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HEADER LIGASE 29-APR-08 2VSQ
TITLE STRUCTURE OF SURFACTIN A SYNTHETASE C (SRFA-C), A
TITLE 2 NONRIBOSOMAL PEPTIDE SYNTHETASE TERMINATION MODULE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SURFACTIN SYNTHETASE SUBUNIT 3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: TERMINATION MODULE OF SURFACTIN A BIOSYNTHESIS
COMPND 5 CLUSTER, RESIDUES 1-1009,1015-1274;
COMPND 6 SYNONYM: SURFACTIN A SYNTHETASE C;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 ATCC: 21332;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: M15;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: PREP4;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTRCHIS2-TOPO_SRFA-C
KEYWDS LIGASE, PEPTIDYL CARRIER PROTEIN, LIGASE PHOSPHOPROTEIN,
KEYWDS 2 TERMINATION MODULE, PHOSPHOPANTETHEINE, NONRIBOSOMAL
KEYWDS 3 PEPTIDE SYNTHESIS, SYNTHETASE, ADENYLATION, SPORULATION,
KEYWDS 4 ANTIBIOTIC BIOSYNTHESIS, ENZYMATIC ASSEMBLY LINE,
KEYWDS 5 SURFACTIN A, CONDENSATION, THIOESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.TANOVIC,S.A.SAMEL,L.-O.ESSEN,M.A.MARAHIEL
REVDAT 3 24-FEB-09 2VSQ 1 VERSN
REVDAT 2 12-AUG-08 2VSQ 1 JRNL REMARK
REVDAT 1 08-JUL-08 2VSQ 0
JRNL AUTH A.TANOVIC,S.A.SAMEL,L.-O.ESSEN,M.A.MARAHIEL
JRNL TITL CRYSTAL STRUCTURE OF THE TERMINATION MODULE OF A
JRNL TITL 2 NONRIBOSOMAL PEPTIDE SYNTHETASE.
JRNL REF SCIENCE V. 321 659 2008
JRNL REFN ISSN 0036-8075
JRNL PMID 18583577
JRNL DOI 10.1126/SCIENCE.1159850
REMARK 2
REMARK 2 RESOLUTION. 2.6 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 82.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.1
REMARK 3 NUMBER OF REFLECTIONS : 44479
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) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.300
REMARK 3 FREE R VALUE TEST SET COUNT : 1040
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2207
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3240
REMARK 3 BIN FREE R VALUE SET COUNT : 50
REMARK 3 BIN FREE R VALUE : 0.4360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10056
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 39
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 79.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.59000
REMARK 3 B22 (A**2) : -0.53000
REMARK 3 B33 (A**2) : 2.11000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.03000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.907
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.349
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.284
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 28.590
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10282 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 6915 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13938 ; 1.272 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16908 ; 0.878 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1269 ; 7.014 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 489 ;37.327 ;24.847
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1770 ;19.167 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 52 ;18.264 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1548 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11458 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2025 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2646 ; 0.228 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 7308 ; 0.188 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5005 ; 0.186 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 5551 ; 0.089 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 309 ; 0.151 ; 0.200
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): 27 ; 0.162 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 70 ; 0.202 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.134 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION 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): 6805 ; 0.463 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10215 ; 0.765 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4310 ; 0.929 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3723 ; 1.408 ; 4.500
