HEADER TRANSFERASE 19-FEB-13 4JAR
TITLE CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS PKS11 IN COMPLEX WITH
TITLE 2 POLYKETIDE INTERMEDIATES AND EVIDENCE THAT IT SYNTHESIZE ALKYLPYRONES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-PYRONE SYNTHESIS POLYKETIDE SYNTHASE-LIKE PKS11;
COMPND 3 CHAIN: A, C, B, D;
COMPND 4 SYNONYM: ALPHA-PYRONE SYNTHESIS POLYKETIDE SYNTHASE TYPE III PKS11,
COMPND 5 CHALCONE SYNTHASE-LIKE PROTEIN, CHS-LIKE;
COMPND 6 EC: 2.3.1.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: PKS11, RV1665, MT1705;
SOURCE 6 EXPRESSION_SYSTEM: MYCOBACTERIUM SMEGMATIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 1772;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: P1601-DEST17
KEYWDS LIPID BIOSYNTHESIS, STRUCTURAL GENOMICS, ENZYME FUNCTION INITIATIVE,
KEYWDS 2 KETOSYNTHASE ENZYME, ALKYLPYRONE SYNTHESIS, TRANSFERASE,
KEYWDS 3 MYCOBACTERIUM TUBERCULOSIS STRUCTURAL PROTEOMICS PROJECT, XMTB
EXPDTA X-RAY DIFFRACTION
AUTHOR K.GOKULAN,J.C.SACCHETTINI,MYCOBACTERIUM TUBERCULOSIS STRUCTURAL
AUTHOR 2 PROTEOMICS PROJECT (XMTB)
REVDAT 3 28-FEB-24 4JAR 1 REMARK
REVDAT 2 27-NOV-13 4JAR 1 JRNL
REVDAT 1 24-APR-13 4JAR 0
JRNL AUTH K.GOKULAN,S.E.O'LEARY,W.K.RUSSELL,D.H.RUSSELL,M.LALGONDAR,
JRNL AUTH 2 T.P.BEGLEY,T.R.IOERGER,J.C.SACCHETTINI
JRNL TITL CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS POLYKETIDE
JRNL TITL 2 SYNTHASE 11 (PKS11) REVEALS INTERMEDIATES IN THE SYNTHESIS
JRNL TITL 3 OF METHYL-BRANCHED ALKYLPYRONES.
JRNL REF J.BIOL.CHEM. V. 288 16484 2013
JRNL REFN ISSN 0021-9258
JRNL PMID 23615910
JRNL DOI 10.1074/JBC.M113.468892
REMARK 2
REMARK 2 RESOLUTION. 1.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6_289)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.24
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.030
REMARK 3 COMPLETENESS FOR RANGE (%) : 70.0
REMARK 3 NUMBER OF REFLECTIONS : 58551
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.270
REMARK 3 R VALUE (WORKING SET) : 0.268
REMARK 3 FREE R VALUE : 0.314
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.430
REMARK 3 FREE R VALUE TEST SET COUNT : 3269
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 38.2400 - 4.2585 0.72 6845 239 0.2140 0.2648
REMARK 3 2 4.2585 - 3.3807 0.76 7018 254 0.2266 0.2642
REMARK 3 3 3.3807 - 2.9536 0.88 8077 285 0.2885 0.3430
REMARK 3 4 2.9536 - 2.6836 0.91 8259 295 0.3217 0.3509
REMARK 3 5 2.6836 - 2.4913 0.86 7850 281 0.3435 0.3964
REMARK 3 6 2.4913 - 2.3444 0.74 6674 249 0.3573 0.4082
REMARK 3 7 2.3444 - 2.2270 0.56 5092 172 0.3837 0.4164
REMARK 3 8 2.2270 - 2.1301 0.39 3515 124 0.4048 0.4344
REMARK 3 9 2.1301 - 2.0481 0.22 2061 70 0.4283 0.4402
REMARK 3 10 2.0481 - 1.9800 0.13 1154 37 0.4435 0.4474
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.32
REMARK 3 B_SOL : 52.37
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 43.930
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) : 5.27920
REMARK 3 B22 (A**2) : 5.68490
REMARK 3 B33 (A**2) : -10.96410
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -6.47860
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 10791
REMARK 3 ANGLE : 1.298 14703
REMARK 3 CHIRALITY : 0.082 1726
REMARK 3 PLANARITY : 0.005 1918
REMARK 3 DIHEDRAL : 19.277 3912
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4JAR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-FEB-13.
