK CA CA A 187 OE1 GLU A 81 1555 1555 2.33
LINK CA CA A 187 O HOH A 189 1555 1555 2.29
LINK CA CA A 188 OD1 ASP A 119 1555 1555 2.25
LINK CA CA A 188 O ILE A 121 1555 1555 2.41
LINK CA CA A 188 OG SER A 117 1555 1555 2.44
LINK CA CA A 188 OE1 GLU A 126 1555 1555 2.22
LINK CA CA A 188 OE2 GLU A 126 1555 1555 2.45
LINK CA CA A 188 OD1 ASP A 115 1555 1555 2.22
SITE 1 EF1 12 ASP A 19 MET A 20 ASN A 21 HIS A 22
SITE 2 EF1 12 ASP A 23 GLY A 24 SER A 25 ILE A 26
SITE 3 EF1 12 GLN A 27 ASP A 28 ASN A 29 ASP A 30
SITE 1 EF2 12 ASP A 70 ILE A 71 ASN A 72 LYS A 73
SITE 2 EF2 12 ASP A 74 ASP A 75 VAL A 76 VAL A 77
SITE 3 EF2 12 SER A 78 TRP A 79 GLU A 80 GLU A 81
SITE 1 EF3 12 ASP A 115 VAL A 116 SER A 117 GLY A 118
SITE 2 EF3 12 ASP A 119 GLY A 120 ILE A 121 VAL A 122
SITE 3 EF3 12 ASP A 123 LEU A 124 GLU A 125 GLU A 126
SITE 1 AC1 5 ASP A 19 ASN A 21 ASP A 23 SER A 25
SITE 2 AC1 5 ASP A 30
SITE 1 AC2 6 ASP A 70 ASN A 72 ASP A 74 VAL A 76
SITE 2 AC2 6 GLU A 81 HOH A 189
SITE 1 AC3 5 ASP A 115 SER A 117 ASP A 119 ILE A 121
SITE 2 AC3 5 GLU A 126
CRYST1 59.600 81.300 82.400 90.00 90.00 90.00 C 2 2 21 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 0.016779 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012300 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012136 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