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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 195
REMARK 3 RESIDUE RANGE : A 283 A 298
REMARK 3 RESIDUE RANGE : A 358 A 381
REMARK 3 ORIGIN FOR THE GROUP (A): -79.8459 -12.8102 -58.4623
REMARK 3 T TENSOR
REMARK 3 T11: -0.2490 T22: -0.2598
REMARK 3 T33: -0.2021 T12: -0.0111
REMARK 3 T13: -0.0186 T23: -0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 2.7182 L22: 4.6256
REMARK 3 L33: 3.5903 L12: -1.9803
REMARK 3 L13: -2.0786 L23: 2.8152
REMARK 3 S TENSOR
REMARK 3 S11: -0.0056 S12: -0.0288 S13: -0.0970
REMARK 3 S21: -0.1592 S22: 0.1647 S23: -0.1555
REMARK 3 S31: -0.0543 S32: 0.2639 S33: -0.1591
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 196 A 282
REMARK 3 RESIDUE RANGE : A 299 A 357
REMARK 3 RESIDUE RANGE : A 382 A 431
REMARK 3 ORIGIN FOR THE GROUP (A): -62.2106 -8.9218 -35.4820
REMARK 3 T TENSOR
REMARK 3 T11: -0.2034 T22: -0.3071
REMARK 3 T33: -0.1848 T12: -0.0453
REMARK 3 T13: -0.0482 T23: -0.0082
REMARK 3 L TENSOR
REMARK 3 L11: 6.5850 L22: 2.6028
REMARK 3 L33: 2.0823 L12: -1.4851
REMARK 3 L13: 1.4003 L23: 0.1264
REMARK 3 S TENSOR
REMARK 3 S11: 0.1471 S12: -0.0394 S13: -0.3622
REMARK 3 S21: -0.0105 S22: -0.0641 S23: 0.0111
REMARK 3 S31: 0.1163 S32: -0.0950 S33: -0.0830
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 432 A 858
REMARK 3 ORIGIN FOR THE GROUP (A): -21.5382 -1.2269 -14.6090
REMARK 3 T TENSOR
REMARK 3 T11: -0.1634 T22: -0.1782
REMARK 3 T33: -0.1878 T12: 0.0773
REMARK 3 T13: -0.1122 T23: 0.1253
REMARK 3 L TENSOR
REMARK 3 L11: 4.4309 L22: 2.3867
REMARK 3 L33: 1.5785 L12: 1.6268
REMARK 3 L13: 0.8520 L23: -0.0532
REMARK 3 S TENSOR
REMARK 3 S11: 0.4190 S12: -0.3345 S13: -0.6083
REMARK 3 S21: 0.5141 S22: -0.2007 S23: -0.4297
REMARK 3 S31: 0.1174 S32: 0.2110 S33: -0.2183
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 859 A 964
REMARK 3 ORIGIN FOR THE GROUP (A): -45.0259 19.2204 -25.7638
REMARK 3 T TENSOR
REMARK 3 T11: 0.1245 T22: 0.2074
REMARK 3 T33: 0.4929 T12: -0.0655
REMARK 3 T13: -0.1458 T23: 0.0567
REMARK 3 L TENSOR
REMARK 3 L11: 0.8527 L22: 11.6508
REMARK 3 L33: 5.1314 L12: -3.1433
REMARK 3 L13: 1.1175 L23: -3.6355
REMARK 3 S TENSOR
REMARK 3 S11: -0.4399 S12: -0.2618 S13: 0.8731
REMARK 3 S21: 0.3485 S22: -0.0730 S23: -1.0340
REMARK 3 S31: -1.1357 S32: 0.4433 S33: 0.5129
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 965 A 1045
REMARK 3 ORIGIN FOR THE GROUP (A): -61.3073 18.5036 -52.4300
REMARK 3 T TENSOR
REMARK 3 T11: 0.7253 T22: 0.0841
REMARK 3 T33: 0.2924 T12: -0.1495
REMARK 3 T13: 0.3559 T23: -0.1012
REMARK 3 L TENSOR
REMARK 3 L11: 3.1789 L22: 14.0407
REMARK 3 L33: 6.1160 L12: 3.5573
REMARK 3 L13: 2.2295 L23: 5.5249
REMARK 3 S TENSOR
REMARK 3 S11: -1.0388 S12: 1.0971 S13: -0.5596
REMARK 3 S21: -2.0172 S22: 0.7840 S23: -0.2472
REMARK 3 S31: 0.5667 S32: 0.5586 S33: 0.2548
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1046 A 1270
REMARK 3 ORIGIN FOR THE GROUP (A): -38.7696 3.8963 -75.8345
REMARK 3 T TENSOR
REMARK 3 T11: 0.8566 T22: 0.9837
REMARK 3 T33: 0.2602 T12: -0.1335
REMARK 3 T13: 0.3925 T23: 0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 7.1353 L22: 5.1593
REMARK 3 L33: 3.3493 L12: -1.1456
REMARK 3 L13: -2.3668 L23: 1.6868
REMARK 3 S TENSOR
REMARK 3 S11: 0.3279 S12: -0.6751 S13: 0.5834
REMARK 3 S21: 0.7886 S22: -0.1175 S23: 0.7345
REMARK 3 S31: -0.2381 S32: -0.4767 S33: -0.2104
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1271 A 1290
REMARK 3 ORIGIN FOR THE GROUP (A): -10.2275 8.1815 -64.2136
REMARK 3 T TENSOR
REMARK 3 T11: 0.0770 T22: 0.1214
REMARK 3 T33: 0.1165 T12: 0.1597
REMARK 3 T13: 0.0937 T23: 0.2790
REMARK 3 L TENSOR
REMARK 3 L11: 8.6683 L22: 16.2944
REMARK 3 L33: 30.3690 L12: 1.0708
REMARK 3 L13: -2.8439 L23: 0.5008
REMARK 3 S TENSOR
REMARK 3 S11: -0.5599 S12: 0.8805 S13: 0.9327
REMARK 3 S21: -0.7583 S22: -0.4055 S23: 0.9164
REMARK 3 S31: -0.8094 S32: -0.8210 S33: 0.9654
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. RESIDUES 1156-1160, 1175-1181 AND 1202-1206
REMARK 3 ARE DISORDERED AND MISSING IN THE SRFA-C STRUCTURE.
REMARK 4
REMARK 4 2VSQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-APR-08.
