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HEADER LYASE/ANTIBIOTIC 25-JUL-18 6E6T
TITLE DIECKMANN CYCLASE, NCMC, BOUND TO CERULENIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NCMC;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROTHRIX SYRINGAE;
SOURCE 3 ORGANISM_TAXID: 103733;
SOURCE 4 ATCC: 51364;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS DIECKMANN CYCLASE, OFF-LOADING, DIECKMANN CONDENSATION, LYASE-
KEYWDS 2 ANTIBIOTIC COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.P.COGAN,S.K.NAIR
REVDAT 4 21-OCT-20 6E6T 1 JRNL
REVDAT 3 05-AUG-20 6E6T 1 HEADER COMPND KEYWDS REMARK
REVDAT 3 2 1 HELIX SHEET LINK SITE
REVDAT 3 3 1 SCALE ATOM
REVDAT 2 12-FEB-20 6E6T 1 JRNL
REVDAT 1 31-JUL-19 6E6T 0
JRNL AUTH D.P.COGAN,J.LY,S.K.NAIR
JRNL TITL STRUCTURAL BASIS FOR ENZYMATIC OFF-LOADING OF HYBRID
JRNL TITL 2 POLYKETIDES BY DIECKMANN CONDENSATION.
JRNL REF ACS CHEM.BIOL. 2020
JRNL REFN ESSN 1554-8937
JRNL PMID 33017142
JRNL DOI 10.1021/ACSCHEMBIO.0C00579
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_3908
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.84
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 64767
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3174
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 45.8400 - 4.5500 1.00 2760 138 0.1865 0.2061
REMARK 3 2 4.5500 - 3.6100 1.00 2729 134 0.1699 0.2189
REMARK 3 3 3.6100 - 3.1500 1.00 2646 189 0.1812 0.2073
REMARK 3 4 3.1500 - 2.8700 1.00 2709 112 0.1937 0.1911
REMARK 3 5 2.8700 - 2.6600 1.00 2730 126 0.1854 0.2260
REMARK 3 6 2.6600 - 2.5000 1.00 2677 144 0.1857 0.2419
REMARK 3 7 2.5000 - 2.3800 1.00 2690 122 0.1802 0.2269
REMARK 3 8 2.3800 - 2.2800 1.00 2660 183 0.1796 0.2121
REMARK 3 9 2.2700 - 2.1900 1.00 2654 162 0.1726 0.1970
REMARK 3 10 2.1900 - 2.1100 1.00 2669 132 0.1702 0.2203
REMARK 3 11 2.1100 - 2.0500 1.00 2690 164 0.1699 0.1859
REMARK 3 12 2.0500 - 1.9900 1.00 2698 127 0.1791 0.1975
REMARK 3 13 1.9900 - 1.9400 1.00 2681 128 0.1802 0.2133
REMARK 3 14 1.9400 - 1.8900 1.00 2698 123 0.1748 0.2412
REMARK 3 15 1.8900 - 1.8500 1.00 2635 183 0.1821 0.2220
REMARK 3 16 1.8400 - 1.8100 1.00 2667 127 0.1949 0.2222
REMARK 3 17 1.8100 - 1.7700 1.00 2712 120 0.2069 0.2598
REMARK 3 18 1.7700 - 1.7400 1.00 2689 139 0.2080 0.2471
REMARK 3 19 1.7400 - 1.7100 1.00 2647 163 0.2257 0.2481
REMARK 3 20 1.7100 - 1.6800 1.00 2699 99 0.2397 0.2793
REMARK 3 21 1.6800 - 1.6500 1.00 2727 100 0.2504 0.2450
REMARK 3 22 1.6500 - 1.6200 0.97 2605 145 0.2766 0.2960
REMARK 3 23 1.6200 - 1.6000 0.95 2521 114 0.2909 0.3172
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.630
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.63
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 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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 6E6T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUL-18.