REMARK 100 THE DEPOSITION ID IS D_1000077810.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XFIT, HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66722
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.970
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.4200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: XFIT
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MAGNESIUM FORMATE DIHYDRATE, 20%
REMARK 280 W/V POLYETHYLENE GLYCOL 3350, PH 7.0, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 298K
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 24.26050
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 4150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 4170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 465 MET C 1
REMARK 465 MET D 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 DISTANCE
REMARK 500 O TYR D 252 OD1 ASP D 256 1.82
REMARK 500 O ASP B 285 OG1 THR B 289 2.00
REMARK 500 O LEU D 261 O LEU D 266 2.10
REMARK 500 OG SER A 169 OD2 ASP A 190 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE1 GLU C 299 NH1 ARG D 303 1455 2.07
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 PRO C 295 C - N - CD ANGL. DEV. = 12.7 DEGREES
REMARK 500 PRO B 329 C - N - CD ANGL. DEV. = 13.7 DEGREES
REMARK 500 PRO D 12 C - N - CD ANGL. DEV. = -16.8 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 PHE A 134 136.15 -170.83
REMARK 500 CYS A 138 8.01 -69.24
REMARK 500 ASP A 200 -70.17 -48.11
REMARK 500 GLN A 205 -9.44 -46.89
REMARK 500 ASP A 215 167.69 170.10
REMARK 500 ASP A 223 66.67 33.93
REMARK 500 LEU A 245 -73.79 -49.63
REMARK 500 LEU A 311 40.86 -104.86
REMARK 500 SER A 312 -130.69 51.31
REMARK 500 ARG A 327 96.52 56.17
REMARK 500 PRO A 329 139.56 -23.93
REMARK 500 PRO A 341 143.19 -39.07
REMARK 500 PRO C 29 141.47 -30.62
REMARK 500 LEU C 31 -9.00 -147.10
REMARK 500 ASN C 92 42.77 74.28
REMARK 500 PRO C 177 72.20 -66.86
REMARK 500 LEU C 214 -72.05 -75.19
REMARK 500 ARG C 217 115.82 -162.23
REMARK 500 SER C 219 98.20 -164.05
REMARK 500 MET C 228 149.72 -176.37
REMARK 500 GLU C 250 15.63 -68.84
REMARK 500 ARG C 251 -49.23 -138.91
REMARK 500 PRO C 278 -121.55 -46.56
REMARK 500 GLU C 299 -81.40 -25.31
REMARK 500 LEU C 300 -21.24 -36.15
REMARK 500 SER C 312 -137.08 73.37
REMARK 500 PRO C 341 142.33 -33.66
REMARK 500 THR B 63 -9.05 -145.98
REMARK 500 VAL B 106 17.40 -148.27
REMARK 500 PRO B 132 95.89 -67.72
REMARK 500 ALA B 155 77.93 -155.62
REMARK 500 LEU B 167 78.40 -112.15
REMARK 500 ARG B 217 114.37 -160.36
REMARK 500 TYR B 252 -27.10 -140.31
REMARK 500 ALA B 263 16.86 -67.34
REMARK 500 HIS B 264 23.38 -145.00
REMARK 500 ALA B 273 118.36 -165.99
REMARK 500 SER B 312 -128.83 56.10
REMARK 500 LYS B 326 30.05 -93.67
REMARK 500 ARG B 327 99.07 5.50
REMARK 500 PRO B 328 -155.87 -61.91
REMARK 500 PRO B 329 63.58 -111.01
REMARK 500 SER B 330 103.44 38.01
REMARK 500 SER B 332 161.64 -42.54
REMARK 500 LEU D 31 27.33 -143.76
REMARK 500 GLU D 33 37.55 -94.44
REMARK 500 HIS D 34 28.18 -146.47
REMARK 500 VAL D 106 12.78 -149.16
REMARK 500 PHE D 134 -59.99 -132.13
REMARK 500 ALA D 155 74.49 -159.90
REMARK 500
REMARK 500 THIS ENTRY HAS 60 RAMACHANDRAN OUTLIERS.
