HEADER LYASE 31-JAN-00 1EE6
TITLE CRYSTAL STRUCTURE OF PECTATE LYASE FROM BACILLUS SP. STRAIN KSM-P15.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PECTATE LYASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 4.2.2.2
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SP.;
SOURCE 3 ORGANISM_TAXID: 98226;
SOURCE 4 STRAIN: KSM-P15
KEYWDS PARALLEL BETA-HELIX, HIGH-ALKALINE, LOW-MOLECULAR-WEIGHT, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.AKITA,A.SUZUKI,T.KOBAYASHI,S.ITO,T.YAMANE
REVDAT 3 13-JUL-11 1EE6 1 VERSN
REVDAT 2 24-FEB-09 1EE6 1 VERSN
REVDAT 1 31-JAN-01 1EE6 0
JRNL AUTH M.AKITA,A.SUZUKI,T.KOBAYASHI,S.ITO,T.YAMANE
JRNL TITL THE FIRST STRUCTURE OF PECTATE LYASE BELONGING TO
JRNL TITL 2 POLYSACCHARIDE LYASE FAMILY 3.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 57 1786 2001
JRNL REFN ISSN 0907-4449
JRNL PMID 11717490
JRNL DOI 10.1107/S0907444900003334
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000
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 : 8859
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) : 0.186
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 466
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 : 1472
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 170
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 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) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 2.70
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 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: FOUR DISORDERED SIDE-CHAIN(1A,7E,20K,
REMARK 3 39K) WERE EXCLUDED IN REFINEMENT STAGE.
REMARK 4
REMARK 4 1EE6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-FEB-00.
REMARK 100 THE RCSB ID CODE IS RCSB010485.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-99
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.7
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 RU300
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 : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10063
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
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 (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.20400
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: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, PH 6.7, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 21.45000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.50000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.25000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 41.50000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.45000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.25000
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: 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 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 7 CB CG CD OE1 OE2
REMARK 480 LYS A 20 CB CG CD CE NZ
REMARK 480 ASN A 39 CB CG OD1 ND2
REMARK 480 LYS A 185 CB CG CD CE NZ
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 HIS A 6 NE2 HIS A 6 CD2 -0.071
REMARK 500 HIS A 66 NE2 HIS A 66 CD2 -0.077
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 TRP A 78 CD1 - CG - CD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 TRP A 78 CE2 - CD2 - CG ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG A 120 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 123 NE - CZ - NH2 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 132 NE - CZ - NH2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 TYR A 174 CB - CG - CD1 ANGL. DEV. = -4.1 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 ASN A 39 71.26 43.69
REMARK 500 ALA A 62 -118.73 43.19
REMARK 500 ASP A 80 102.78 -167.75
REMARK 500 ASP A 106 -97.17 -132.02
REMARK 500 ASP A 126 77.07 60.94
REMARK 500 ASN A 134 125.32 -39.98
REMARK 500 ARG A 152 71.92 52.56