REMARK 100 THE PDBE ID CODE IS EBI-36028.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUL-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y ; Y
REMARK 200 RADIATION SOURCE : ESRF ; SLS
REMARK 200 BEAMLINE : ID14-2 ; X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M ; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9330 ; 0.9794, 0.9792,
REMARK 200 0.9717
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45564
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.60
REMARK 200 RESOLUTION RANGE LOW (A) : 82.50
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 2.2
REMARK 200 R MERGE (I) : 0.04
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.90
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) : 2.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 68.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.48
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.00
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRIES 1AMU AND 2JGP
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MGCL2, 0.05 M HEPES (PH
REMARK 280 7.5), 15 % (W/V) PEG 2000
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,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 53.28100
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, SER 1003 TO ALA
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 ASP A 1156
REMARK 465 LEU A 1157
REMARK 465 ASP A 1158
REMARK 465 GLY A 1159
REMARK 465 ARG A 1160
REMARK 465 ASP A 1175
REMARK 465 ASN A 1176
REMARK 465 GLU A 1177
REMARK 465 ALA A 1178
REMARK 465 LEU A 1179
REMARK 465 ASN A 1180
REMARK 465 SER A 1181
REMARK 465 LEU A 1202
REMARK 465 ILE A 1203
REMARK 465 SER A 1204
REMARK 465 THR A 1205
REMARK 465 GLY A 1206
REMARK 465 GLU A 1291
REMARK 465 ASP A 1292
REMARK 465 LEU A 1293
REMARK 465 ASN A 1294
REMARK 465 SER A 1295
REMARK 465 ALA A 1296
REMARK 465 VAL A 1297
REMARK 465 ASP A 1298
REMARK 465 HIS A 1299
REMARK 465 HIS A 1300
REMARK 465 HIS A 1301
REMARK 465 HIS A 1302
REMARK 465 HIS A 1303
REMARK 465 HIS A 1304
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 LYS A 6 CG CD CE NZ
REMARK 470 LYS A 223 CG CD CE NZ
REMARK 470 LYS A 464 CG CD CE NZ
REMARK 470 LYS A 471 CG CD CE NZ
REMARK 470 GLU A 498 CG CD OE1 OE2
REMARK 470 GLU A 550 CG CD OE1 OE2
REMARK 470 GLN A 574 CG CD OE1 NE2
REMARK 470 LYS A 825 CG CD CE NZ
REMARK 470 LYS A 878 CG CD CE NZ
REMARK 470 ARG A 910 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 919 CG CD CE NZ
REMARK 470 LYS A 951 CG CD CE NZ
REMARK 470 GLU A 972 CG CD OE1 OE2
REMARK 470 LYS A1014 CG CD CE NZ
REMARK 470 LYS A1015 CG CD CE NZ
REMARK 470 LYS A1131 CG CD CE NZ
REMARK 470 GLU A1135 CB CG CD OE1 OE2
REMARK 470 VAL A1237 CG1 CG2
REMARK 470 GLU A1261 CB CG CD OE1 OE2
REMARK 470 GLU A1290 CG CD OE1 OE2
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 GLN A 596 CD GLN A 596 NE2 0.324
REMARK 500 GLN A 596 CD GLN A 596 OE1 0.191
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 GLN A 596 CG - CD - NE2 ANGL. DEV. = 16.0 DEGREES
REMARK 500 GLN A 596 CG - CD - OE1 ANGL. DEV. = -27.0 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 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 HIS A 72 -30.15 -144.82
REMARK 500 LYS A 74 88.18 70.67
REMARK 500 VAL A 75 137.42 171.56
REMARK 500 ARG A 123 -42.19 -149.65
REMARK 500 PRO A 126 32.39 -74.72