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 GLY A 272 ALA A 273 114.34
REMARK 500 CYS C 344 THR C 345 142.52
REMARK 500 SER B 2 VAL B 3 -148.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4JAO RELATED DB: PDB
REMARK 900 RELATED ID: 4JAP RELATED DB: PDB
REMARK 900 RELATED ID: 4JAQ RELATED DB: PDB
REMARK 900 RELATED ID: 4JAT RELATED DB: PDB
REMARK 900 RELATED ID: 4JD3 RELATED DB: PDB
DBREF 4JAR A 1 353 UNP O06587 PKS11_MYCTU 1 353
DBREF 4JAR C 1 353 UNP O06587 PKS11_MYCTU 1 353
DBREF 4JAR B 1 353 UNP O06587 PKS11_MYCTU 1 353
DBREF 4JAR D 1 353 UNP O06587 PKS11_MYCTU 1 353
SEQRES 1 A 353 MET SER VAL ILE ALA GLY VAL PHE GLY ALA LEU PRO PRO
SEQRES 2 A 353 HIS ARG TYR SER GLN SER GLU ILE THR ASP SER PHE VAL
SEQRES 3 A 353 GLU PHE PRO GLY LEU LYS GLU HIS GLU GLU ILE ILE ARG
SEQRES 4 A 353 ARG LEU HIS ALA ALA ALA LYS VAL ASN GLY ARG HIS LEU
SEQRES 5 A 353 VAL LEU PRO LEU GLN GLN TYR PRO SER LEU THR ASP PHE
SEQRES 6 A 353 GLY ASP ALA ASN GLU ILE PHE ILE GLU LYS ALA VAL ASP
SEQRES 7 A 353 LEU GLY VAL GLU ALA LEU LEU GLY ALA LEU ASP ASP ALA
SEQRES 8 A 353 ASN LEU ARG PRO SER ASP ILE ASP MET ILE ALA THR ALA
SEQRES 9 A 353 THR VAL THR GLY VAL ALA VAL PRO SER LEU ASP ALA ARG
SEQRES 10 A 353 ILE ALA GLY ARG LEU GLY LEU ARG PRO ASP VAL ARG ARG
SEQRES 11 A 353 MET PRO LEU PHE GLY LEU GLY CYS VAL ALA GLY ALA ALA
SEQRES 12 A 353 GLY VAL ALA ARG LEU ARG ASP TYR LEU ARG GLY ALA PRO
SEQRES 13 A 353 ASP ASP VAL ALA VAL LEU VAL SER VAL GLU LEU CYS SER
SEQRES 14 A 353 LEU THR TYR PRO ALA VAL LYS PRO THR VAL SER SER LEU
SEQRES 15 A 353 VAL GLY THR ALA LEU PHE GLY ASP GLY ALA ALA ALA VAL
SEQRES 16 A 353 VAL ALA VAL GLY ASP ARG ARG ALA GLU GLN VAL ARG ALA
SEQRES 17 A 353 GLY GLY PRO ASP ILE LEU ASP SER ARG SER SER LEU TYR
SEQRES 18 A 353 PRO ASP SER LEU HIS ILE MET GLY TRP ASP VAL GLY SER
SEQRES 19 A 353 HIS GLY LEU ARG LEU ARG LEU SER PRO ASP LEU THR ASN
SEQRES 20 A 353 LEU ILE GLU ARG TYR LEU ALA ASN ASP VAL THR THR PHE
SEQRES 21 A 353 LEU ASP ALA HIS ARG LEU THR LYS ASP ASP ILE GLY ALA
SEQRES 22 A 353 TRP VAL SER HIS PRO GLY GLY PRO LYS VAL ILE ASP ALA
SEQRES 23 A 353 VAL ALA THR SER LEU ALA LEU PRO PRO GLU ALA LEU GLU
SEQRES 24 A 353 LEU THR TRP ARG SER LEU GLY GLU ILE GLY ASN LEU SER
SEQRES 25 A 353 SER ALA SER ILE LEU HIS ILE LEU ARG ASP THR ILE GLU
