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HEADER HYDROLASE 30-MAR-13 4JYM
TITLE CRYSTAL STRUCTURE OF KAI2 IN COMPLEX WITH 3-METHYL-2H-FURO[2,3-
TITLE 2 C]PYRAN-2-ONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROLASE, ALPHA/BETA FOLD FAMILY PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: KAI2;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS,THALE-CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: F6G17.120, AT4G37470, AT4G37470, AT4G37470;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS ALPHA/BETA-HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.GUO,Z.ZHENG,J.P.NOEL
REVDAT 1 08-MAY-13 4JYM 0
JRNL AUTH Y.GUO,Z.ZHENG,J.J.LA CLAIR,J.CHORY,J.P.NOEL
JRNL TITL SMOKE-DERIVED KARRIKIN PERCEPTION BY THE
JRNL TITL 2 ALPHA/BETA-HYDROLASE KAI2 FROM ARABIDOPSIS.
JRNL REF PROC.NATL.ACAD.SCI.USA 2013
JRNL REFN ESSN 1091-6490
JRNL PMID 23613584
JRNL DOI 10.1073/PNAS.1306265110
REMARK 2
REMARK 2 RESOLUTION. 1.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.49
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 85.8
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 4974
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 26.4917 - 4.1895 0.98 3573 197 0.1518 0.1841
REMARK 3 2 4.1895 - 3.3274 0.97 3577 170 0.1459 0.1629
REMARK 3 3 3.3274 - 2.9074 0.97 3491 191 0.1651 0.2081
REMARK 3 4 2.9074 - 2.6418 0.96 3541 191 0.1790 0.2341
REMARK 3 5 2.6418 - 2.4526 0.96 3496 192 0.1701 0.2018
REMARK 3 6 2.4526 - 2.3081 0.96 3495 185 0.1623 0.1748
REMARK 3 7 2.3081 - 2.1926 0.95 3528 180 0.1664 0.2204
REMARK 3 8 2.1926 - 2.0972 0.95 3490 190 0.1541 0.1679
REMARK 3 9 2.0972 - 2.0165 0.95 3469 177 0.1688 0.1928
REMARK 3 10 2.0165 - 1.9469 0.94 3489 184 0.1668 0.1828
REMARK 3 11 1.9469 - 1.8860 0.94 3411 163 0.1894 0.2264
REMARK 3 12 1.8860 - 1.8321 0.94 3430 192 0.1808 0.2212
REMARK 3 13 1.8321 - 1.7839 0.94 3441 171 0.1814 0.2473
REMARK 3 14 1.7839 - 1.7404 0.93 3418 180 0.1894 0.2202
REMARK 3 15 1.7404 - 1.7008 0.93 3408 194 0.1959 0.2438
REMARK 3 16 1.7008 - 1.6646 0.93 3409 152 0.1962 0.2401
REMARK 3 17 1.6646 - 1.6314 0.93 3347 189 0.1934 0.2307
REMARK 3 18 1.6314 - 1.6006 0.92 3398 173 0.2035 0.2846
REMARK 3 19 1.6006 - 1.5720 0.92 3358 173 0.2077 0.2443
REMARK 3 20 1.5720 - 1.5453 0.92 3382 170 0.2207 0.2889
REMARK 3 21 1.5453 - 1.5204 0.88 3229 186 0.2526 0.2952
REMARK 3 22 1.5204 - 1.4970 0.84 3040 184 0.2620 0.3311
REMARK 3 23 1.4970 - 1.4750 0.82 3026 137 0.2750 0.2877
REMARK 3 24 1.4750 - 1.4542 0.84 3022 174 0.2984 0.3099
REMARK 3 25 1.4542 - 1.4346 0.83 3090 173 0.3122 0.3117
REMARK 3 26 1.4346 - 1.4160 0.61 2236 103 0.2896 0.3129
REMARK 3 27 1.4160 - 1.3983 0.52 1858 111 0.2945 0.3147
REMARK 3 28 1.3983 - 1.3814 0.54 1998 94 0.3017 0.3429
REMARK 3 29 1.3814 - 1.3654 0.49 1807 103 0.3237 0.3116
REMARK 3 30 1.3654 - 1.3500 0.49 1767 95 0.3109 0.3362
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.160
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.26
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 : 0.006 4327
REMARK 3 ANGLE : 1.055 5908
REMARK 3 CHIRALITY : 0.075 674
REMARK 3 PLANARITY : 0.005 771
REMARK 3 DIHEDRAL : 13.013 1552
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 4JYM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-APR-13.