REMARK 500 GLN A 222 164.40 -43.10
REMARK 500 LYS A 223 146.66 -30.53
REMARK 500 ALA A 286 -38.40 -38.01
REMARK 500 PHE A 298 -44.80 -134.72
REMARK 500 ALA A 343 -32.27 -165.32
REMARK 500 ASP A 344 -29.51 90.39
REMARK 500 PRO A 346 -87.11 -55.48
REMARK 500 LYS A 347 83.62 -64.09
REMARK 500 ASN A 357 -66.40 -27.33
REMARK 500 ASN A 365 49.13 -97.82
REMARK 500 GLU A 367 86.84 67.37
REMARK 500 SER A 384 97.48 -69.69
REMARK 500 ALA A 460 -77.90 -67.17
REMARK 500 HIS A 461 129.15 -16.97
REMARK 500 THR A 463 124.61 87.80
REMARK 500 LYS A 464 138.27 -178.48
REMARK 500 ASN A 477 80.74 -163.61
REMARK 500 ALA A 562 99.40 -57.33
REMARK 500 THR A 567 -148.98 -133.11
REMARK 500 HIS A 568 -57.80 -135.67
REMARK 500 GLN A 569 -42.17 111.35
REMARK 500 GLU A 573 38.53 -81.10
REMARK 500 ALA A 575 -76.56 -61.56
REMARK 500 ALA A 576 -117.38 46.31
REMARK 500 TYR A 580 102.64 -176.38
REMARK 500 ALA A 601 47.19 -89.48
REMARK 500 THR A 602 96.57 -69.09
REMARK 500 THR A 618 82.57 -60.81
REMARK 500 MET A 642 177.48 -11.41
REMARK 500 THR A 759 84.54 67.45
REMARK 500 VAL A 760 -75.15 72.01
REMARK 500 HIS A 768 -61.75 -128.71
REMARK 500 SER A 775 -86.76 -74.10
REMARK 500 LYS A 834 84.11 -161.88
REMARK 500 VAL A 886 -47.66 -140.60
REMARK 500 LYS A 887 -109.24 71.21
REMARK 500 HIS A 896 -154.81 -99.99
REMARK 500 GLU A 897 69.16 -65.63
REMARK 500 ASN A 909 -61.60 -152.94
REMARK 500 ARG A 910 -120.70 133.24
REMARK 500 LYS A 923 -58.03 -23.87
REMARK 500 LEU A 943 -62.80 -128.46
REMARK 500 THR A 944 97.23 74.18
REMARK 500 THR A 945 -139.87 46.90
REMARK 500 LYS A 951 96.72 -57.53
REMARK 500 LEU A 953 78.52 -63.88
REMARK 500 PRO A 969 126.21 -30.26
REMARK 500 GLN A 989 65.59 62.62
REMARK 500 ALA A1003 -71.28 -46.09
REMARK 500 LYS A1015 -104.75 113.48
REMARK 500 GLU A1016 84.57 -32.64
REMARK 500 ILE A1019 25.13 -157.80
REMARK 500 ASP A1020 129.61 76.43
REMARK 500 LEU A1021 143.82 -170.09
REMARK 500 PRO A1022 123.79 -26.78
REMARK 500 LEU A1025 34.07 -159.57
REMARK 500 ASP A1056 36.01 -87.97
REMARK 500 GLN A1057 -104.73 -103.93
REMARK 500 GLU A1058 -73.39 -177.28
REMARK 500 GLN A1059 104.65 -58.72
REMARK 500 ASP A1096 37.27 -93.05
REMARK 500 GLN A1109 107.02 -160.11
REMARK 500 SER A1120 -140.37 63.98
REMARK 500 GLU A1128 69.34 -69.38
REMARK 500 ALA A1129 -57.48 -177.59
REMARK 500 VAL A1154 -63.08 -139.36
REMARK 500 ALA A1233 4.40 -64.91
REMARK 500 LEU A1251 47.61 -107.64
REMARK 500 THR A1269 -68.20 46.42
REMARK 500 GLN A1270 -53.17 90.40
REMARK 500 VAL A1272 74.47 27.65
REMARK 500 SER A1289 89.75 -57.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU A 462 THR A 463 134.86
REMARK 500 THR A 567 HIS A 568 -142.54
REMARK 500 ILE A 587 ASP A 588 147.66
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 600
REMARK 600 HETEROGEN
REMARK 600 L-LEUCINE (LEU): L-LEUCINE IS BOUND TO THE SUBSTRATE
REMARK 600 BINDING SITE OF THE A DOMAIN OF SRFA-C.
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LEU A2291
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A2292
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JMK RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS FOR THE CYCLIZATION OF THE
REMARK 900 LIPOPEPTIDEANTIBIOTIC SURFACTIN BY THE
REMARK 900 THIOESTERASE DOMAIN SRFTE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 PLEASE NOTE THAT THE GENBANK ENTRY CONTAINS THE SEQUENCE
