HEADER HYDROLASE 08-JUN-10 3NEF
TITLE HIGH-RESOLUTION PYRABACTIN-BOUND PYL1 STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ABSCISIC ACID RECEPTOR PYL1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 20-221;
COMPND 5 SYNONYM: PYL1, PYR1-LIKE PROTEIN 1, ABI1-BINDING PROTEIN 6,
COMPND 6 REGULATORY COMPONENTS OF ABA RECEPTOR 9;
COMPND 7 EC: 3.1.3.16;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-15B
KEYWDS PYL1, PYRABACTIN, HORMONE RECEPTOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.YAN
REVDAT 4 01-NOV-23 3NEF 1 REMARK
REVDAT 3 15-SEP-10 3NEF 1 JRNL
REVDAT 2 30-JUN-10 3NEF 1 JRNL
REVDAT 1 16-JUN-10 3NEF 0
JRNL AUTH Q.HAO,P.YIN,C.YAN,X.YUAN,W.LI,Z.ZHANG,L.LIU,J.WANG,N.YAN
JRNL TITL FUNCTIONAL MECHANISM OF THE ABA AGONIST PYRABACTIN
JRNL REF J.BIOL.CHEM. V. 285 28946 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20554531
JRNL DOI 10.1074/JBC.M110.149005
REMARK 2
REMARK 2 RESOLUTION. 2.40 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.62
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 3 NUMBER OF REFLECTIONS : 30549
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.370
REMARK 3 FREE R VALUE TEST SET COUNT : 1639
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 40.6220 - 5.4906 0.99 2644 198 0.1907 0.1981
REMARK 3 2 5.4906 - 4.3597 1.00 2643 130 0.1551 0.1748
REMARK 3 3 4.3597 - 3.8091 1.00 2746 0 0.1513 0.0000
REMARK 3 4 3.8091 - 3.4610 1.00 2532 204 0.1608 0.1925
REMARK 3 5 3.4610 - 3.2130 1.00 2538 195 0.1742 0.2286
REMARK 3 6 3.2130 - 3.0237 1.00 2723 0 0.1917 0.0000
REMARK 3 7 3.0237 - 2.8723 1.00 2514 218 0.2074 0.2289
REMARK 3 8 2.8723 - 2.7473 1.00 2416 275 0.2358 0.2833
REMARK 3 9 2.7473 - 2.6415 1.00 2697 0 0.2446 0.0000
REMARK 3 10 2.6415 - 2.5504 0.99 2386 290 0.2596 0.2968
REMARK 3 11 2.5504 - 2.4707 0.71 1911 0 0.2446 0.0000
REMARK 3 12 2.4707 - 2.4000 0.47 1160 129 0.2465 0.2710
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 : 0.36
REMARK 3 B_SOL : 44.09
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.670
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.98500
REMARK 3 B22 (A**2) : 6.98500
REMARK 3 B33 (A**2) : -13.96990
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
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 : 0.008 2943
REMARK 3 ANGLE : 1.142 3988
REMARK 3 CHIRALITY : 0.078 453
REMARK 3 PLANARITY : 0.004 520
REMARK 3 DIHEDRAL : 17.818 1076
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): -55.7048 37.1466 -12.4183
REMARK 3 T TENSOR
REMARK 3 T11: 0.2053 T22: 0.2288
REMARK 3 T33: 0.2156 T12: -0.0565
REMARK 3 T13: -0.0242 T23: -0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 1.2288 L22: 1.6141
REMARK 3 L33: 3.5060 L12: 0.0256
REMARK 3 L13: 0.0025 L23: 1.3149
REMARK 3 S TENSOR
REMARK 3 S11: -0.1557 S12: -0.0611 S13: 0.0281
REMARK 3 S21: -0.0914 S22: 0.1561 S23: 0.0902
REMARK 3 S31: -0.2073 S32: 0.2338 S33: -0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): -43.5197 56.7944 3.1263
REMARK 3 T TENSOR
REMARK 3 T11: 0.2619 T22: 0.3355
REMARK 3 T33: 0.2574 T12: -0.2460
REMARK 3 T13: -0.0364 T23: 0.0395
REMARK 3 L TENSOR
REMARK 3 L11: 2.3274 L22: 2.0973
REMARK 3 L33: 3.2559 L12: 0.6731
REMARK 3 L13: 0.2070 L23: -0.0078
REMARK 3 S TENSOR
REMARK 3 S11: -0.1587 S12: 0.2033 S13: 0.0242
REMARK 3 S21: -0.1294 S22: 0.3915 S23: 0.0675
REMARK 3 S31: -0.3365 S32: 0.3270 S33: 0.0003
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 3NEF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000059725.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-MAY-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9067