SEQRES 26 A 353 LYS ARG PRO PRO SER GLY SER ALA GLY LEU MET LEU ALA
SEQRES 27 A 353 MET GLY PRO GLY PHE CYS THR GLU LEU VAL LEU LEU ARG
SEQRES 28 A 353 TRP ARG
SEQRES 1 C 353 MET SER VAL ILE ALA GLY VAL PHE GLY ALA LEU PRO PRO
SEQRES 2 C 353 HIS ARG TYR SER GLN SER GLU ILE THR ASP SER PHE VAL
SEQRES 3 C 353 GLU PHE PRO GLY LEU LYS GLU HIS GLU GLU ILE ILE ARG
SEQRES 4 C 353 ARG LEU HIS ALA ALA ALA LYS VAL ASN GLY ARG HIS LEU
SEQRES 5 C 353 VAL LEU PRO LEU GLN GLN TYR PRO SER LEU THR ASP PHE
SEQRES 6 C 353 GLY ASP ALA ASN GLU ILE PHE ILE GLU LYS ALA VAL ASP
SEQRES 7 C 353 LEU GLY VAL GLU ALA LEU LEU GLY ALA LEU ASP ASP ALA
SEQRES 8 C 353 ASN LEU ARG PRO SER ASP ILE ASP MET ILE ALA THR ALA
SEQRES 9 C 353 THR VAL THR GLY VAL ALA VAL PRO SER LEU ASP ALA ARG
SEQRES 10 C 353 ILE ALA GLY ARG LEU GLY LEU ARG PRO ASP VAL ARG ARG
SEQRES 11 C 353 MET PRO LEU PHE GLY LEU GLY CYS VAL ALA GLY ALA ALA
SEQRES 12 C 353 GLY VAL ALA ARG LEU ARG ASP TYR LEU ARG GLY ALA PRO
SEQRES 13 C 353 ASP ASP VAL ALA VAL LEU VAL SER VAL GLU LEU CYS SER
SEQRES 14 C 353 LEU THR TYR PRO ALA VAL LYS PRO THR VAL SER SER LEU
SEQRES 15 C 353 VAL GLY THR ALA LEU PHE GLY ASP GLY ALA ALA ALA VAL
SEQRES 16 C 353 VAL ALA VAL GLY ASP ARG ARG ALA GLU GLN VAL ARG ALA
SEQRES 17 C 353 GLY GLY PRO ASP ILE LEU ASP SER ARG SER SER LEU TYR
SEQRES 18 C 353 PRO ASP SER LEU HIS ILE MET GLY TRP ASP VAL GLY SER
SEQRES 19 C 353 HIS GLY LEU ARG LEU ARG LEU SER PRO ASP LEU THR ASN
SEQRES 20 C 353 LEU ILE GLU ARG TYR LEU ALA ASN ASP VAL THR THR PHE
SEQRES 21 C 353 LEU ASP ALA HIS ARG LEU THR LYS ASP ASP ILE GLY ALA
SEQRES 22 C 353 TRP VAL SER HIS PRO GLY GLY PRO LYS VAL ILE ASP ALA
SEQRES 23 C 353 VAL ALA THR SER LEU ALA LEU PRO PRO GLU ALA LEU GLU
SEQRES 24 C 353 LEU THR TRP ARG SER LEU GLY GLU ILE GLY ASN LEU SER
SEQRES 25 C 353 SER ALA SER ILE LEU HIS ILE LEU ARG ASP THR ILE GLU
SEQRES 26 C 353 LYS ARG PRO PRO SER GLY SER ALA GLY LEU MET LEU ALA
SEQRES 27 C 353 MET GLY PRO GLY PHE CYS THR GLU LEU VAL LEU LEU ARG
SEQRES 28 C 353 TRP ARG
SEQRES 1 B 353 MET SER VAL ILE ALA GLY VAL PHE GLY ALA LEU PRO PRO
SEQRES 2 B 353 HIS ARG TYR SER GLN SER GLU ILE THR ASP SER PHE VAL
SEQRES 3 B 353 GLU PHE PRO GLY LEU LYS GLU HIS GLU GLU ILE ILE ARG
SEQRES 4 B 353 ARG LEU HIS ALA ALA ALA LYS VAL ASN GLY ARG HIS LEU
