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HEADER HYDROLASE 17-JUL-03 1Q0R
TITLE CRYSTAL STRUCTURE OF ACLACINOMYCIN METHYLESTERASE (RDMC)
TITLE 2 WITH BOUND PRODUCT ANALOGUE, 10-
TITLE 3 DECARBOXYMETHYLACLACINOMYCIN T (DCMAT)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACLACINOMYCIN METHYLESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RDMC;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES PURPURASCENS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 GENE: RDMC;
SOURCE 5 EXPRESSION_SYSTEM: STREPTOMYCES LIVIDANS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: TK24;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PIJ487;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRDM*12
KEYWDS ANTHRACYCLINE, METHYLESTERASE, HYDROLASE, POLYKETIDE,
KEYWDS 2 STREPTOMYCES, TAILORING ENZYME
EXPDTA X-RAY DIFFRACTION
AUTHOR A.JANSSON,J.NIEMI,P.MANTSALA,G.SCHNEIDER
REVDAT 1 25-NOV-03 1Q0R 0
JRNL AUTH A.JANSSON,J.NIEMI,P.MANTSALA,G.SCHNEIDER
JRNL TITL CRYSTAL STRUCTURE OF ACLACINOMYCIN METHYLESTERASE
JRNL TITL 2 WITH BOUND PRODUCT ANALOGUES: IMPLICATIONS FOR
JRNL TITL 3 ANTHRACYCLINE RECOGNITION AND MECHANISM.
JRNL REF J.BIOL.CHEM. V. 278 39006 2003
JRNL REFN ASTM JBCHA3 US ISSN 0021-9258
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.JANSSON,J.NIEMI,P.MANTSALA,G.SCHNEIDER
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION
REMARK 1 TITL 2 STUDIES OF ACLACINOMYCIN-10-METHYL ESTERASE AND
REMARK 1 TITL 3 ACLACINOMYCIN-10-HYDROXYLASE FROM STREPTOMYCES
REMARK 1 TITL 4 PURPURASCENS
REMARK 1 REF ACTA CRYSTALLOGR., SECT.D V. 59 1637 2003
REMARK 1 REFN ASTM ABCRE6 DK ISSN 0907-4449
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 18.45
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 33778
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 + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2761
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.45
REMARK 3 BIN RESOLUTION RANGE LOW : 1.51
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2200
REMARK 3 BIN FREE R VALUE SET COUNT : 160
REMARK 3 BIN FREE R VALUE : 0.2400
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 2557
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.00
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; 0.008 ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; 1.331 ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RIDING HYDROGENS
REMARK 4
REMARK 4 1Q0R COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-AUG-2003.
REMARK 100 THE RCSB ID CODE IS RCSB019771.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-APR-2002
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8094
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
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 : 34733
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 18.450
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.8
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04100
REMARK 200 FOR THE DATA SET : 15.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 63.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.27300
REMARK 200 FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: SOLVE/ARP-WARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, PEG400, HEPES,
REMARK 280 PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,1/2+Y,-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 42.35000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 MET A 1
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
REMARK 500 O HOH 397 O HOH 399 1.91
