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HEADER HYDROLASE 03-JAN-06 2CBG
TITLE CRYSTAL STRUCTURE OF THE PMSF-INHIBITED THIOESTERASE DOMAIN
TITLE 2 OF THE FENGYCIN BIOSYNTHESIS CLUSTER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FENGYCIN SYNTHETASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: THIOESTERASE DOMAIN, RESIDUES 1043-1274;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: RECOMBINANT FRAGMENT OF THE NRPS SYNTHETASE
COMPND 7 FENB (Q1043-H1274), INHIBITED FORM GENERATED BY CRYSTALS
COMPND 8 SOAKED IN THE PRESENCE OF PMSF
SOURCE MOL_ID: 1;
SOURCE 2 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 3 EXPRESSION_SYSTEM_STRAIN: M15;
SOURCE 4 EXPRESSION_SYSTEM_VECTOR: PQE-60;
SOURCE 5 EXPRESSION_SYSTEM_VARIANT: PREP4;
SOURCE 6 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 7 STRAIN: F29-3
KEYWDS FENGYCIN THIOESTERASE, NON-RIBOSOMAL PEPTIDE SYNTHESIS,
KEYWDS 2 ALPHA/BETA-HYDROLASE, PHOSPHOPANTETHEINE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.SAMEL,M.A.MARAHIEL,L.-O.ESSEN
REVDAT 1 06-MAR-07 2CBG 0
JRNL AUTH S.SAMEL,B.WAGNER,M.A.MARAHIEL,L.-O.ESSEN
JRNL TITL THE THIOESTERASE DOMAIN OF THE FENGYCIN
JRNL TITL 2 BIOSYNTHESIS CLUSTER: A STRUCTURAL BASE FOR THE
JRNL TITL 3 MACROCYCLIZATION OF A NON-RIBOSOMAL LIPOPEPTIDE
JRNL REF J.MOL.BIOL. V. 359 876 2006
JRNL REFN ASTM JMOBAK UK ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.5 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.18
REMARK 3 NUMBER OF REFLECTIONS : 8690
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) : 0.16574
REMARK 3 R VALUE (WORKING SET) : 0.16166
REMARK 3 FREE R VALUE : 0.23692
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.3
REMARK 3 FREE R VALUE TEST SET COUNT : 489
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) : 2.500
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.564
REMARK 3 REFLECTION IN BIN (WORKING SET) : 424
REMARK 3 BIN R VALUE (WORKING SET) : 0.252
REMARK 3 BIN FREE R VALUE SET COUNT : 20
REMARK 3 BIN FREE R VALUE : 0.287
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1665
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 75
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.6
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.396
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.53
REMARK 3 B22 (A**2) : 0.53
REMARK 3 B33 (A**2) : -0.80
REMARK 3 B12 (A**2) : 0.27
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.430
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.278
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.183
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.380
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.876
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED (A): 1708 ; 0.041 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED (DEGREES): 2302 ; 2.589 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 208 ; 8.721 ; 5.000
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): 244 ; 0.167 ; 0.200
REMARK 3 GENERAL PLANES REFINED (A): 1312 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED (A): 873 ; 0.238 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED (A): 113 ; 0.198 ; 0.200
REMARK 3 SYMMETRY VDW REFINED (A): 42 ; 0.231 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED (A): 5 ; 0.231 ; 0.200
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED (A**2): 1037 ; 1.608 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED (A**2): 1655 ; 2.982 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED (A**2): 671 ; 4.495 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED (A**2): 647 ; 6.856 ; 4.500
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS :1.40
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. THE RESIDUES T123-A131 WERE DISORDERED
REMARK 4
REMARK 4 2CBG COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 4-JAN-2006.