SEQRES 5 B 353 VAL LEU PRO LEU GLN GLN TYR PRO SER LEU THR ASP PHE
SEQRES 6 B 353 GLY ASP ALA ASN GLU ILE PHE ILE GLU LYS ALA VAL ASP
SEQRES 7 B 353 LEU GLY VAL GLU ALA LEU LEU GLY ALA LEU ASP ASP ALA
SEQRES 8 B 353 ASN LEU ARG PRO SER ASP ILE ASP MET ILE ALA THR ALA
SEQRES 9 B 353 THR VAL THR GLY VAL ALA VAL PRO SER LEU ASP ALA ARG
SEQRES 10 B 353 ILE ALA GLY ARG LEU GLY LEU ARG PRO ASP VAL ARG ARG
SEQRES 11 B 353 MET PRO LEU PHE GLY LEU GLY CYS VAL ALA GLY ALA ALA
SEQRES 12 B 353 GLY VAL ALA ARG LEU ARG ASP TYR LEU ARG GLY ALA PRO
SEQRES 13 B 353 ASP ASP VAL ALA VAL LEU VAL SER VAL GLU LEU CYS SER
SEQRES 14 B 353 LEU THR TYR PRO ALA VAL LYS PRO THR VAL SER SER LEU
SEQRES 15 B 353 VAL GLY THR ALA LEU PHE GLY ASP GLY ALA ALA ALA VAL
SEQRES 16 B 353 VAL ALA VAL GLY ASP ARG ARG ALA GLU GLN VAL ARG ALA
SEQRES 17 B 353 GLY GLY PRO ASP ILE LEU ASP SER ARG SER SER LEU TYR
SEQRES 18 B 353 PRO ASP SER LEU HIS ILE MET GLY TRP ASP VAL GLY SER
SEQRES 19 B 353 HIS GLY LEU ARG LEU ARG LEU SER PRO ASP LEU THR ASN
SEQRES 20 B 353 LEU ILE GLU ARG TYR LEU ALA ASN ASP VAL THR THR PHE
SEQRES 21 B 353 LEU ASP ALA HIS ARG LEU THR LYS ASP ASP ILE GLY ALA
SEQRES 22 B 353 TRP VAL SER HIS PRO GLY GLY PRO LYS VAL ILE ASP ALA
SEQRES 23 B 353 VAL ALA THR SER LEU ALA LEU PRO PRO GLU ALA LEU GLU
SEQRES 24 B 353 LEU THR TRP ARG SER LEU GLY GLU ILE GLY ASN LEU SER
SEQRES 25 B 353 SER ALA SER ILE LEU HIS ILE LEU ARG ASP THR ILE GLU
SEQRES 26 B 353 LYS ARG PRO PRO SER GLY SER ALA GLY LEU MET LEU ALA
SEQRES 27 B 353 MET GLY PRO GLY PHE CYS THR GLU LEU VAL LEU LEU ARG
SEQRES 28 B 353 TRP ARG
SEQRES 1 D 353 MET SER VAL ILE ALA GLY VAL PHE GLY ALA LEU PRO PRO
SEQRES 2 D 353 HIS ARG TYR SER GLN SER GLU ILE THR ASP SER PHE VAL
SEQRES 3 D 353 GLU PHE PRO GLY LEU LYS GLU HIS GLU GLU ILE ILE ARG
SEQRES 4 D 353 ARG LEU HIS ALA ALA ALA LYS VAL ASN GLY ARG HIS LEU
SEQRES 5 D 353 VAL LEU PRO LEU GLN GLN TYR PRO SER LEU THR ASP PHE
SEQRES 6 D 353 GLY ASP ALA ASN GLU ILE PHE ILE GLU LYS ALA VAL ASP
SEQRES 7 D 353 LEU GLY VAL GLU ALA LEU LEU GLY ALA LEU ASP ASP ALA
SEQRES 8 D 353 ASN LEU ARG PRO SER ASP ILE ASP MET ILE ALA THR ALA
SEQRES 9 D 353 THR VAL THR GLY VAL ALA VAL PRO SER LEU ASP ALA ARG
SEQRES 10 D 353 ILE ALA GLY ARG LEU GLY LEU ARG PRO ASP VAL ARG ARG