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 SER A 15 CB SER A 15 OG 0.080
REMARK 500 GLY A 256 N GLY A 256 CA -0.117
REMARK 500 GLY A 256 CA GLY A 256 C -0.159
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 327 DISTANCE = 5.32 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Q0Z RELATED DB: PDB
DBREF 1Q0R A 1 298 GB 505671 AAA83422 1 298
SEQRES 1 A 298 MET SER GLU ARG ILE VAL PRO SER GLY ASP VAL GLU LEU
SEQRES 2 A 298 TRP SER ASP ASP PHE GLY ASP PRO ALA ASP PRO ALA LEU
SEQRES 3 A 298 LEU LEU VAL MET GLY GLY ASN LEU SER ALA LEU GLY TRP
SEQRES 4 A 298 PRO ASP GLU PHE ALA ARG ARG LEU ALA ASP GLY GLY LEU
SEQRES 5 A 298 HIS VAL ILE ARG TYR ASP HIS ARG ASP THR GLY ARG SER
SEQRES 6 A 298 THR THR ARG ASP PHE ALA ALA HIS PRO TYR GLY PHE GLY
SEQRES 7 A 298 GLU LEU ALA ALA ASP ALA VAL ALA VAL LEU ASP GLY TRP
SEQRES 8 A 298 GLY VAL ASP ARG ALA HIS VAL VAL GLY LEU SER MET GLY
SEQRES 9 A 298 ALA THR ILE THR GLN VAL ILE ALA LEU ASP HIS HIS ASP
SEQRES 10 A 298 ARG LEU SER SER LEU THR MET LEU LEU GLY GLY GLY LEU
SEQRES 11 A 298 ASP ILE ASP PHE ASP ALA ASN ILE GLU ARG VAL MET ARG
SEQRES 12 A 298 GLY GLU PRO THR LEU ASP GLY LEU PRO GLY PRO GLN GLN
SEQRES 13 A 298 PRO PHE LEU ASP ALA LEU ALA LEU MET ASN GLN PRO ALA
SEQRES 14 A 298 GLU GLY ARG ALA ALA GLU VAL ALA LYS ARG VAL SER LYS
SEQRES 15 A 298 TRP ARG ILE LEU SER GLY THR GLY VAL PRO PHE ASP ASP
SEQRES 16 A 298 ALA GLU TYR ALA ARG TRP GLU GLU ARG ALA ILE ASP HIS
SEQRES 17 A 298 ALA GLY GLY VAL LEU ALA GLU PRO TYR ALA HIS TYR SER
SEQRES 18 A 298 LEU THR LEU PRO PRO PRO SER ARG ALA ALA GLU LEU ARG
SEQRES 19 A 298 GLU VAL THR VAL PRO THR LEU VAL ILE GLN ALA GLU HIS
SEQRES 20 A 298 ASP PRO ILE ALA PRO ALA PRO HIS GLY LYS HIS LEU ALA
SEQRES 21 A 298 GLY LEU ILE PRO THR ALA ARG LEU ALA GLU ILE PRO GLY
SEQRES 22 A 298 MET GLY HIS ALA LEU PRO SER SER VAL HIS GLY PRO LEU
SEQRES 23 A 298 ALA GLU VAL ILE LEU ALA HIS THR ARG SER ALA ALA
HET AKT 600 37
HET SO4 3482 5
HET 1PE 2712 16
HETNAM AKT 10-DECARBOXYMETHYLACLACINOMYCIN T (DCMAT)
HETNAM SO4 SULFATE ION
HETNAM 1PE PENTAETHYLENE GLYCOL
HETSYN AKT 10-(4-DIMETHYLAMINO-5-HYDROXY-6-METHYL-TETRAHYDRO-
HETSYN 2 AKT PYRAN-2-YLOXY)-8-ETHYL-1,8,11-TRIHYDROXY-7,8,9,10-
HETSYN 3 AKT TETRAHYDRO-NAPHTHACENE-5,12-DIONE
HETSYN 1PE PEG400
FORMUL 2 AKT C28 H33 N1 O8
FORMUL 3 SO4 O4 S1 2-
FORMUL 4 1PE C10 H22 O6
FORMUL 5 HOH *256(H2 O1)
HELIX 1 1 SER A 35 TRP A 39 5 5
HELIX 2 2 PRO A 40 ASP A 49 1 10
HELIX 3 3 GLY A 76 TRP A 91 1 16
HELIX 4 4 SER A 102 HIS A 115 1 14
HELIX 5 5 ASP A 133 GLY A 144 1 12
HELIX 6 6 GLN A 155 GLN A 167 1 13
HELIX 7 7 GLY A 171 GLY A 188 1 18
HELIX 8 8 ASP A 194 ALA A 209 1 16
HELIX 9 9 TYR A 217 LEU A 222 5 6
HELIX 10 10 PRO A 226 VAL A 236 5 11
HELIX 11 11 PRO A 254 LEU A 262 1 9
HELIX 12 12 PRO A 279 SER A 281 5 3
HELIX 13 13 VAL A 282 ALA A 297 1 16
SHEET 1 A 8 GLU A 3 SER A 8 0
SHEET 2 A 8 VAL A 11 PHE A 18 -1 O LEU A 13 N VAL A 6
SHEET 3 A 8 HIS A 53 TYR A 57 -1 O ARG A 56 N ASP A 16
SHEET 4 A 8 ALA A 25 VAL A 29 1 N LEU A 26 O ILE A 55
SHEET 5 A 8 ALA A 96 LEU A 101 1 O VAL A 99 N VAL A 29
SHEET 6 A 8 LEU A 119 LEU A 125 1 O THR A 123 N GLY A 100
SHEET 7 A 8 THR A 240 ALA A 245 1 O ILE A 243 N MET A 124
SHEET 8 A 8 ALA A 266 ILE A 271 1 O ARG A 267 N VAL A 242
CISPEP 1 ALA A 253 PRO A 254 0 6.81
CRYST1 38.200 84.700 44.300 90.00 99.99 90.00 P 1 21 1 2
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 0.026178 -0.000001 0.004610 0.00000
SCALE2 0.000000 0.011806 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022921 0.00000
TER 2244 ALA A 298
MASTER 268 0 3 13 8 0 0 6 2557 1 58 23
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