REMARK 100 THE RCSB ID CODE IS RCSB078668.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-SEP-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 99300
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
REMARK 200 RESOLUTION RANGE LOW (A) : 26.487
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.9
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.12200
REMARK 200 FOR THE DATA SET : 4.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 51.3
REMARK 200 DATA REDUNDANCY IN SHELL : 1.10
REMARK 200 R MERGE FOR SHELL (I) : 0.41300
REMARK 200 R SYM FOR SHELL (I) : 0.41300
REMARK 200 FOR SHELL : 1.400
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: 1WOM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% (W/V) POLYETHYLENE GLYCOL 8000,
REMARK 280 0.1 M NA+-PIPES (PH 6.5), 0.3 M NABR AND 2 MM DTT, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 MET A 1
REMARK 465 ALA A 269
REMARK 465 MET A 270
REMARK 465 MET B 1
REMARK 465 ALA B 269
REMARK 465 MET B 270
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 OE1 GLU B 82 O HOH B 502 2.14
REMARK 500 O HOH B 650 O HOH B 671 2.14
REMARK 500 O HOH A 710 O HOH A 718 2.14
REMARK 500 O HOH B 523 O HOH B 537 2.15
REMARK 500 O HOH B 515 O HOH B 677 2.15
REMARK 500 O HOH B 667 O HOH B 697 2.16
REMARK 500 O09 KKN B 301 O HOH B 675 2.16
REMARK 500 O HOH A 687 O HOH A 721 2.16
REMARK 500 O HOH B 698 O HOH B 702 2.17
REMARK 500 O HOH A 697 O HOH A 717 2.17
REMARK 500 OE1 GLU A 82 O HOH A 485 2.18
REMARK 500 OD1 ASN B 180 O HOH B 658 2.18
REMARK 500 O HOH A 597 O HOH A 683 2.18
REMARK 500 O HOH B 639 O HOH B 691 2.18
REMARK 500 O HOH A 564 O HOH A 636 2.19
REMARK 500 O HOH A 600 O HOH A 667 2.19
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 O HOH A 657 O HOH B 705 1544 2.18
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 THR A 28 -161.76 -120.96
REMARK 500 SER A 95 -123.64 54.24
REMARK 500 ARG A 123 124.76 -172.33
REMARK 500 ASN A 149 93.72 -161.62
REMARK 500 THR B 28 -162.17 -121.72
REMARK 500 SER B 95 -124.07 53.87
REMARK 500 ARG B 123 122.95 -172.50
REMARK 500 ASN B 149 92.89 -162.17
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 B 683 DISTANCE = 7.53 ANGSTROMS
REMARK 525 HOH B 709 DISTANCE = 6.83 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KKN A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KKN B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4JYP RELATED DB: PDB
DBREF 4JYM A 1 270 UNP Q9SZU7 Q9SZU7_ARATH 1 270
DBREF 4JYM B 1 270 UNP Q9SZU7 Q9SZU7_ARATH 1 270
SEQRES 1 A 270 MET GLY VAL VAL GLU GLU ALA HIS ASN VAL LYS VAL ILE