REMARK 100 THE EBI ID CODE IS EBI-26626.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-OCT-2003
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
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 : BRUKER-NONIUS FR591
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
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 : 9190
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.50
REMARK 200 RESOLUTION RANGE LOW (A) : 24.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.6
REMARK 200 DATA REDUNDANCY : 3.76
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.20
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 54.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.22
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.40
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1JMK
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.6
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M NH4 ACETATE, 0.1 M NA
REMARK 280 CITRATE (PH 5.6), 22.5 % PEG 8000, 10 MG/ML PROTEIN
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 Y-X,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,Y-X,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 32.11100
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 64.22200
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 48.16650
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 80.27750
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 16.05550
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 300
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: MONOMERIC
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 0
REMARK 465 ALA A 1
REMARK 465 ARG A 2
REMARK 465 SER A 3
REMARK 465 GLN A 4
REMARK 465 LEU A 5
REMARK 465 THR A 123
REMARK 465 GLU A 124
REMARK 465 ASN A 125
REMARK 465 ASP A 126
REMARK 465 ASP A 127
REMARK 465 SER A 128
REMARK 465 ALA A 129
REMARK 465 ALA A 130
REMARK 465 TYR A 131
REMARK 465 ASN A 225
REMARK 465 SER A 226
REMARK 465 ASP A 227
REMARK 465 GLN A 228
REMARK 465 LYS A 229
REMARK 465 VAL A 230
REMARK 465 LEU A 231
REMARK 465 PRO A 232
REMARK 465 ASN A 233
REMARK 465 LYS A 234
REMARK 465 HIS A 235
REMARK 465 GLY A 236
REMARK 465 SER A 237
REMARK 465 HIS A 238
REMARK 465 HIS A 239
REMARK 465 HIS A 240
REMARK 465 HIS A 241
REMARK 465 HIS A 242
REMARK 465 HIS A 243
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LYS A 183 CD - CE - NZ ANGL. DEV. = 21.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 AND BY MORE THAN 0.150 ANGSTROMS (M=MODEL
REMARK 500 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 500 NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,1X,2(A4,A1,3X),12X,F5.3)
REMARK 500
REMARK 500 EXPECTED VALUESS: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET A 141 SD MET A 141 CE 0.336
REMARK 500 MET A 179 SD MET A 179 CE 0.372
REMARK 500 LYS A 183 CE LYS A 183 NZ 0.357
REMARK 500
REMARK 500 REMARK: NULL
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 DISTANCE
REMARK 500 OH TYR A 36 O HOH Z 14 2.17
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY
REMARK 525 ASSOCIATED WITH:
REMARK 525 PROTEIN CHAIN SOLVENT CHAIN
