HEADER OXIDOREDUCTASE 19-JUN-03 1PQW
TITLE PUTATIVE ENOYL REDUCTASE DOMAIN OF POLYKETIDE SYNTHASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYKETIDE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: PUTATIVE ENOYL REDUCTASE DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83331;
SOURCE 4 STRAIN: CDC1551;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PSMT3
KEYWDS ROSSMANN FOLD, DIMER, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS,
KEYWDS 3 NYSGXRC, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.GOGOS,H.MU,L.SHAPIRO,S.K.BURLEY,NEW YORK SGX RESEARCH CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (NYSGXRC)
REVDAT 6 14-FEB-24 1PQW 1 REMARK
REVDAT 5 03-FEB-21 1PQW 1 AUTHOR REMARK SEQADV LINK
REVDAT 4 13-JUL-11 1PQW 1 VERSN
REVDAT 3 24-FEB-09 1PQW 1 VERSN
REVDAT 2 25-JAN-05 1PQW 1 AUTHOR KEYWDS REMARK
REVDAT 1 08-JUL-03 1PQW 0
JRNL AUTH A.GOGOS,H.MU,L.SHAPIRO
JRNL TITL PUTATIVE ENOYL REDUCTASE DOMAIN OF POLYKETIDE SYNTHASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.66 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 2.66
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 17.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 24404
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 : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1204
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
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) : 2.66
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.78
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2944
REMARK 3 BIN R VALUE (WORKING SET) : 0.2220
REMARK 3 BIN FREE R VALUE : 0.2530
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 140
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2633
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 141
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.80000
REMARK 3 B22 (A**2) : -1.57000
REMARK 3 B33 (A**2) : -2.23000
REMARK 3 B12 (A**2) : 0.00000
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) : 0.25
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) : 0.34
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.34
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.400
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 : CNS BULK SOLVENT MODEL USED
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 24.72
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_REP.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: NULL
REMARK 4
REMARK 4 1PQW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUN-03.
REMARK 100 THE DEPOSITION ID IS D_1000019517.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-APR-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97917, 0.97942, 0.96864
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.660
REMARK 200 RESOLUTION RANGE LOW (A) : 17.970
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : 0.07600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.16000
REMARK 200 R SYM FOR SHELL (I) : 0.16000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 15.00
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE, RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, ISOPROPANOL CALCIUM