REMARK 999 OF B. SUBTILIS STRAIN 168, WHEREAS THE RECOMBINANT PROTEIN'
REMARK 999 S SOURCE IS B. SUBTILIS STRAIN ATCC 21332. THEREFORE THERE
REMARK 999 ARE THE FOLLOWING AMINO ACID EXCHANGES COMPARED TO THE
REMARK 999 AFOREMENTIONED GENBANK ENTRY. P26A, T33S, L235P. RESIDUES
REMARK 999 1010-1014, VPHQQ, ARE REPLACED BY ASRIKK DUE TO A FRAME
REMARK 999 SHIFT. THE PROTEIN CONTAINS A S1003A POINT MUTATION AND
REMARK 999 29 AMINO ACIDS THAT ARE DERIVED FROM THE VECTOR'S MULTIPLE
REMARK 999 CLONING SITE, C-MYC EPITOPE SEQUENCE, A LINKER AND A HEXA-
REMARK 999 HISTIDINE TAG.
DBREF 2VSQ A 1 1009 UNP Q08787 SRFAC_BACSU 1 1009
DBREF 2VSQ A 1010 1015 PDB 2VSQ 2VSQ 1010 1015
DBREF 2VSQ A 1016 1275 UNP Q08787 SRFAC_BACSU 1015 1274
DBREF 2VSQ A 1276 1304 PDB 2VSQ 2VSQ 1276 1304
SEQADV 2VSQ ALA A 26 UNP Q08787 PRO 26 CONFLICT SEE REMARK 999
SEQADV 2VSQ SER A 33 UNP Q08787 THR 33 CONFLICT SEE REMARK 999
SEQADV 2VSQ PRO A 235 UNP Q08787 LEU 235 CONFLICT SEE REMARK 999
SEQADV 2VSQ ALA A 1003 UNP Q08787 SER 1003 ENGINEERED MUTATION
SEQADV 2VSQ ILE A 1223 UNP Q08787 MET 1222 CONFLICT
SEQADV 2VSQ MET A 1240 UNP Q08787 ASN 1239 CONFLICT
SEQRES 1 A 1304 MET SER GLN PHE SER LYS ASP GLN VAL GLN ASP MET TYR
SEQRES 2 A 1304 TYR LEU SER PRO MET GLN GLU GLY MET LEU PHE HIS ALA
SEQRES 3 A 1304 ILE LEU ASN PRO GLY GLN SER PHE TYR LEU GLU GLN ILE
SEQRES 4 A 1304 THR MET LYS VAL LYS GLY SER LEU ASN ILE LYS CYS LEU
SEQRES 5 A 1304 GLU GLU SER MET ASN VAL ILE MET ASP ARG TYR ASP VAL
SEQRES 6 A 1304 PHE ARG THR VAL PHE ILE HIS GLU LYS VAL LYS ARG PRO
SEQRES 7 A 1304 VAL GLN VAL VAL LEU LYS LYS ARG GLN PHE HIS ILE GLU
SEQRES 8 A 1304 GLU ILE ASP LEU THR HIS LEU THR GLY SER GLU GLN THR
SEQRES 9 A 1304 ALA LYS ILE ASN GLU TYR LYS GLU GLN ASP LYS ILE ARG
SEQRES 10 A 1304 GLY PHE ASP LEU THR ARG ASP ILE PRO MET ARG ALA ALA
SEQRES 11 A 1304 ILE PHE LYS LYS ALA GLU GLU SER PHE GLU TRP VAL TRP
SEQRES 12 A 1304 SER TYR HIS HIS ILE ILE LEU ASP GLY TRP CYS PHE GLY
SEQRES 13 A 1304 ILE VAL VAL GLN ASP LEU PHE LYS VAL TYR ASN ALA LEU
SEQRES 14 A 1304 ARG GLU GLN LYS PRO TYR SER LEU PRO PRO VAL LYS PRO
SEQRES 15 A 1304 TYR LYS ASP TYR ILE LYS TRP LEU GLU LYS GLN ASP LYS
SEQRES 16 A 1304 GLN ALA SER LEU ARG TYR TRP ARG GLU TYR LEU GLU GLY
SEQRES 17 A 1304 PHE GLU GLY GLN THR THR PHE ALA GLU GLN ARG LYS LYS
SEQRES 18 A 1304 GLN LYS ASP GLY TYR GLU PRO LYS GLU LEU LEU PHE SER
SEQRES 19 A 1304 PRO SER GLU ALA GLU THR LYS ALA PHE THR GLU LEU ALA
SEQRES 20 A 1304 LYS SER GLN HIS THR THR LEU SER THR ALA LEU GLN ALA
SEQRES 21 A 1304 VAL TRP SER VAL LEU ILE SER ARG TYR GLN GLN SER GLY
SEQRES 22 A 1304 ASP LEU ALA PHE GLY THR VAL VAL SER GLY ARG PRO ALA
SEQRES 23 A 1304 GLU ILE LYS GLY VAL GLU HIS MET VAL GLY LEU PHE ILE
SEQRES 24 A 1304 ASN VAL VAL PRO ARG ARG VAL LYS LEU SER GLU GLY ILE
SEQRES 25 A 1304 THR PHE ASN GLY LEU LEU LYS ARG LEU GLN GLU GLN SER
SEQRES 26 A 1304 LEU GLN SER GLU PRO HIS GLN TYR VAL PRO LEU TYR ASP
SEQRES 27 A 1304 ILE GLN SER GLN ALA ASP GLN PRO LYS LEU ILE ASP HIS
SEQRES 28 A 1304 ILE ILE VAL PHE GLU ASN TYR PRO LEU GLN ASP ALA LYS
SEQRES 29 A 1304 ASN GLU GLU SER SER GLU ASN GLY PHE ASP MET VAL ASP
SEQRES 30 A 1304 VAL HIS VAL PHE GLU LYS SER ASN TYR ASP LEU ASN LEU
SEQRES 31 A 1304 MET ALA SER PRO GLY ASP GLU MET LEU ILE LYS LEU ALA
SEQRES 32 A 1304 TYR ASN GLU ASN VAL PHE ASP GLU ALA PHE ILE LEU ARG