SEQRES 11 D 353 MET PRO LEU PHE GLY LEU GLY CYS VAL ALA GLY ALA ALA
SEQRES 12 D 353 GLY VAL ALA ARG LEU ARG ASP TYR LEU ARG GLY ALA PRO
SEQRES 13 D 353 ASP ASP VAL ALA VAL LEU VAL SER VAL GLU LEU CYS SER
SEQRES 14 D 353 LEU THR TYR PRO ALA VAL LYS PRO THR VAL SER SER LEU
SEQRES 15 D 353 VAL GLY THR ALA LEU PHE GLY ASP GLY ALA ALA ALA VAL
SEQRES 16 D 353 VAL ALA VAL GLY ASP ARG ARG ALA GLU GLN VAL ARG ALA
SEQRES 17 D 353 GLY GLY PRO ASP ILE LEU ASP SER ARG SER SER LEU TYR
SEQRES 18 D 353 PRO ASP SER LEU HIS ILE MET GLY TRP ASP VAL GLY SER
SEQRES 19 D 353 HIS GLY LEU ARG LEU ARG LEU SER PRO ASP LEU THR ASN
SEQRES 20 D 353 LEU ILE GLU ARG TYR LEU ALA ASN ASP VAL THR THR PHE
SEQRES 21 D 353 LEU ASP ALA HIS ARG LEU THR LYS ASP ASP ILE GLY ALA
SEQRES 22 D 353 TRP VAL SER HIS PRO GLY GLY PRO LYS VAL ILE ASP ALA
SEQRES 23 D 353 VAL ALA THR SER LEU ALA LEU PRO PRO GLU ALA LEU GLU
SEQRES 24 D 353 LEU THR TRP ARG SER LEU GLY GLU ILE GLY ASN LEU SER
SEQRES 25 D 353 SER ALA SER ILE LEU HIS ILE LEU ARG ASP THR ILE GLU
SEQRES 26 D 353 LYS ARG PRO PRO SER GLY SER ALA GLY LEU MET LEU ALA
SEQRES 27 D 353 MET GLY PRO GLY PHE CYS THR GLU LEU VAL LEU LEU ARG
SEQRES 28 D 353 TRP ARG
HELIX 1 1 GLN A 18 VAL A 26 1 9
HELIX 2 2 GLY A 30 GLU A 33 5 4
HELIX 3 3 HIS A 34 ALA A 44 1 11
HELIX 4 4 PRO A 55 LEU A 62 5 8
HELIX 5 5 ASP A 64 ALA A 91 1 28
HELIX 6 6 ARG A 94 ILE A 98 5 5
HELIX 7 7 SER A 113 LEU A 122 1 10
HELIX 8 8 VAL A 139 ARG A 153 1 15
HELIX 9 9 SER A 169 VAL A 175 5 7
HELIX 10 10 THR A 178 PHE A 188 1 11
HELIX 11 11 GLY A 199 GLU A 204 1 6
HELIX 12 12 SER A 224 HIS A 226 5 3
HELIX 13 13 LEU A 245 HIS A 264 1 20
HELIX 14 14 THR A 267 ASP A 269 5 3
HELIX 15 15 GLY A 280 ALA A 292 1 13
HELIX 16 16 LEU A 298 ILE A 308 1 11
HELIX 17 17 LEU A 311 SER A 313 5 3
HELIX 18 18 ALA A 314 LYS A 326 1 13
HELIX 19 19 GLN C 18 VAL C 26 1 9
HELIX 20 20 LEU C 31 GLU C 33 5 3
HELIX 21 21 HIS C 34 ALA C 44 1 11
HELIX 22 22 PRO C 55 LEU C 62 5 8
HELIX 23 23 ASP C 64 ALA C 91 1 28
HELIX 24 24 ARG C 94 ILE C 98 5 5
HELIX 25 25 SER C 113 GLY C 123 1 11
HELIX 26 26 LEU C 136 CYS C 138 5 3
HELIX 27 27 VAL C 139 ARG C 153 1 15
HELIX 28 28 SER C 169 VAL C 175 5 7
HELIX 29 29 THR C 178 PHE C 188 1 11
HELIX 30 30 GLY C 199 ARG C 207 1 9
HELIX 31 31 SER C 224 HIS C 226 5 3
HELIX 32 32 ASP C 244 ALA C 263 1 20