REMARK 280 CHLORIDE, TRIS, NADPH , PH 8.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 34.91500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.80200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.19550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.80200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.91500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.19550
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 SER A 1
REMARK 465 ASP A 2
REMARK 465 LEU A 3
REMARK 465 VAL A 4
REMARK 465 VAL A 5
REMARK 465 PRO A 6
REMARK 465 ILE A 7
REMARK 465 PRO A 8
REMARK 465 ASP A 9
REMARK 465 THR A 10
REMARK 465 LEU A 11
REMARK 465 ALA A 12
REMARK 465 ASP A 13
REMARK 465 ALA A 197
REMARK 465 PHE A 198
REMARK 465 SER B 1
REMARK 465 ASP B 2
REMARK 465 LEU B 3
REMARK 465 VAL B 4
REMARK 465 VAL B 5
REMARK 465 PRO B 6
REMARK 465 ILE B 7
REMARK 465 PRO B 8
REMARK 465 ASP B 9
REMARK 465 THR B 10
REMARK 465 LEU B 11
REMARK 465 ALA B 12
REMARK 465 ASP B 13
REMARK 465 ASN B 14
REMARK 465 GLU B 15
REMARK 465 ALA B 16
REMARK 465 LYS B 139
REMARK 465 ASP B 140
REMARK 465 VAL B 141
REMARK 465 TYR B 142
REMARK 465 ALA B 143
REMARK 465 ASP B 144
REMARK 465 PHE B 198
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 ASN A 14 CG OD1 ND2
REMARK 470 ARG A 65 CZ NH1 NH2
REMARK 470 GLU A 77 CD OE1 OE2
REMARK 470 GLN A 121 CG CD OE1 NE2
REMARK 470 LYS A 138 CG CD CE NZ
REMARK 470 ASP A 140 CG OD1 OD2
REMARK 470 ASP A 144 CG OD1 OD2
REMARK 470 GLU B 77 CG CD OE1 OE2
REMARK 470 LYS B 138 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 LYS A 139 -19.08 -42.43
REMARK 500 ALA A 143 -76.61 -33.25
REMARK 500 VAL A 195 -161.38 -79.83
REMARK 500 THR B 196 20.17 -70.87
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 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 101 OE1
REMARK 620 2 GLU A 101 OE2 52.2
REMARK 620 3 HOH A 549 O 81.9 88.5
REMARK 620 4 ASP B 94 OD1 124.3 73.2 87.2
REMARK 620 5 ASP B 94 OD2 106.4 64.6 132.2 48.6
REMARK 620 N 1 2 3 4
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 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-T109 RELATED DB: TARGETDB
DBREF 1PQW A 2 198 UNP P96202 P96202_MYCTU 1559 1755
DBREF 1PQW B 2 198 UNP P96202 P96202_MYCTU 1559 1755
SEQADV 1PQW SER A 1 UNP P96202 CLONING ARTIFACT
SEQADV 1PQW SER B 1 UNP P96202 CLONING ARTIFACT
SEQRES 1 A 198 SER ASP LEU VAL VAL PRO ILE PRO ASP THR LEU ALA ASP
SEQRES 2 A 198 ASN GLU ALA ALA THR PHE GLY VAL ALA TYR LEU THR ALA
SEQRES 3 A 198 TRP HIS SER LEU CYS GLU VAL GLY ARG LEU SER PRO GLY
SEQRES 4 A 198 GLU ARG VAL LEU ILE HIS SER ALA THR GLY GLY VAL GLY
SEQRES 5 A 198 MET ALA ALA VAL SER ILE ALA LYS MET ILE GLY ALA ARG
SEQRES 6 A 198 ILE TYR THR THR ALA GLY SER ASP ALA LYS ARG GLU MET
SEQRES 7 A 198 LEU SER ARG LEU GLY VAL GLU TYR VAL GLY ASP SER ARG
SEQRES 8 A 198 SER VAL ASP PHE ALA ASP GLU ILE LEU GLU LEU THR ASP
SEQRES 9 A 198 GLY TYR GLY VAL ASP VAL VAL LEU ASN SER LEU ALA GLY
SEQRES 10 A 198 GLU ALA ILE GLN ARG GLY VAL GLN ILE LEU ALA PRO GLY
SEQRES 11 A 198 GLY ARG PHE ILE GLU LEU GLY LYS LYS ASP VAL TYR ALA
SEQRES 12 A 198 ASP ALA SER LEU GLY LEU ALA ALA LEU ALA LYS SER ALA
SEQRES 13 A 198 SER PHE SER VAL VAL ASP LEU ASP LEU ASN LEU LYS LEU