SEQRES 33 A 1304 LEU LYS SER GLN LEU LEU THR ALA ILE GLN GLN LEU ILE
SEQRES 34 A 1304 GLN ASN PRO ASP GLN PRO VAL SER THR ILE ASN LEU VAL
SEQRES 35 A 1304 ASP ASP ARG GLU ARG GLU PHE LEU LEU THR GLY LEU ASN
SEQRES 36 A 1304 PRO PRO ALA GLN ALA HIS GLU THR LYS PRO LEU THR TYR
SEQRES 37 A 1304 TRP PHE LYS GLU ALA VAL ASN ALA ASN PRO ASP ALA PRO
SEQRES 38 A 1304 ALA LEU THR TYR SER GLY GLN THR LEU SER TYR ARG GLU
SEQRES 39 A 1304 LEU ASP GLU GLU ALA ASN ARG ILE ALA ARG ARG LEU GLN
SEQRES 40 A 1304 LYS HIS GLY ALA GLY LYS GLY SER VAL VAL ALA LEU TYR
SEQRES 41 A 1304 THR LYS ARG SER LEU GLU LEU VAL ILE GLY ILE LEU GLY
SEQRES 42 A 1304 VAL LEU LYS ALA GLY ALA ALA TYR LEU PRO VAL ASP PRO
SEQRES 43 A 1304 LYS LEU PRO GLU ASP ARG ILE SER TYR MET LEU ALA ASP
SEQRES 44 A 1304 SER ALA ALA ALA CYS LEU LEU THR HIS GLN GLU MET LYS
SEQRES 45 A 1304 GLU GLN ALA ALA GLU LEU PRO TYR THR GLY THR THR LEU
SEQRES 46 A 1304 PHE ILE ASP ASP GLN THR ARG PHE GLU GLU GLN ALA SER
SEQRES 47 A 1304 ASP PRO ALA THR ALA ILE ASP PRO ASN ASP PRO ALA TYR
SEQRES 48 A 1304 ILE MET TYR THR SER GLY THR THR GLY LYS PRO LYS GLY
SEQRES 49 A 1304 ASN ILE THR THR HIS ALA ASN ILE GLN GLY LEU VAL LYS
SEQRES 50 A 1304 HIS VAL ASP TYR MET ALA PHE SER ASP GLN ASP THR PHE
SEQRES 51 A 1304 LEU SER VAL SER ASN TYR ALA PHE ASP ALA PHE THR PHE
SEQRES 52 A 1304 ASP PHE TYR ALA SER MET LEU ASN ALA ALA ARG LEU ILE
SEQRES 53 A 1304 ILE ALA ASP GLU HIS THR LEU LEU ASP THR GLU ARG LEU
SEQRES 54 A 1304 THR ASP LEU ILE LEU GLN GLU ASN VAL ASN VAL MET PHE
SEQRES 55 A 1304 ALA THR THR ALA LEU PHE ASN LEU LEU THR ASP ALA GLY
SEQRES 56 A 1304 GLU ASP TRP MET LYS GLY LEU ARG CYS ILE LEU PHE GLY
SEQRES 57 A 1304 GLY GLU ARG ALA SER VAL PRO HIS VAL ARG LYS ALA LEU
SEQRES 58 A 1304 ARG ILE MET GLY PRO GLY LYS LEU ILE ASN CYS TYR GLY
SEQRES 59 A 1304 PRO THR GLU GLY THR VAL PHE ALA THR ALA HIS VAL VAL
SEQRES 60 A 1304 HIS ASP LEU PRO ASP SER ILE SER SER LEU PRO ILE GLY
SEQRES 61 A 1304 LYS PRO ILE SER ASN ALA SER VAL TYR ILE LEU ASN GLU
SEQRES 62 A 1304 GLN SER GLN LEU GLN PRO PHE GLY ALA VAL GLY GLU LEU
SEQRES 63 A 1304 CYS ILE SER GLY MET GLY VAL SER LYS GLY TYR VAL ASN
SEQRES 64 A 1304 ARG ALA ASP LEU THR LYS GLU LYS PHE ILE GLU ASN PRO
SEQRES 65 A 1304 PHE LYS PRO GLY GLU THR LEU TYR ARG THR GLY ASP LEU
SEQRES 66 A 1304 ALA ARG TRP LEU PRO ASP GLY THR ILE GLU TYR ALA GLY
SEQRES 67 A 1304 ARG ILE ASP ASP GLN VAL LYS ILE ARG GLY HIS ARG ILE
SEQRES 68 A 1304 GLU LEU GLU GLU ILE GLU LYS GLN LEU GLN GLU TYR PRO
SEQRES 69 A 1304 GLY VAL LYS ASP ALA VAL VAL VAL ALA ASP ARG HIS GLU
SEQRES 70 A 1304 SER GLY ASP ALA SER ILE ASN ALA TYR LEU VAL ASN ARG
SEQRES 71 A 1304 THR GLN LEU SER ALA GLU ASP VAL LYS ALA HIS LEU LYS
SEQRES 72 A 1304 LYS GLN LEU PRO ALA TYR MET VAL PRO GLN THR PHE THR
SEQRES 73 A 1304 PHE LEU ASP GLU LEU PRO LEU THR THR ASN GLY LYS VAL
SEQRES 74 A 1304 ASN LYS ARG LEU LEU PRO LYS PRO ASP GLN ASP GLN LEU
SEQRES 75 A 1304 ALA GLU GLU TRP ILE GLY PRO ARG ASN GLU MET GLU GLU
SEQRES 76 A 1304 THR ILE ALA GLN ILE TRP SER GLU VAL LEU GLY ARG LYS
SEQRES 77 A 1304 GLN ILE GLY ILE HIS ASP ASP PHE PHE ALA LEU GLY GLY
SEQRES 78 A 1304 HIS ALA LEU LYS ALA MET THR ALA ALA SER ARG ILE LYS
SEQRES 79 A 1304 LYS GLU LEU GLY ILE ASP LEU PRO VAL LYS LEU LEU PHE
SEQRES 80 A 1304 GLU ALA PRO THR ILE ALA GLY ILE SER ALA TYR LEU LYS