HELIX 33 33 GLY C 280 LEU C 291 1 12
HELIX 34 34 LEU C 298 GLY C 309 1 12
HELIX 35 35 SER C 313 GLU C 325 1 13
HELIX 36 36 GLN B 18 VAL B 26 1 9
HELIX 37 37 LEU B 31 GLU B 33 5 3
HELIX 38 38 HIS B 34 ALA B 45 1 12
HELIX 39 39 PRO B 55 LEU B 62 5 8
HELIX 40 40 ASP B 64 ALA B 91 1 28
HELIX 41 41 ARG B 94 ILE B 98 5 5
HELIX 42 42 SER B 113 GLY B 123 1 11
HELIX 43 43 LEU B 136 CYS B 138 5 3
HELIX 44 44 VAL B 139 GLY B 154 1 16
HELIX 45 45 SER B 169 VAL B 175 5 7
HELIX 46 46 THR B 178 PHE B 188 1 11
HELIX 47 47 GLY B 199 VAL B 206 1 8
HELIX 48 48 SER B 224 HIS B 226 5 3
HELIX 49 49 ASP B 244 ALA B 263 1 20
HELIX 50 50 GLY B 280 LEU B 291 1 12
HELIX 51 51 LEU B 298 GLY B 309 1 12
HELIX 52 52 LEU B 311 SER B 313 5 3
HELIX 53 53 ALA B 314 LYS B 326 1 13
HELIX 54 54 GLN D 18 VAL D 26 1 9
HELIX 55 55 LEU D 31 GLU D 33 5 3
HELIX 56 56 HIS D 34 ALA D 45 1 12
HELIX 57 57 PRO D 55 TYR D 59 5 5
HELIX 58 58 ASP D 64 ALA D 91 1 28
HELIX 59 59 ARG D 94 ILE D 98 5 5
HELIX 60 60 SER D 113 GLY D 123 1 11
HELIX 61 61 LEU D 136 CYS D 138 5 3
HELIX 62 62 VAL D 139 ARG D 153 1 15
HELIX 63 63 SER D 169 VAL D 175 5 7
HELIX 64 64 THR D 178 PHE D 188 1 11
HELIX 65 65 LEU D 245 LEU D 261 1 17
HELIX 66 66 GLY D 280 LEU D 291 1 12
HELIX 67 67 LEU D 298 GLY D 309 1 12
HELIX 68 68 LEU D 311 SER D 313 5 3
HELIX 69 69 ALA D 314 ARG D 327 1 14
SHEET 1 A 5 VAL A 3 ALA A 10 0
SHEET 2 A 5 ASP A 190 VAL A 198 -1 O VAL A 196 N ALA A 5
SHEET 3 A 5 VAL A 159 LEU A 167 -1 N SER A 164 O ALA A 193
SHEET 4 A 5 MET A 100 ALA A 104 1 N ALA A 104 O VAL A 165
SHEET 5 A 5 ARG A 129 LEU A 133 1 O ARG A 129 N ILE A 101
SHEET 1 B 2 TYR A 16 SER A 17 0
SHEET 2 B 2 GLY A 49 ARG A 50 -1 O ARG A 50 N TYR A 16
SHEET 1 C 4 ASP A 212 LEU A 220 0
SHEET 2 C 4 CYS A 344 ARG A 351 -1 O LEU A 347 N ARG A 217
SHEET 3 C 4 ALA A 333 GLY A 340 -1 N GLY A 334 O LEU A 350
SHEET 4 C 4 ILE A 271 SER A 276 1 N VAL A 275 O LEU A 335
SHEET 1 D 2 MET A 228 GLY A 233 0
SHEET 2 D 2 GLY A 236 LEU A 241 -1 O ARG A 238 N ASP A 231
SHEET 1 E 5 VAL C 3 ALA C 10 0
SHEET 2 E 5 ASP C 190 VAL C 198 -1 O VAL C 196 N GLY C 6
SHEET 3 E 5 VAL C 159 LEU C 167 -1 N ALA C 160 O ALA C 197
SHEET 4 E 5 MET C 100 ALA C 104 1 N ALA C 102 O VAL C 161
SHEET 5 E 5 ARG C 129 LEU C 133 1 O ARG C 129 N ILE C 101
SHEET 1 F 2 ARG C 15 SER C 17 0