REMARK 100 THE DEPOSITION ID IS D_1000235833.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUN-16
REMARK 200 TEMPERATURE (KELVIN) : 100
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 : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : DIAMOND(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AUTOPROC
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64817
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 80.270
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 10.70
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.92400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 6E6Y
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M AMMONIUM SULFATE, 1.8% W/V
REMARK 280 PEG400, 4% V/V FORMAMIDE, 0.1 M HEPES, PH 7.0, 3 MM DTT, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 282K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.87150
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 19.43575
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 58.30725
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: MONOMERIC
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 ALA A 3
REMARK 465 PRO A 4
REMARK 465 PRO A 15
REMARK 465 ALA A 16
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ALA B 3
REMARK 465 PRO B 4
REMARK 465 PRO B 15
REMARK 465 ALA B 16
REMARK 465 LEU B 140
REMARK 465 GLY B 141
REMARK 465 GLU B 142
REMARK 465 GLN B 143
REMARK 465 ALA B 144
REMARK 465 ALA B 184
REMARK 465 ASP B 185
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 GLY A 17 C PRO A 18 N 0.137
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 A 18 C - N - CA ANGL. DEV. = 10.2 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 ALA A 27 94.70 -160.89
REMARK 500 CYS A 89 -127.54 57.44
REMARK 500 ALA A 183 -28.98 -147.90
REMARK 500 CYS B 89 -128.77 57.89
REMARK 500 LEU B 136 36.49 -95.12
REMARK 500 ALA B 148 -72.18 -124.26
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 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 608 DISTANCE = 6.95 ANGSTROMS
REMARK 525 HOH B 566 DISTANCE = 7.37 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HVV A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide HVV B 302 and CYS B
REMARK 800 89
DBREF1 6E6T A 1 272 UNP A0A1X9WEN9_9PSEU
DBREF2 6E6T A A0A1X9WEN9 1 272
DBREF1 6E6T B 1 272 UNP A0A1X9WEN9_9PSEU
DBREF2 6E6T B A0A1X9WEN9 1 272
SEQADV 6E6T SER A -2 UNP A0A1X9WEN EXPRESSION TAG
SEQADV 6E6T ASN A -1 UNP A0A1X9WEN EXPRESSION TAG
SEQADV 6E6T ALA A 0 UNP A0A1X9WEN EXPRESSION TAG
SEQADV 6E6T SER B -2 UNP A0A1X9WEN EXPRESSION TAG
SEQADV 6E6T ASN B -1 UNP A0A1X9WEN EXPRESSION TAG
SEQADV 6E6T ALA B 0 UNP A0A1X9WEN EXPRESSION TAG
SEQRES 1 A 275 SER ASN ALA MET THR ALA PRO ARG ALA TRP ARG PRO ILE
SEQRES 2 A 275 ALA GLY GLY PRO PRO ALA GLY PRO LEU VAL LEU ALA VAL