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30549
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 40.616
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.9
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.10300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 54.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.36500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
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 3KDJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M CITRIC ACID PH 5.5, 0.01M
REMARK 280 GSH/GSSG, 10% PEG 4000, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
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 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 29.08000
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 58.16000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 58.16000
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 29.08000
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 ILE A -1
REMARK 465 SER A 0
REMARK 465 THR A 1
REMARK 465 LEU A 2
REMARK 465 GLU A 138
REMARK 465 GLU A 139
REMARK 465 GLU A 140
REMARK 465 GLU A 141
REMARK 465 GLU A 142
REMARK 465 ASN A 190
REMARK 465 ASN A 191
REMARK 465 ASN A 192
REMARK 465 ASN A 193
REMARK 465 ASN A 194
REMARK 465 ASN A 195
REMARK 465 SER A 196
REMARK 465 SER A 197
REMARK 465 GLN A 198
REMARK 465 VAL A 199
REMARK 465 ARG A 200
REMARK 465 ILE B -1
REMARK 465 SER B 0
REMARK 465 THR B 1
REMARK 465 LEU B 2
REMARK 465 HIS B 3
REMARK 465 HIS B 4
REMARK 465 GLN B 5
REMARK 465 THR B 6
REMARK 465 MET B 7
REMARK 465 PRO B 8
REMARK 465 GLU B 138
REMARK 465 GLU B 139
REMARK 465 GLU B 140
REMARK 465 GLU B 141
REMARK 465 GLU B 142
REMARK 465 ARG B 143
REMARK 465 ASN B 192
REMARK 465 ASN B 193
REMARK 465 ASN B 194
REMARK 465 ASN B 195
REMARK 465 SER B 196
REMARK 465 SER B 197
REMARK 465 GLN B 198
REMARK 465 VAL B 199
REMARK 465 ARG B 200
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 HIS A 3 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 137 CG CD CE NZ
REMARK 470 SER B 9 OG
REMARK 470 GLU B 120 CG CD OE1 OE2
REMARK 470 HIS B 121 CG ND1 CD2 CE1 NE2
REMARK 470 ARG B 122 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 136 CG CD OE1 OE2
REMARK 470 LYS B 137 CG CD CE NZ
REMARK 470 ASN B 191 CG OD1 ND2
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 LEU A 31 -136.46 -124.51
REMARK 500 ASN A 33 84.29 68.72
REMARK 500 TYR A 64 -6.79 -145.78
REMARK 500 ASP A 76 36.02 -97.06
REMARK 500 HIS A 121 -179.05 -174.15
REMARK 500 LEU A 123 68.89 -110.51
REMARK 500 ASN A 188 -138.99 49.00
REMARK 500 ASP B 10 112.16 165.31
REMARK 500 LEU B 11 -115.34 -89.93
REMARK 500 THR B 12 146.12 -173.34
REMARK 500 MET B 79 90.33 -65.05
REMARK 500 PRO B 94 -109.68 -22.26
REMARK 500 ASN B 96 86.72 167.52
REMARK 500 LEU B 105 108.18 -163.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYV A 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KDH RELATED DB: PDB
REMARK 900 APO-PYL2
REMARK 900 RELATED ID: 3KDI RELATED DB: PDB
REMARK 900 (+)-ABA BOUND PYL2
REMARK 900 RELATED ID: 3KDJ RELATED DB: PDB
REMARK 900 (+)-ABA-BOUND PYL1 AND ABI1
REMARK 900 RELATED ID: 3NEG RELATED DB: PDB
REMARK 900 PYRABACTIN-BOUND PYL1 AT 2.8A
DBREF 3NEF A -1 200 UNP Q8VZS8 PYL1_ARATH 20 221
DBREF 3NEF B -1 200 UNP Q8VZS8 PYL1_ARATH 20 221
SEQRES 1 A 202 ILE SER THR LEU HIS HIS GLN THR MET PRO SER ASP LEU
SEQRES 2 A 202 THR GLN ASP GLU PHE THR GLN LEU SER GLN SER ILE ALA
SEQRES 3 A 202 GLU PHE HIS THR TYR GLN LEU GLY ASN GLY ARG CYS SER
SEQRES 4 A 202 SER LEU LEU ALA GLN ARG ILE HIS ALA PRO PRO GLU THR