SEQRES 14 A 198 GLN PRO ALA ARG TYR ARG GLN LEU LEU GLN HIS ILE LEU
SEQRES 15 A 198 GLN HIS VAL ALA ASP GLY LYS LEU GLU VAL LEU PRO VAL
SEQRES 16 A 198 THR ALA PHE
SEQRES 1 B 198 SER ASP LEU VAL VAL PRO ILE PRO ASP THR LEU ALA ASP
SEQRES 2 B 198 ASN GLU ALA ALA THR PHE GLY VAL ALA TYR LEU THR ALA
SEQRES 3 B 198 TRP HIS SER LEU CYS GLU VAL GLY ARG LEU SER PRO GLY
SEQRES 4 B 198 GLU ARG VAL LEU ILE HIS SER ALA THR GLY GLY VAL GLY
SEQRES 5 B 198 MET ALA ALA VAL SER ILE ALA LYS MET ILE GLY ALA ARG
SEQRES 6 B 198 ILE TYR THR THR ALA GLY SER ASP ALA LYS ARG GLU MET
SEQRES 7 B 198 LEU SER ARG LEU GLY VAL GLU TYR VAL GLY ASP SER ARG
SEQRES 8 B 198 SER VAL ASP PHE ALA ASP GLU ILE LEU GLU LEU THR ASP
SEQRES 9 B 198 GLY TYR GLY VAL ASP VAL VAL LEU ASN SER LEU ALA GLY
SEQRES 10 B 198 GLU ALA ILE GLN ARG GLY VAL GLN ILE LEU ALA PRO GLY
SEQRES 11 B 198 GLY ARG PHE ILE GLU LEU GLY LYS LYS ASP VAL TYR ALA
SEQRES 12 B 198 ASP ALA SER LEU GLY LEU ALA ALA LEU ALA LYS SER ALA
SEQRES 13 B 198 SER PHE SER VAL VAL ASP LEU ASP LEU ASN LEU LYS LEU
SEQRES 14 B 198 GLN PRO ALA ARG TYR ARG GLN LEU LEU GLN HIS ILE LEU
SEQRES 15 B 198 GLN HIS VAL ALA ASP GLY LYS LEU GLU VAL LEU PRO VAL
SEQRES 16 B 198 THR ALA PHE
HET CA A 501 1
HETNAM CA CALCIUM ION
FORMUL 3 CA CA 2+
FORMUL 4 HOH *141(H2 O)
HELIX 1 1 ASN A 14 GLU A 32 1 19
HELIX 2 2 GLY A 49 GLY A 63 1 15
HELIX 3 3 SER A 72 ARG A 81 1 10
HELIX 4 4 ASP A 94 THR A 103 1 10
HELIX 5 5 GLY A 117 ILE A 126 1 10
HELIX 6 6 LYS A 138 TYR A 142 5 5
HELIX 7 7 ALA A 150 ALA A 153 5 4
HELIX 8 8 ASP A 162 GLN A 170 1 9
HELIX 9 9 GLN A 170 ASP A 187 1 18
HELIX 10 10 THR B 18 CYS B 31 1 14
HELIX 11 11 GLY B 49 GLY B 63 1 15
HELIX 12 12 SER B 72 LEU B 82 1 11
HELIX 13 13 ASP B 94 THR B 103 1 10
HELIX 14 14 GLY B 117 ILE B 126 1 10
HELIX 15 15 ALA B 150 ALA B 153 5 4
HELIX 16 16 ASP B 162 GLN B 170 1 9
HELIX 17 17 GLN B 170 ASP B 187 1 18
SHEET 1 A12 TYR A 86 ASP A 89 0
SHEET 2 A12 ARG A 65 ALA A 70 1 N THR A 68 O GLY A 88
SHEET 3 A12 ARG A 41 ILE A 44 1 N ILE A 44 O TYR A 67
SHEET 4 A12 VAL A 108 ASN A 113 1 O VAL A 110 N LEU A 43
SHEET 5 A12 LEU A 127 GLU A 135 1 O ALA A 128 N VAL A 108
SHEET 6 A12 SER A 157 VAL A 160 1 O SER A 159 N PHE A 133
SHEET 7 A12 SER B 157 VAL B 160 -1 O PHE B 158 N PHE A 158
SHEET 8 A12 LEU B 127 GLU B 135 1 N GLU B 135 O SER B 159
SHEET 9 A12 VAL B 108 ASN B 113 1 N ASN B 113 O ILE B 134
SHEET 10 A12 ARG B 41 ILE B 44 1 N LEU B 43 O VAL B 110
SHEET 11 A12 ARG B 65 ALA B 70 1 O TYR B 67 N ILE B 44
SHEET 12 A12 TYR B 86 ASP B 89 1 O TYR B 86 N THR B 68
SHEET 1 B 2 SER A 146 GLY A 148 0
SHEET 2 B 2 SER B 146 GLY B 148 -1 O LEU B 147 N LEU A 147
LINK OE1 GLU A 101 CA CA A 501 1555 1555 2.69
LINK OE2 GLU A 101 CA CA A 501 1555 1555 2.19
LINK CA CA A 501 O HOH A 549 1555 1555 2.79
LINK CA CA A 501 OD1 ASP B 94 1555 3545 2.81
LINK CA CA A 501 OD2 ASP B 94 1555 3545 2.48
SITE 1 AC1 3 GLU A 101 HOH A 549 ASP B 94
CRYST1 69.830 78.391 81.604 90.00 90.00 90.00 P 21 21 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 0.014320 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012757 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012254 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