REMARK 525 A Z
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 BENZYLSULFINIC ACID (PMS): COVALENTLY LINKED TO ACTIVE SITE
REMARK 600 SERINE SER A84
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: PMS BINDING SITE FOR CHAIN A
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2CB9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE THIOESTERASE DOMAIN
REMARK 900 OF THE FENGYCIN BIOSYNTHESIS CLUSTER
DBREF 2CBG A 0 3 PDB 2CBG 2CBG 0 3
DBREF 2CBG A 4 235 UNP Q45563 Q45563_BACSU 1043 1274
DBREF 2CBG A 236 243 PDB 2CBG 2CBG 236 243
SEQRES 1 A 244 MET ALA ARG SER GLN LEU SER ALA ALA GLY GLU GLN HIS
SEQRES 2 A 244 VAL ILE GLN LEU ASN GLN GLN GLY GLY LYS ASN LEU PHE
SEQRES 3 A 244 CYS PHE PRO PRO ILE SER GLY PHE GLY ILE TYR PHE LYS
SEQRES 4 A 244 ASP LEU ALA LEU GLN LEU ASN HIS LYS ALA ALA VAL TYR
SEQRES 5 A 244 GLY PHE HIS PHE ILE GLU GLU ASP SER ARG ILE GLU GLN
SEQRES 6 A 244 TYR VAL SER ARG ILE THR GLU ILE GLN PRO GLU GLY PRO
SEQRES 7 A 244 TYR VAL LEU LEU GLY TYR SER ALA GLY GLY ASN LEU ALA
SEQRES 8 A 244 PHE GLU VAL VAL GLN ALA MET GLU GLN LYS GLY LEU GLU
SEQRES 9 A 244 VAL SER ASP PHE ILE ILE VAL ASP ALA TYR LYS LYS ASP
SEQRES 10 A 244 GLN SER ILE THR ALA ASP THR GLU ASN ASP ASP SER ALA
SEQRES 11 A 244 ALA TYR LEU PRO GLU ALA VAL ARG GLU THR VAL MET GLN
SEQRES 12 A 244 LYS LYS ARG CYS TYR GLN GLU TYR TRP ALA GLN LEU ILE
SEQRES 13 A 244 ASN GLU GLY ARG ILE LYS SER ASN ILE HIS PHE ILE GLU
SEQRES 14 A 244 ALA GLY ILE GLN THR GLU THR SER GLY ALA MET VAL LEU
SEQRES 15 A 244 GLN LYS TRP GLN ASP ALA ALA GLU GLU GLY TYR ALA GLU
SEQRES 16 A 244 TYR THR GLY TYR GLY ALA HIS LYS ASP MET LEU GLU GLY
SEQRES 17 A 244 GLU PHE ALA GLU LYS ASN ALA ASN ILE ILE LEU ASN ILE
SEQRES 18 A 244 LEU ASP LYS ILE ASN SER ASP GLN LYS VAL LEU PRO ASN
SEQRES 19 A 244 LYS HIS GLY SER HIS HIS HIS HIS HIS HIS
HET PMS A1225 10
HETNAM PMS BENZYLSULFINIC ACID
FORMUL 2 PMS C7 H8 O2 S1
FORMUL 3 HOH *75(H2 O1)
HELIX 1 1 PHE A 33 TYR A 36 5 4
HELIX 2 2 PHE A 37 LEU A 44 1 8
HELIX 3 3 SER A 60 GLN A 73 1 14
HELIX 4 4 SER A 84 LYS A 100 1 17
HELIX 5 5 PRO A 133 MET A 141 1 9
HELIX 6 6 MET A 141 LEU A 154 1 14
HELIX 7 7 MET A 179 LYS A 183 5 5
HELIX 8 8 TRP A 184 ALA A 187 5 4
HELIX 9 9 ALA A 200 MET A 204 5 5
HELIX 10 10 GLU A 208 ILE A 224 1 17
SHEET 1 AA 7 VAL A 13 GLN A 15 0
SHEET 2 AA 7 ALA A 49 PHE A 53 -1 O GLY A 52 N ILE A 14
SHEET 3 AA 7 ASN A 23 PHE A 27 1 O LEU A 24 N TYR A 51
SHEET 4 AA 7 TYR A 78 TYR A 83 1 O VAL A 79 N PHE A 25
SHEET 5 AA 7 VAL A 104 VAL A 110 1 N SER A 105 O TYR A 78
SHEET 6 AA 7 ASN A 163 GLU A 168 1 O ASN A 163 N PHE A 107
SHEET 7 AA 7 TYR A 192 THR A 196 1 O ALA A 193 N PHE A 166
LINK OG SER A 84 S PMS A1225 1555 1555
CISPEP 1 GLY A 76 PRO A 77 0 -4.59
SITE 1 AC1 5 PRO A 29 ILE A 30 SER A 84 ALA A 85
SITE 2 AC1 5 TRP A 151
CRYST1 72.354 72.354 96.333 90.00 90.00 120.00 P 61 6
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 0.013821 0.007980 0.000000 0.00000
SCALE2 0.000000 0.015959 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010381 0.00000
TER 1666 ILE A 224
MASTER 333 0 1 10 7 0 2 6 1750 1 11 19
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