SEQRES 81 A 1304 ASN GLY GLY SER ASP GLY LEU GLN ASP VAL THR ILE MET
SEQRES 82 A 1304 ASN GLN ASP GLN GLU GLN ILE ILE PHE ALA PHE PRO PRO
SEQRES 83 A 1304 VAL LEU GLY TYR GLY LEU MET TYR GLN ASN LEU SER SER
SEQRES 84 A 1304 ARG LEU PRO SER TYR LYS LEU CYS ALA PHE ASP PHE ILE
SEQRES 85 A 1304 GLU GLU GLU ASP ARG LEU ASP ARG TYR ALA ASP LEU ILE
SEQRES 86 A 1304 GLN LYS LEU GLN PRO GLU GLY PRO LEU THR LEU PHE GLY
SEQRES 87 A 1304 TYR SER ALA GLY CYS SER LEU ALA PHE GLU ALA ALA LYS
SEQRES 88 A 1304 LYS LEU GLU GLU GLN GLY ARG ILE VAL GLN ARG ILE ILE
SEQRES 89 A 1304 MET VAL ASP SER TYR LYS LYS GLN GLY VAL SER ASP LEU
SEQRES 90 A 1304 ASP GLY ARG THR VAL GLU SER ASP VAL GLU ALA LEU MET
SEQRES 91 A 1304 ASN VAL ASN ARG ASP ASN GLU ALA LEU ASN SER GLU ALA
SEQRES 92 A 1304 VAL LYS HIS GLY LEU LYS GLN LYS THR HIS ALA PHE TYR
SEQRES 93 A 1304 SER TYR TYR VAL ASN LEU ILE SER THR GLY GLN VAL LYS
SEQRES 94 A 1304 ALA ASP ILE ASP LEU LEU THR SER GLY ALA ASP PHE ASP
SEQRES 95 A 1304 ILE PRO GLU TRP LEU ALA SER TRP GLU GLU ALA THR THR
SEQRES 96 A 1304 GLY VAL TYR ARG MET LYS ARG GLY PHE GLY THR HIS ALA
SEQRES 97 A 1304 GLU MET LEU GLN GLY GLU THR LEU ASP ARG ASN ALA GLU
SEQRES 98 A 1304 ILE LEU LEU GLU PHE LEU ASN THR GLN THR VAL THR VAL
SEQRES 99 A 1304 SER LYS GLY GLU PHE GLU ALA TYR VAL GLU GLN LYS LEU
SEQRES 100 A 1304 ILE SER GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS
SEQRES 101 A 1304 HIS HIS HIS HIS
HET LEU A2291 9
HET SO4 A2292 5
HETNAM SO4 SULFATE ION
HETNAM LEU LEUCINE
FORMUL 2 SO4 O4 S 2-
FORMUL 3 LEU C6 H13 N O2
FORMUL 4 HOH *39(H2 O1)
HELIX 1 1 SER A 5 ASP A 7 5 3
HELIX 2 2 SER A 16 ASN A 29 1 14
HELIX 3 3 ASN A 48 TYR A 63 1 16
HELIX 4 4 ASP A 64 PHE A 66 5 3
HELIX 5 5 THR A 99 GLY A 118 1 20
HELIX 6 6 ILE A 148 LEU A 150 5 3
HELIX 7 7 ASP A 151 GLU A 171 1 21
HELIX 8 8 TYR A 183 LYS A 192 1 10
HELIX 9 9 ASP A 194 GLU A 207 1 14
HELIX 10 10 SER A 236 GLN A 250 1 15
HELIX 11 11 THR A 253 GLN A 271 1 19
HELIX 12 12 GLY A 290 MET A 294 5 5
HELIX 13 13 THR A 313 GLU A 329 1 17
HELIX 14 14 PRO A 330 GLN A 332 5 3
HELIX 15 15 PRO A 335 GLN A 342 1 8
HELIX 16 16 PRO A 359 LYS A 364 1 6
HELIX 17 17 GLU A 367 GLY A 372 1 6
HELIX 18 18 ASP A 410 ASN A 431 1 22
HELIX 19 19 VAL A 436 ILE A 439 5 4
HELIX 20 20 ASP A 443 THR A 452 1 10
HELIX 21 21 PRO A 465 ASN A 477 1 13
HELIX 22 22 TYR A 492 HIS A 509 1 18
HELIX 23 23 SER A 524 ALA A 537 1 14
HELIX 24 24 PRO A 549 ALA A 561 1 13
HELIX 25 25 ASP A 589 GLU A 595 5 7
HELIX 26 26 HIS A 629 LYS A 637 1 9
HELIX 27 27 ASP A 659 LEU A 670 1 12
HELIX 28 28 ASP A 679 LEU A 683 5 5
HELIX 29 29 ASP A 685 ASN A 697 1 13
HELIX 30 30 THR A 705 GLY A 715 1 11
HELIX 31 31 GLU A 716 GLY A 721 1 6
HELIX 32 32 SER A 733 GLY A 745 1 13
HELIX 33 33 PRO A 755 THR A 759 5 5
HELIX 34 34 ARG A 820 LYS A 827 1 8
HELIX 35 35 LEU A 873 TYR A 883 1 11
HELIX 36 36 SER A 914 LEU A 926 1 13
HELIX 37 37 PRO A 927 VAL A 931 5 5
HELIX 38 38 ASP A 958 ALA A 963 5 6
HELIX 39 39 ASN A 971 GLY A 986 1 16
HELIX 40 40 HIS A 1002 ILE A 1013 1 12
HELIX 41 41 THR A 1031 GLY A 1042 1 12
HELIX 42 42 GLY A 1071 MET A 1073 5 3
HELIX 43 43 TYR A 1074 SER A 1079 1 6
HELIX 44 44 ASP A 1096 GLN A 1109 1 14
HELIX 45 45 ALA A 1121 GLN A 1136 1 16
HELIX 46 46 THR A 1161 ASN A 1171 1 11
HELIX 47 47 LYS A 1185 GLY A 1187 5 3
HELIX 48 48 LEU A 1188 ASN A 1201 1 14
HELIX 49 49 ALA A 1248 LEU A 1251 5 4