SEQRES 2 A 270 GLY SER GLY GLU ALA THR ILE VAL LEU GLY HIS GLY PHE
SEQRES 3 A 270 GLY THR ASP GLN SER VAL TRP LYS HIS LEU VAL PRO HIS
SEQRES 4 A 270 LEU VAL ASP ASP TYR ARG VAL VAL LEU TYR ASP ASN MET
SEQRES 5 A 270 GLY ALA GLY THR THR ASN PRO ASP TYR PHE ASP PHE ASP
SEQRES 6 A 270 ARG TYR SER ASN LEU GLU GLY TYR SER PHE ASP LEU ILE
SEQRES 7 A 270 ALA ILE LEU GLU ASP LEU LYS ILE GLU SER CYS ILE PHE
SEQRES 8 A 270 VAL GLY HIS SER VAL SER ALA MET ILE GLY VAL LEU ALA
SEQRES 9 A 270 SER LEU ASN ARG PRO ASP LEU PHE SER LYS ILE VAL MET
SEQRES 10 A 270 ILE SER ALA SER PRO ARG TYR VAL ASN ASP VAL ASP TYR
SEQRES 11 A 270 GLN GLY GLY PHE GLU GLN GLU ASP LEU ASN GLN LEU PHE
SEQRES 12 A 270 GLU ALA ILE ARG SER ASN TYR LYS ALA TRP CYS LEU GLY
SEQRES 13 A 270 PHE ALA PRO LEU ALA VAL GLY GLY ASP MET ASP SER ILE
SEQRES 14 A 270 ALA VAL GLN GLU PHE SER ARG THR LEU PHE ASN MET ARG
SEQRES 15 A 270 PRO ASP ILE ALA LEU SER VAL GLY GLN THR ILE PHE GLN
SEQRES 16 A 270 SER ASP MET ARG GLN ILE LEU PRO PHE VAL THR VAL PRO
SEQRES 17 A 270 CYS HIS ILE LEU GLN SER VAL LYS ASP LEU ALA VAL PRO
SEQRES 18 A 270 VAL VAL VAL SER GLU TYR LEU HIS ALA ASN LEU GLY CYS
SEQRES 19 A 270 GLU SER VAL VAL GLU VAL ILE PRO SER ASP GLY HIS LEU
SEQRES 20 A 270 PRO GLN LEU SER SER PRO ASP SER VAL ILE PRO VAL ILE
SEQRES 21 A 270 LEU ARG HIS ILE ARG ASN ASP ILE ALA MET
SEQRES 1 B 270 MET GLY VAL VAL GLU GLU ALA HIS ASN VAL LYS VAL ILE
SEQRES 2 B 270 GLY SER GLY GLU ALA THR ILE VAL LEU GLY HIS GLY PHE
SEQRES 3 B 270 GLY THR ASP GLN SER VAL TRP LYS HIS LEU VAL PRO HIS
SEQRES 4 B 270 LEU VAL ASP ASP TYR ARG VAL VAL LEU TYR ASP ASN MET
SEQRES 5 B 270 GLY ALA GLY THR THR ASN PRO ASP TYR PHE ASP PHE ASP
SEQRES 6 B 270 ARG TYR SER ASN LEU GLU GLY TYR SER PHE ASP LEU ILE
SEQRES 7 B 270 ALA ILE LEU GLU ASP LEU LYS ILE GLU SER CYS ILE PHE
SEQRES 8 B 270 VAL GLY HIS SER VAL SER ALA MET ILE GLY VAL LEU ALA
SEQRES 9 B 270 SER LEU ASN ARG PRO ASP LEU PHE SER LYS ILE VAL MET
SEQRES 10 B 270 ILE SER ALA SER PRO ARG TYR VAL ASN ASP VAL ASP TYR
SEQRES 11 B 270 GLN GLY GLY PHE GLU GLN GLU ASP LEU ASN GLN LEU PHE
SEQRES 12 B 270 GLU ALA ILE ARG SER ASN TYR LYS ALA TRP CYS LEU GLY
SEQRES 13 B 270 PHE ALA PRO LEU ALA VAL GLY GLY ASP MET ASP SER ILE
SEQRES 14 B 270 ALA VAL GLN GLU PHE SER ARG THR LEU PHE ASN MET ARG
SEQRES 15 B 270 PRO ASP ILE ALA LEU SER VAL GLY GLN THR ILE PHE GLN
SEQRES 16 B 270 SER ASP MET ARG GLN ILE LEU PRO PHE VAL THR VAL PRO
SEQRES 17 B 270 CYS HIS ILE LEU GLN SER VAL LYS ASP LEU ALA VAL PRO
SEQRES 18 B 270 VAL VAL VAL SER GLU TYR LEU HIS ALA ASN LEU GLY CYS
SEQRES 19 B 270 GLU SER VAL VAL GLU VAL ILE PRO SER ASP GLY HIS LEU