SEQRES 3 A 275 ASP PHE ALA ALA THR GLY ARG PRO GLU ALA ALA PHE ALA
SEQRES 4 A 275 ASP LEU VAL ALA ARG LEU ASP PRO GLY THR GLU VAL TRP
SEQRES 5 A 275 GLU SER LEU GLN PRO PRO LEU GLY THR GLU THR GLY MET
SEQRES 6 A 275 VAL ALA GLU ASP TYR VAL THR ARG TRP GLU GLU GLU VAL
SEQRES 7 A 275 ARG ALA SER GLY ARG ARG ILE GLY ALA VAL LEU GLY PHE
SEQRES 8 A 275 CYS ALA GLY SER ALA PHE ALA GLY GLU LEU ALA VAL ARG
SEQRES 9 A 275 LEU ALA ARG SER GLN PRO ARG SER PRO ARG LEU VAL VAL
SEQRES 10 A 275 PHE ASP PRO GLU SER PRO THR THR SER THR LEU TYR TYR
SEQRES 11 A 275 GLN PHE ARG LYS VAL VAL GLU SER LEU ALA GLY VAL LEU
SEQRES 12 A 275 GLY GLU GLN ALA ALA ARG GLU ALA LEU ALA GLU GLY THR
SEQRES 13 A 275 ALA ALA ALA ASP ARG ILE GLY ASP VAL GLU GLY LEU GLY
SEQRES 14 A 275 ALA GLU LEU VAL ARG VAL PHE THR ALA ALA GLY ARG ALA
SEQRES 15 A 275 ALA CYS ALA ALA ALA ASP LEU ASP ASP GLU PHE ALA ASP
SEQRES 16 A 275 GLU LEU THR ALA THR TYR ARG SER PHE VAL SER TYR LEU
SEQRES 17 A 275 VAL ALA ALA ALA ALA VAL ASP HIS VAL LYS CYS TRP SER
SEQRES 18 A 275 GLY ALA VAL ALA VAL SER SER ALA THR PRO THR SER GLY
SEQRES 19 A 275 LEU ASN PRO LEU ASP PRO ALA ALA ARG ALA ALA LEU VAL
SEQRES 20 A 275 GLU ARG GLU LEU THR PHE ASP VAL HIS HIS ALA ASP LEU
SEQRES 21 A 275 LEU ARG ASP PRO GLY VAL ALA ARG ALA VAL ALA ARG LEU
SEQRES 22 A 275 LEU ALA
SEQRES 1 B 275 SER ASN ALA MET THR ALA PRO ARG ALA TRP ARG PRO ILE
SEQRES 2 B 275 ALA GLY GLY PRO PRO ALA GLY PRO LEU VAL LEU ALA VAL
SEQRES 3 B 275 ASP PHE ALA ALA THR GLY ARG PRO GLU ALA ALA PHE ALA
SEQRES 4 B 275 ASP LEU VAL ALA ARG LEU ASP PRO GLY THR GLU VAL TRP
SEQRES 5 B 275 GLU SER LEU GLN PRO PRO LEU GLY THR GLU THR GLY MET
SEQRES 6 B 275 VAL ALA GLU ASP TYR VAL THR ARG TRP GLU GLU GLU VAL
SEQRES 7 B 275 ARG ALA SER GLY ARG ARG ILE GLY ALA VAL LEU GLY PHE
SEQRES 8 B 275 CYS ALA GLY SER ALA PHE ALA GLY GLU LEU ALA VAL ARG
SEQRES 9 B 275 LEU ALA ARG SER GLN PRO ARG SER PRO ARG LEU VAL VAL
SEQRES 10 B 275 PHE ASP PRO GLU SER PRO THR THR SER THR LEU TYR TYR
SEQRES 11 B 275 GLN PHE ARG LYS VAL VAL GLU SER LEU ALA GLY VAL LEU
SEQRES 12 B 275 GLY GLU GLN ALA ALA ARG GLU ALA LEU ALA GLU GLY THR
SEQRES 13 B 275 ALA ALA ALA ASP ARG ILE GLY ASP VAL GLU GLY LEU GLY
SEQRES 14 B 275 ALA GLU LEU VAL ARG VAL PHE THR ALA ALA GLY ARG ALA
SEQRES 15 B 275 ALA CYS ALA ALA ALA ASP LEU ASP ASP GLU PHE ALA ASP
SEQRES 16 B 275 GLU LEU THR ALA THR TYR ARG SER PHE VAL SER TYR LEU
SEQRES 17 B 275 VAL ALA ALA ALA ALA VAL ASP HIS VAL LYS CYS TRP SER
SEQRES 18 B 275 GLY ALA VAL ALA VAL SER SER ALA THR PRO THR SER GLY
SEQRES 19 B 275 LEU ASN PRO LEU ASP PRO ALA ALA ARG ALA ALA LEU VAL
SEQRES 20 B 275 GLU ARG GLU LEU THR PHE ASP VAL HIS HIS ALA ASP LEU
SEQRES 21 B 275 LEU ARG ASP PRO GLY VAL ALA ARG ALA VAL ALA ARG LEU
SEQRES 22 B 275 LEU ALA
HET SO4 A 301 5
HET HVV A 302 16
HET SO4 B 301 5