REMARK 500 ASP A 155 -62.60 -125.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 380 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH A 381 DISTANCE = 5.51 ANGSTROMS
REMARK 525 HOH A 385 DISTANCE = 5.08 ANGSTROMS
REMARK 525 HOH A 437 DISTANCE = 5.21 ANGSTROMS
REMARK 525 HOH A 439 DISTANCE = 7.16 ANGSTROMS
REMARK 525 HOH A 442 DISTANCE = 5.30 ANGSTROMS
REMARK 525 HOH A 445 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH A 446 DISTANCE = 6.74 ANGSTROMS
REMARK 525 HOH A 464 DISTANCE = 5.54 ANGSTROMS
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 300 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 81 O
REMARK 620 2 ASP A 80 OD2 89.0
REMARK 620 3 LYS A 103 O 92.7 90.3
REMARK 620 4 HOH A 359 O 155.1 67.9 96.4
REMARK 620 5 HOH A 327 O 69.5 158.4 88.9 133.7
REMARK 620 6 HOH A 467 O 94.4 104.0 164.2 82.9 80.4
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 300
DBREF 1EE6 A 1 197 UNP Q9RHW0 Q9RHW0_BACSP 28 224
SEQRES 1 A 197 ALA PRO THR VAL VAL HIS GLU THR ILE ARG VAL PRO ALA
SEQRES 2 A 197 GLY GLN THR PHE ASP GLY LYS GLY GLN THR TYR VAL ALA
SEQRES 3 A 197 ASN PRO ASN THR LEU GLY ASP GLY SER GLN ALA GLU ASN
SEQRES 4 A 197 GLN LYS PRO ILE PHE ARG LEU GLU ALA GLY ALA SER LEU
SEQRES 5 A 197 LYS ASN VAL VAL ILE GLY ALA PRO ALA ALA ASP GLY VAL
SEQRES 6 A 197 HIS CYS TYR GLY ASP CYS THR ILE THR ASN VAL ILE TRP
SEQRES 7 A 197 GLU ASP VAL GLY GLU ASP ALA LEU THR LEU LYS SER SER
SEQRES 8 A 197 GLY THR VAL ASN ILE SER GLY GLY ALA ALA TYR LYS ALA
SEQRES 9 A 197 TYR ASP LYS VAL PHE GLN ILE ASN ALA ALA GLY THR ILE
SEQRES 10 A 197 ASN ILE ARG ASN PHE ARG ALA ASP ASP ILE GLY LYS LEU
SEQRES 11 A 197 VAL ARG GLN ASN GLY GLY THR THR TYR LYS VAL VAL MET
SEQRES 12 A 197 ASN VAL GLU ASN CYS ASN ILE SER ARG VAL LYS ASP ALA
SEQRES 13 A 197 ILE LEU ARG THR ASP SER SER THR SER THR GLY ARG ILE
SEQRES 14 A 197 VAL ASN THR ARG TYR SER ASN VAL PRO THR LEU PHE LYS
SEQRES 15 A 197 GLY PHE LYS SER GLY ASN THR THR ALA SER GLY ASN THR
SEQRES 16 A 197 GLN TYR
HET CA A 300 1
HETNAM CA CALCIUM ION
FORMUL 2 CA CA 2+
FORMUL 3 HOH *170(H2 O)
SHEET 1 A 9 THR A 3 VAL A 5 0
SHEET 2 A 9 THR A 16 ALA A 26 1 O THR A 23 N THR A 3
SHEET 3 A 9 ALA A 50 ILE A 57 1 O SER A 51 N PHE A 17
SHEET 4 A 9 CYS A 71 TRP A 78 1 O THR A 72 N LEU A 52
SHEET 5 A 9 GLY A 92 SER A 97 1 O THR A 93 N CYS A 71
SHEET 6 A 9 GLY A 115 ARG A 120 1 O THR A 116 N VAL A 94
SHEET 7 A 9 VAL A 141 GLU A 146 1 N VAL A 142 O GLY A 115
SHEET 8 A 9 THR A 166 VAL A 170 1 O THR A 166 N MET A 143
SHEET 9 A 9 THR A 189 SER A 192 1 N THR A 190 O GLY A 167
SHEET 1 B13 ILE A 9 VAL A 11 0
SHEET 2 B13 PHE A 44 LEU A 46 1 N ARG A 45 O ILE A 9
SHEET 3 B13 VAL A 65 TYR A 68 1 O HIS A 66 N LEU A 46
SHEET 4 B13 LEU A 86 SER A 90 1 N THR A 87 O VAL A 65
SHEET 5 B13 ALA A 100 ILE A 111 1 O VAL A 108 N LEU A 86
SHEET 6 B13 CYS A 71 TRP A 78 1 O VAL A 76 N ALA A 100
SHEET 7 B13 ALA A 100 ILE A 111 1 O ALA A 100 N TRP A 78
SHEET 8 B13 ARG A 123 GLN A 133 1 O ARG A 123 N ALA A 101
SHEET 9 B13 ASN A 149 ARG A 159 1 O ASN A 149 N ALA A 124
SHEET 10 B13 PHE A 181 LYS A 182 1 N LYS A 182 O LEU A 158
SHEET 11 B13 ASN A 149 ARG A 159 1 O LEU A 158 N LYS A 182
SHEET 12 B13 ARG A 173 SER A 175 1 O ARG A 173 N ILE A 150
SHEET 13 B13 THR A 195 GLN A 196 1 O THR A 195 N TYR A 174
SSBOND 1 CYS A 67 CYS A 71 1555 1555 1.97
LINK CA CA A 300 O VAL A 81 1555 1555 2.17
LINK CA CA A 300 OD2 ASP A 80 1555 1555 2.22
LINK CA CA A 300 O LYS A 103 1555 1555 2.28
LINK CA CA A 300 O HOH A 359 1555 1555 2.96
LINK CA CA A 300 O HOH A 327 1555 1555 2.50
LINK CA CA A 300 O HOH A 467 1555 1555 2.19
CISPEP 1 ALA A 59 PRO A 60 0 -3.73
SITE 1 AC1 6 ASP A 80 VAL A 81 LYS A 103 HOH A 327
SITE 2 AC1 6 HOH A 359 HOH A 467
CRYST1 42.900 60.500 83.000 90.00 90.00 90.00 P 21 21 21 4
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 0.023310 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016530 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012050 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