SHEET 2 F 2 GLY C 49 HIS C 51 -1 O ARG C 50 N TYR C 16
SHEET 1 G 4 ASP C 212 LEU C 220 0
SHEET 2 G 4 CYS C 344 ARG C 351 -1 O ARG C 351 N ASP C 212
SHEET 3 G 4 ALA C 333 GLY C 340 -1 N ALA C 338 O GLU C 346
SHEET 4 G 4 ILE C 271 SER C 276 1 N GLY C 272 O ALA C 333
SHEET 1 H 2 MET C 228 GLY C 233 0
SHEET 2 H 2 GLY C 236 LEU C 241 -1 O ARG C 238 N ASP C 231
SHEET 1 I 9 ARG B 129 PHE B 134 0
SHEET 2 I 9 MET B 100 THR B 105 1 N ILE B 101 O ARG B 129
SHEET 3 I 9 VAL B 159 LEU B 167 1 O VAL B 161 N ALA B 102
SHEET 4 I 9 ASP B 190 VAL B 198 -1 O ALA B 193 N SER B 164
SHEET 5 I 9 SER B 2 ALA B 10 -1 N ALA B 10 O ALA B 192
SHEET 6 I 9 ASP B 212 LEU B 220 -1 O ILE B 213 N SER B 2
SHEET 7 I 9 CYS B 344 ARG B 351 -1 O ARG B 351 N ASP B 212
SHEET 8 I 9 ALA B 333 GLY B 340 -1 N GLY B 334 O LEU B 350
SHEET 9 I 9 ILE B 271 SER B 276 1 N GLY B 272 O ALA B 333
SHEET 1 J 2 HIS B 14 SER B 17 0
SHEET 2 J 2 GLY B 49 LEU B 52 -1 O LEU B 52 N HIS B 14
SHEET 1 K 2 MET B 228 GLY B 233 0
SHEET 2 K 2 GLY B 236 LEU B 241 -1 O ARG B 240 N GLY B 229
SHEET 1 L 5 VAL D 3 ALA D 10 0
SHEET 2 L 5 ASP D 190 VAL D 198 -1 O VAL D 196 N GLY D 6
SHEET 3 L 5 VAL D 159 LEU D 167 -1 N ALA D 160 O ALA D 197
SHEET 4 L 5 MET D 100 ALA D 104 1 N ALA D 104 O VAL D 163
SHEET 5 L 5 ARG D 129 LEU D 133 1 O LEU D 133 N THR D 103
SHEET 1 M 2 ARG D 15 SER D 17 0
SHEET 2 M 2 GLY D 49 HIS D 51 -1 O ARG D 50 N TYR D 16
SHEET 1 N 4 ASP D 212 LEU D 220 0
SHEET 2 N 4 CYS D 344 ARG D 351 -1 O LEU D 349 N ASP D 215
SHEET 3 N 4 ALA D 333 GLY D 340 -1 N GLY D 334 O LEU D 350
SHEET 4 N 4 ILE D 271 SER D 276 1 N GLY D 272 O ALA D 333
SHEET 1 O 2 MET D 228 GLY D 233 0
SHEET 2 O 2 GLY D 236 LEU D 241 -1 O ARG D 238 N ASP D 231
CISPEP 1 VAL A 111 PRO A 112 0 4.58
CISPEP 2 PHE A 134 GLY A 135 0 -7.57
CISPEP 3 GLY A 342 PHE A 343 0 -7.41
CISPEP 4 VAL C 111 PRO C 112 0 -2.17
CISPEP 5 GLY C 342 PHE C 343 0 -6.28
CISPEP 6 VAL B 111 PRO B 112 0 -0.62
CISPEP 7 GLY B 342 PHE B 343 0 -5.74
CISPEP 8 VAL D 111 PRO D 112 0 4.30
CISPEP 9 GLY D 342 PHE D 343 0 -9.66
CRYST1 72.598 48.521 195.234 90.00 98.41 90.00 P 1 21 1 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 0.013774 0.000000 0.002036 0.00000
SCALE2 0.000000 0.020610 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005178 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