SEQRES 20 B 270 PRO GLN LEU SER SER PRO ASP SER VAL ILE PRO VAL ILE
SEQRES 21 B 270 LEU ARG HIS ILE ARG ASN ASP ILE ALA MET
HET KKN A 301 11
HET KKN B 301 11
HETNAM KKN 3-METHYL-2H-FURO[2,3-C]PYRAN-2-ONE
FORMUL 3 KKN 2(C8 H6 O3)
FORMUL 5 HOH *640(H2 O)
HELIX 1 1 GLY A 2 HIS A 8 1 7
HELIX 2 2 ASP A 29 LYS A 34 5 6
HELIX 3 3 LEU A 36 LEU A 40 5 5
HELIX 4 4 ASN A 58 PHE A 62 5 5
HELIX 5 5 ASP A 65 SER A 68 5 4
HELIX 6 6 ASN A 69 LEU A 84 1 16
HELIX 7 7 SER A 95 ARG A 108 1 14
HELIX 8 8 GLU A 135 ASN A 149 1 15
HELIX 9 9 ASN A 149 GLY A 163 1 15
HELIX 10 10 SER A 168 ASN A 180 1 13
HELIX 11 11 ARG A 182 GLN A 195 1 14
HELIX 12 12 MET A 198 VAL A 205 5 8
HELIX 13 13 PRO A 221 LEU A 232 1 12
HELIX 14 14 LEU A 247 SER A 252 1 6
HELIX 15 15 SER A 252 ASN A 266 1 15
HELIX 16 16 VAL B 3 HIS B 8 1 6
HELIX 17 17 ASP B 29 LYS B 34 5 6
HELIX 18 18 LEU B 36 LEU B 40 5 5
HELIX 19 19 ASN B 58 PHE B 62 5 5
HELIX 20 20 ASP B 65 ASN B 69 5 5
HELIX 21 21 LEU B 70 LEU B 84 1 15
HELIX 22 22 SER B 95 ARG B 108 1 14
HELIX 23 23 GLU B 135 ASN B 149 1 15
HELIX 24 24 ASN B 149 GLY B 163 1 15
HELIX 25 25 SER B 168 MET B 181 1 14
HELIX 26 26 ARG B 182 GLN B 195 1 14
HELIX 27 27 MET B 198 VAL B 205 5 8
HELIX 28 28 PRO B 221 LEU B 232 1 12
HELIX 29 29 LEU B 247 SER B 252 1 6
HELIX 30 30 SER B 252 ASN B 266 1 15
SHEET 1 A 7 LYS A 11 ILE A 13 0
SHEET 2 A 7 ARG A 45 LEU A 48 -1 O VAL A 46 N ILE A 13
SHEET 3 A 7 THR A 19 GLY A 23 1 N ILE A 20 O VAL A 47
SHEET 4 A 7 CYS A 89 HIS A 94 1 O VAL A 92 N VAL A 21
SHEET 5 A 7 PHE A 112 ILE A 118 1 O VAL A 116 N PHE A 91
SHEET 6 A 7 CYS A 209 LYS A 216 1 O HIS A 210 N MET A 117
SHEET 7 A 7 SER A 236 ASP A 244 1 O VAL A 237 N ILE A 211
SHEET 1 B 7 LYS B 11 ILE B 13 0
SHEET 2 B 7 ARG B 45 LEU B 48 -1 O VAL B 46 N ILE B 13
SHEET 3 B 7 THR B 19 GLY B 23 1 N ILE B 20 O VAL B 47
SHEET 4 B 7 CYS B 89 HIS B 94 1 O VAL B 92 N VAL B 21
SHEET 5 B 7 PHE B 112 ILE B 118 1 O VAL B 116 N PHE B 91
SHEET 6 B 7 CYS B 209 LYS B 216 1 O HIS B 210 N MET B 117
SHEET 7 B 7 SER B 236 ASP B 244 1 O VAL B 237 N ILE B 211
SITE 1 AC1 7 TYR A 124 PHE A 134 LEU A 142 PHE A 157
SITE 2 AC1 7 PHE A 194 ALA A 219 HIS A 246
SITE 1 AC2 9 TYR B 124 PHE B 134 LEU B 142 PHE B 157
SITE 2 AC2 9 PHE B 194 ALA B 219 HIS B 246 HOH B 675
SITE 3 AC2 9 HOH B 688
CRYST1 50.950 53.200 55.760 90.04 90.04 116.03 P 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 0.019627 0.009585 0.000024 0.00000
SCALE2 0.000000 0.020919 0.000023 0.00000
SCALE3 0.000000 0.000000 0.017934 0.00000
TER 2097 ILE A 268
TER 4200 ILE B 268
MASTER 325 0 2 30 14 0 5 6 4810 2 22 42
END |