HELIX 50 50 GLN A 1252 THR A 1269 1 18
HELIX 51 51 SER A 1275 SER A 1289 1 15
SHEET 1 AA 3 VAL A 9 TYR A 14 0
SHEET 2 AA 3 VAL A 79 LEU A 83 -1 O GLN A 80 N TYR A 13
SHEET 3 AA 3 THR A 68 ILE A 71 -1 O VAL A 69 N VAL A 81
SHEET 1 AB 5 ILE A 90 ASP A 94 0
SHEET 2 AB 5 MET A 127 ALA A 135 1 O ALA A 129 N GLU A 91
SHEET 3 AB 5 SER A 138 HIS A 146 -1 O SER A 138 N LYS A 134
SHEET 4 AB 5 LEU A 36 GLY A 45 -1 O GLU A 37 N TYR A 145
SHEET 5 AB 5 PHE A 373 VAL A 380 -1 O ASP A 374 N LYS A 44
SHEET 1 AC 6 PRO A 228 PHE A 233 0
SHEET 2 AC 6 LEU A 399 ASN A 405 -1 O ILE A 400 N PHE A 233
SHEET 3 AC 6 LEU A 388 SER A 393 -1 O ASN A 389 N ALA A 403
SHEET 4 AC 6 ILE A 352 PHE A 355 1 O ILE A 352 N LEU A 390
SHEET 5 AC 6 ASP A 274 VAL A 281 1 O GLY A 278 N ILE A 353
SHEET 6 AC 6 ASN A 300 LYS A 307 -1 O ASN A 300 N VAL A 281
SHEET 1 AD 9 THR A 489 SER A 491 0
SHEET 2 AD 9 PRO A 481 THR A 484 -1 N ALA A 482 O LEU A 490
SHEET 3 AD 9 ARG A 674 ILE A 677 1 O LEU A 675 N THR A 484
SHEET 4 AD 9 THR A 649 SER A 652 1 O PHE A 650 N ILE A 676
SHEET 5 AD 9 VAL A 700 THR A 704 1 O VAL A 700 N LEU A 651
SHEET 6 AD 9 CYS A 724 GLY A 728 1 O CYS A 724 N MET A 701
SHEET 7 AD 9 LEU A 749 TYR A 753 1 O ILE A 750 N PHE A 727
SHEET 8 AD 9 THR A 763 VAL A 766 -1 O THR A 763 N TYR A 753
SHEET 9 AD 9 LYS A 781 PRO A 782 -1 O LYS A 781 N ALA A 764
SHEET 1 AE 4 ALA A 540 PRO A 543 0
SHEET 2 AE 4 VAL A 516 LEU A 519 1 O VAL A 517 N LEU A 542
SHEET 3 AE 4 CYS A 564 THR A 567 1 O CYS A 564 N ALA A 518
SHEET 4 AE 4 THR A 583 PHE A 586 1 O THR A 583 N LEU A 565
SHEET 1 AF 2 PRO A 609 THR A 615 0
SHEET 2 AF 2 LYS A 623 THR A 628 -1 O LYS A 623 N THR A 615
SHEET 1 AG 4 ALA A 786 LEU A 791 0
SHEET 2 AG 4 GLY A 804 GLY A 810 -1 O GLU A 805 N LEU A 791
SHEET 3 AG 4 THR A 838 TRP A 848 -1 O TYR A 840 N ILE A 808
SHEET 4 AG 4 PHE A 828 GLU A 830 -1 O ILE A 829 N LEU A 839
SHEET 1 AH 4 ALA A 786 LEU A 791 0
SHEET 2 AH 4 GLY A 804 GLY A 810 -1 O GLU A 805 N LEU A 791
SHEET 3 AH 4 THR A 838 TRP A 848 -1 O TYR A 840 N ILE A 808
SHEET 4 AH 4 ILE A 854 ARG A 859 -1 O GLU A 855 N ARG A 847
SHEET 1 AI 2 GLN A 863 ILE A 866 0
SHEET 2 AI 2 HIS A 869 GLU A 872 -1 O HIS A 869 N ILE A 866
SHEET 1 AJ 3 ASP A 888 ASP A 894 0
SHEET 2 AJ 3 SER A 902 VAL A 908 -1 O SER A 902 N ASP A 894
SHEET 3 AJ 3 THR A 934 LEU A 938 1 O THR A 934 N ALA A 905
SHEET 1 AK 3 THR A1051 MET A1053 0
SHEET 2 AK 3 LYS A1085 ALA A1088 -1 O LEU A1086 N MET A1053
SHEET 3 AK 3 ILE A1060 PHE A1062 1 O ILE A1061 N CYS A1087
SHEET 1 AL 4 LEU A1114 TYR A1119 0
SHEET 2 AL 4 VAL A1140 VAL A1146 1 N GLN A1141 O LEU A1114
SHEET 3 AL 4 ASP A1211 THR A1216 1 O ASP A1211 N ILE A1143
SHEET 4 AL 4 MET A1240 ARG A1242 1 O LYS A1241 N THR A1216
SHEET 1 AM 2 LYS A1150 LYS A1151 0
SHEET 2 AM 2 LEU A1227 ALA A1228 -1 O ALA A1228 N LYS A1150
CISPEP 1 LEU A 578 PRO A 579 0 -15.36
SITE 1 AC1 7 ASP A 659 ALA A 660 PHE A 702 GLY A 728
SITE 2 AC1 7 GLY A 729 CYS A 752 VAL A 760
SITE 1 AC2 4 GLN A 193 GLU A 287 ASN A 697 GLY A 721
CRYST1 83.106 106.562 92.401 90.00 97.35 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 0.012033 0.000000 0.001552 0.00000
SCALE2 0.000000 0.009384 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010912 0.00000
TER 10057 GLU A1290
MASTER 614 0 2 51 51 0 3 610109 1 14 101
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