SEQRES 5 A 202 VAL TRP SER VAL VAL ARG ARG PHE ASP ARG PRO GLN ILE
SEQRES 6 A 202 TYR LYS HIS PHE ILE LYS SER CYS ASN VAL SER GLU ASP
SEQRES 7 A 202 PHE GLU MET ARG VAL GLY CYS THR ARG ASP VAL ASN VAL
SEQRES 8 A 202 ILE SER GLY LEU PRO ALA ASN THR SER ARG GLU ARG LEU
SEQRES 9 A 202 ASP LEU LEU ASP ASP ASP ARG ARG VAL THR GLY PHE SER
SEQRES 10 A 202 ILE THR GLY GLY GLU HIS ARG LEU ARG ASN TYR LYS SER
SEQRES 11 A 202 VAL THR THR VAL HIS ARG PHE GLU LYS GLU GLU GLU GLU
SEQRES 12 A 202 GLU ARG ILE TRP THR VAL VAL LEU GLU SER TYR VAL VAL
SEQRES 13 A 202 ASP VAL PRO GLU GLY ASN SER GLU GLU ASP THR ARG LEU
SEQRES 14 A 202 PHE ALA ASP THR VAL ILE ARG LEU ASN LEU GLN LYS LEU
SEQRES 15 A 202 ALA SER ILE THR GLU ALA MET ASN ARG ASN ASN ASN ASN
SEQRES 16 A 202 ASN ASN SER SER GLN VAL ARG
SEQRES 1 B 202 ILE SER THR LEU HIS HIS GLN THR MET PRO SER ASP LEU
SEQRES 2 B 202 THR GLN ASP GLU PHE THR GLN LEU SER GLN SER ILE ALA
SEQRES 3 B 202 GLU PHE HIS THR TYR GLN LEU GLY ASN GLY ARG CYS SER
SEQRES 4 B 202 SER LEU LEU ALA GLN ARG ILE HIS ALA PRO PRO GLU THR
SEQRES 5 B 202 VAL TRP SER VAL VAL ARG ARG PHE ASP ARG PRO GLN ILE
SEQRES 6 B 202 TYR LYS HIS PHE ILE LYS SER CYS ASN VAL SER GLU ASP
SEQRES 7 B 202 PHE GLU MET ARG VAL GLY CYS THR ARG ASP VAL ASN VAL
SEQRES 8 B 202 ILE SER GLY LEU PRO ALA ASN THR SER ARG GLU ARG LEU
SEQRES 9 B 202 ASP LEU LEU ASP ASP ASP ARG ARG VAL THR GLY PHE SER
SEQRES 10 B 202 ILE THR GLY GLY GLU HIS ARG LEU ARG ASN TYR LYS SER
SEQRES 11 B 202 VAL THR THR VAL HIS ARG PHE GLU LYS GLU GLU GLU GLU
SEQRES 12 B 202 GLU ARG ILE TRP THR VAL VAL LEU GLU SER TYR VAL VAL
SEQRES 13 B 202 ASP VAL PRO GLU GLY ASN SER GLU GLU ASP THR ARG LEU
SEQRES 14 B 202 PHE ALA ASP THR VAL ILE ARG LEU ASN LEU GLN LYS LEU
SEQRES 15 B 202 ALA SER ILE THR GLU ALA MET ASN ARG ASN ASN ASN ASN
SEQRES 16 B 202 ASN ASN SER SER GLN VAL ARG
HET PYV A 201 22
HETNAM PYV 4-BROMO-N-(PYRIDIN-2-YLMETHYL)NAPHTHALENE-1-SULFONAMIDE
HETSYN PYV PYRABACTIN
FORMUL 3 PYV C16 H13 BR N2 O2 S
FORMUL 4 HOH *123(H2 O)
HELIX 1 1 THR A 12 HIS A 27 1 16
HELIX 2 2 PRO A 47 ARG A 56 1 10
HELIX 3 3 ARG A 60 TYR A 64 5 5
HELIX 4 4 SER A 161 MET A 187 1 27
HELIX 5 5 THR B 12 HIS B 27 1 16
HELIX 6 6 PRO B 47 ARG B 56 1 10
HELIX 7 7 ARG B 60 TYR B 64 5 5
HELIX 8 8 SER B 161 ASN B 190 1 30
SHEET 1 A 7 ARG A 35 ILE A 44 0
SHEET 2 A 7 TRP A 145 ASP A 155 -1 O VAL A 148 N GLN A 42
SHEET 3 A 7 LYS A 127 PHE A 135 -1 N THR A 131 O LEU A 149
SHEET 4 A 7 VAL A 111 ILE A 116 -1 N THR A 112 O THR A 130
SHEET 5 A 7 THR A 97 ASP A 106 -1 N ARG A 101 O SER A 115
SHEET 6 A 7 THR A 84 VAL A 89 -1 N ARG A 85 O GLU A 100
SHEET 7 A 7 ILE A 68 ASN A 72 -1 N SER A 70 O ASN A 88
SHEET 1 B 7 ARG B 35 ILE B 44 0
SHEET 2 B 7 TRP B 145 ASP B 155 -1 O THR B 146 N ILE B 44
SHEET 3 B 7 LYS B 127 PHE B 135 -1 N THR B 131 O LEU B 149
SHEET 4 B 7 VAL B 111 GLY B 118 -1 N THR B 112 O THR B 130
SHEET 5 B 7 THR B 97 ASP B 106 -1 N ASP B 103 O GLY B 113
SHEET 6 B 7 THR B 84 VAL B 89 -1 N ARG B 85 O GLU B 100
SHEET 7 B 7 ILE B 68 ASN B 72 -1 N SER B 70 O ASN B 88
CISPEP 1 THR A 117 GLY A 118 0 5.77
CISPEP 2 ASP B 10 LEU B 11 0 -0.67
SITE 1 AC1 11 ILE A 68 VAL A 87 ALA A 95 SER A 98
SITE 2 AC1 11 GLU A 100 HIS A 121 LEU A 123 TYR A 126
SITE 3 AC1 11 VAL A 172 HOH A 206 HOH A 235
CRYST1 128.570 128.570 87.240 90.00 90.00 120.00 P 31 2 1 12
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 0.007778 0.004491 0.000000 0.00000
SCALE2 0.000000 0.008981 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011462 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