HET HVV B 302 16
HETNAM SO4 SULFATE ION
HETNAM HVV (4S,5R)-4,5-DIHYDROXY-5-[(3E,6E)-OCTA-3,6-DIEN-1-
HETNAM 2 HVV YL]PYRROLIDIN-2-ONE
HETSYN HVV CERULENIN, BOUND FORM
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 4 HVV 2(C12 H19 N O3)
FORMUL 7 HOH *374(H2 O)
HELIX 1 AA1 ALA A 34 ALA A 40 1 7
HELIX 2 AA2 VAL A 63 GLY A 79 1 17
HELIX 3 AA3 ALA A 90 GLN A 106 1 17
HELIX 4 AA4 THR A 121 LEU A 136 1 16
HELIX 5 AA5 LEU A 136 GLY A 141 1 6
HELIX 6 AA6 GLY A 141 ILE A 159 1 19
HELIX 7 AA7 ASP A 161 CYS A 181 1 21
HELIX 8 AA8 ASP A 187 VAL A 211 1 25
HELIX 9 AA9 ASP A 212 TRP A 217 1 6
HELIX 10 AB1 ASP A 236 VAL A 244 1 9
HELIX 11 AB2 HIS A 253 ARG A 259 5 7
HELIX 12 AB3 ASP A 260 ALA A 272 1 13
HELIX 13 AB4 ALA B 34 ALA B 40 1 7
HELIX 14 AB5 VAL B 63 GLY B 79 1 17
HELIX 15 AB6 ALA B 90 GLN B 106 1 17
HELIX 16 AB7 THR B 121 LEU B 136 1 16
HELIX 17 AB8 ARG B 146 ILE B 159 1 14
HELIX 18 AB9 ASP B 161 ALA B 183 1 23
HELIX 19 AC1 ASP B 187 VAL B 211 1 25
HELIX 20 AC2 ASP B 212 TRP B 217 1 6
HELIX 21 AC3 ASP B 236 VAL B 244 1 9
HELIX 22 AC4 HIS B 253 ARG B 259 5 7
HELIX 23 AC5 ASP B 260 ALA B 272 1 13
SHEET 1 AA1 7 TRP A 7 ALA A 11 0
SHEET 2 AA1 7 VAL A 48 SER A 51 -1 O GLU A 50 N ARG A 8
SHEET 3 AA1 7 LEU A 19 VAL A 23 1 N ALA A 22 O SER A 51
SHEET 4 AA1 7 ILE A 82 PHE A 88 1 O LEU A 86 N LEU A 21
SHEET 5 AA1 7 ARG A 111 PHE A 115 1 O PHE A 115 N GLY A 87
SHEET 6 AA1 7 VAL A 221 SER A 224 1 O VAL A 223 N VAL A 114
SHEET 7 AA1 7 ARG A 246 THR A 249 1 O ARG A 246 N ALA A 222
SHEET 1 AA2 7 TRP B 7 ALA B 11 0
SHEET 2 AA2 7 VAL B 48 SER B 51 -1 O GLU B 50 N ARG B 8
SHEET 3 AA2 7 LEU B 19 VAL B 23 1 N VAL B 20 O TRP B 49
SHEET 4 AA2 7 ILE B 82 PHE B 88 1 O LEU B 86 N LEU B 21
SHEET 5 AA2 7 ARG B 111 PHE B 115 1 O ARG B 111 N VAL B 85
SHEET 6 AA2 7 VAL B 221 SER B 224 1 O VAL B 223 N VAL B 114
SHEET 7 AA2 7 ARG B 246 THR B 249 1 O ARG B 246 N ALA B 222
LINK SG CYS A 89 CAF HVV A 302 1555 1555 1.82
LINK SG CYS B 89 CAF HVV B 302 1555 1555 1.82
SITE 1 AC1 5 ARG A 81 ARG A 108 PHE A 250 HOH A 482
SITE 2 AC1 5 HOH A 546
SITE 1 AC2 12 ARG A 30 PRO A 31 GLU A 32 PHE A 88
SITE 2 AC2 12 CYS A 89 ALA A 90 LYS A 131 SER A 135
SITE 3 AC2 12 PHE A 201 HIS A 254 HOH A 452 HOH A 462
SITE 1 AC3 5 ARG B 81 ARG B 108 PHE B 250 HOH B 402
SITE 2 AC3 5 HOH B 463
SITE 1 AC4 14 ARG B 30 GLU B 32 PHE B 88 ALA B 90
SITE 2 AC4 14 GLY B 91 SER B 92 PHE B 115 ASP B 116
SITE 3 AC4 14 PRO B 117 GLU B 118 LYS B 131 VAL B 132
SITE 4 AC4 14 HIS B 254 HOH B 422
CRYST1 80.269 80.269 77.743 90.00 90.00 90.00 P 41 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 0.012458 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012458 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012863 0.00000
TER 1973 ALA A 272
TER 3898 ALA B 272
MASTER 342 0 4 23 14 0 11 6 4312 2 44 44
END |